TY  - JOUR
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2014
UR  - http://repository.ubn.ru.nl/handle/2066/128385
TI  - How citrullination invaded rheumatoid arthritis research
SN  - 1478-6354
IS  - iss. 1
JF  - Arthritis Research & Therapy
VL  - vol. 16
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/128385/128385.pdf?sequence=1
ER  - 
TY  - MGZN
AU  - Kappel, R.M.
AU  - Venrooij, W.J.W. van
AU  - Tervaert, J.W. Cohen
AU  - Pruijn, G.J.M.
PY  - 2012
UR  - https://hdl.handle.net/2066/103319
TI  - Een alternatief voor siliconen
EP  - 982
SP  - 980
JF  - Medisch Contact
ER  - 
TY  - JOUR
AU  - Venrooij, W.J.W. van
AU  - Beers, J.J.B.C. van
AU  - Pruijn, G.J.M.
PY  - 2011
UR  - https://hdl.handle.net/2066/91562
TI  - Anti-ccp antibodies: The past, the present and the future
EP  - 398
SN  - 1759-4790
IS  - iss. 7
SP  - 391
JF  - Nature Reviews. Rheumatology
VL  - vol. 7
PS  - 8 p.
DO  - http://dx.doi.org/10.1038/nrrheum.2011.76
ER  - 
TY  - JOUR
AU  - Dooren, S.H.J. van
AU  - Raijmakers, R.
AU  - Pluk, H.
AU  - Lokate, A.M.C.
AU  - Koemans, T.S.
AU  - Spanjers, R.E.C.
AU  - Heck, A.J.R.
AU  - Boelens, W.C.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2011
UR  - https://hdl.handle.net/2066/92165
TI  - Oxidative stress-induced modifications of histidyl-trna synthetase affect its trna aminoacylation activity but not its immunoreactivity
EP  - 553
SN  - 0829-8211
IS  - iss. 6
SP  - 545
JF  - Biochemistry and Cell Biology
VL  - vol. 89
PS  - 9 p.
DO  - http://dx.doi.org/10.1139/O11-055
ER  - 
TY  - JOUR
AU  - Dooren, S.H.J. van
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.M.
PY  - 2011
UR  - https://hdl.handle.net/2066/92105
TI  - Myositis-specific autoantibodies: Detection and clinical associations
EP  - 20
SN  - 2038-3274
IS  - iss. 1
SP  - 5
JF  - Autoimmunity Highlights
VL  - vol. 2
PS  - 16 p.
ER  - 
TY  - JOUR
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2009
UR  - https://hdl.handle.net/2066/75459
TI  - De vicieuze cirkel die leidt tot reumatoide artritis
EP  - B232-6
SN  - 0028-2162
SP  - B232-1
JF  - Nederlands Tijdschrift voor Geneeskunde
VL  - vol. 153
PS  - 7 p.
ER  - 
TY  - CHAP
AU  - Beers, J.J.B.C. van
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2009
UR  - https://hdl.handle.net/2066/75663
PB  - Lengerich : Pabst Science Publishers
TI  - Two major classes of rheumatoid arthritis: CCP distinguishes between ACPA-positive and ACPA-negative RA
EP  - 278
SN  - 9783899675795
SP  - 265
CT  - Conrad, K.; Chan, E.K.L.; Fritzler, M.J. (ed.), From Pathogenesis to Therapy of Autoimmune Diseases: Autoantigens, Autoantibodies, Autoimmunity
ER  - 
TY  - JOUR
AU  - Venrooij, W.J.W. van
AU  - Beers, J.J.B.C. van
AU  - Pruijn, G.J.M.
PY  - 2008
UR  - https://hdl.handle.net/2066/72017
TI  - Anti-CCP antibody, a marker for the early detection of rheumatoid arthritis
EP  - 285
SN  - 0077-8923
IS  - iss. 1143
SP  - 268
JF  - Annals of the New York Academy of Sciences
VL  - vol. 2008
PS  - 16 p.
ER  - 
TY  - JOUR
AU  - Venrooij, W.J.W. van
PY  - 2008
UR  - https://hdl.handle.net/2066/72473
TI  - The diagnostic accuracy of anti-citrulline antibody assessment in the diagnosis of patients suspected of rheumatoid arthritis by a general practitioner
EP  - 1244
SN  - 0028-2162
IS  - iss. 21
SP  - 1243
JF  - Nederlands Tijdschrift voor Geneeskunde
VL  - vol. 152
ER  - 
TY  - JOUR
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2008
UR  - https://hdl.handle.net/2066/72622
TI  - An important step towards completing the rheumatoid arthritis cycle
EP  - 120
SN  - 1478-6354
IS  - iss. 5
SP  - 117
JF  - Arthritis Research & Therapy
VL  - vol. 10
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/72622/72622.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Venrooij, W.J.W. van
AU  - Zendman, A.J.W.
PY  - 2008
UR  - https://hdl.handle.net/2066/65997
TI  - Anti-CCP2 antibodies: An overview and perspective of the diagnostic abilities of this serological marker for early rheumatoid arthritis
EP  - 39
SN  - 1080-0549
IS  - iss. 1
SP  - 36
JF  - Clinical Reviews in Allergy and Immunology
VL  - vol. 34
PS  - 4 p.
DO  - https://doi.org/10.1007/s12016-007-8029-y
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/65997/65997.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Welting, T.J.M.
AU  - Mattijssen, S.
AU  - Peters, F.M.
AU  - Doorn, N.L. van
AU  - Dekkers, L.
AU  - Venrooij, W.J.W. van
AU  - Heus, H.A.
AU  - Bonafe, L.
AU  - Pruijn, G.J.M.
PY  - 2008
UR  - https://hdl.handle.net/2066/71925
TI  - Cartilage-hair hypoplasia-associated mutations in the RNase MRP P3 domain affect RNA folding and ribonucleoprotein assembly
EP  - 466
SN  - 0006-3002
IS  - iss. 3
SP  - 455
JF  - Biochimica et Biophysica Acta
VL  - vol. 1783
PS  - 12 p.
ER  - 
TY  - JOUR
AU  - Vannini, A.
AU  - Cheung, K.
AU  - Fusconi, M.
AU  - Stammen-Vogelzangs, J.
AU  - Drenth, J.P.H.
AU  - Dall'aglio, A.C.
AU  - Bianchi, F.B.
AU  - Bakker-Jonges, L.E.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
AU  - Zendman, A.J.W.
PY  - 2007
UR  - https://hdl.handle.net/2066/187121
TI  - Anti-cyclic citrullinated peptide positivity in non-rheumatoid arthritis disease samples: citrulline-dependent or not?
EP  - 516
SN  - 0003-4967
IS  - iss. 4
SP  - 511
JF  - Annals of the Rheumatic Diseases
VL  - vol. 66
ER  - 
TY  - JOUR
AU  - Vannini, A.
AU  - Cheung, K.
AU  - Fusconi, M.
AU  - Stammen-Vogelzangs, J.
AU  - Drenth, J.P.H.
AU  - Dall'aglio, A.C.
AU  - Bianchi, F.B.
AU  - Bakker-Jonges, L.E.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
AU  - Zendman, A.J.W.
PY  - 2007
UR  - https://hdl.handle.net/2066/35130
AB  - BACKGROUND: Antibodies directed against citrullinated proteins (eg anti-cyclic citrullinated peptide (CCP)) have excellent diagnostic and good prognostic potential for rheumatoid arthritis. Type 1 autoimmune hepatitis (AIH-1) is a chronic liver disease characterised by a variety of serum autoantibodies. Recently, in a large group of patients with AIH-1 without clear rheumatoid arthritis overlap, a relatively high percentage (9%) of anti-CCP2 positivity was scored. OBJECTIVES: To characterise the citrulline-dependence of the observed anti-CCP2 positivity in AIH-1 sera as well as in other groups of patients without rheumatoid arthritis (mainly rheumatic diseases). METHODS: Serum samples of 57 patients with AIH-1 and 66 patients without rheumatoid arthritis, most of them reported as anti-CCP positive, were tested for citrulline-specific reactivity with a second generation anti-CCP kit, with the citrullinated and the corresponding non-citrullinated (arginine-containing) antigen. A subset of AIH-1 sera was also tested with a CCP1 ELISA (and arginine control). RESULTS: The anti-CCP2 reactivity of most non-rheumatoid arthritis rheumatic diseases samples (87-93%) was citrulline-specific, whereas a relatively high percentage of AIH-1 samples (42-50%) turned out to be reactive in a citrulline-independent manner. The use of citrullinated and non-citrullinated CCP1 peptides confirmed a high occurrence of citrulline-independent reactivity in AIH-1 samples. CONCLUSIONS: In rheumatoid arthritis and most non-rheumatoid arthritis rheumatologic disease sera, anti-CCP positivity is citrulline-dependent. However in some patients, particularly patients with AIH-1, citrulline-independent reactivity in the anti-CCP2 test can occur. A positive CCP test in a non-rheumatic disease (eg liver disease) should therefore be interpreted with care, and preferably followed by a control ELISA with a non-citrullinated antigen.
TI  - Anti-cyclic citrullinated peptide positivity in non-rheumatoid arthritis disease samples: citrulline-dependent or not?
EP  - 516
SN  - 0003-4967
IS  - iss. 4
SP  - 511
JF  - Annals of the Rheumatic Diseases
VL  - vol. 66
ER  - 
TY  - CHAP
AU  - Beers, J.J.B.C. van
AU  - Zendman, A.J.W.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2007
UR  - https://hdl.handle.net/2066/35034
PB  - Lengerich, Germany : Pabst Science Publishers
TI  - Citrullination in the arthritic synovium; the citrullinome, the antibodies and their connection with RA pathogenesis
EP  - 388
SN  - 389967409X
SP  - 378
CT  - Conrad, K.; Chan, E.K.L.; Fritzler, M.J. (ed.), Autoantigens, autoantibodies, autoimmunity
ER  - 
TY  - JOUR
AU  - Schilders, G.W.
AU  - Raijmakers, R.
AU  - Malmegrim, K.C.
AU  - Walle, L. Vande
AU  - Saelens, X.
AU  - Vree Egberts, W.T.M.
AU  - Venrooij, W.J.W. van
AU  - Vandenabeele, P.
AU  - Pruijn, G.J.M.
PY  - 2007
UR  - https://hdl.handle.net/2066/35021
TI  - Caspase-mediated cleavage of the exosome subunit PM/Scl-75 during apoptosis
EP  - R12-9
SN  - 1478-6354
IS  - iss. 1
SP  - R12
JF  - Arthritis Research & Therapy
VL  - vol. 9
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/35021/35021.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Zendman, A.J.W.
AU  - Raijmakers, R.
AU  - Nijenhuis, S.
AU  - Vossenaar, E.R.
AU  - Tillaart, M. van den
AU  - Chirivi, R.G.S.
AU  - Raats, J.M.H.
AU  - Venrooij, W.J.W. van
AU  - Drijfhout, J.W.
AU  - Pruijn, G.J.M.
PY  - 2007
UR  - https://hdl.handle.net/2066/35240
TI  - ABAP: antibody-based assay for peptidylarginine deiminase activity
EP  - 240
SN  - 0003-2697
IS  - iss. 2
SP  - 232
JF  - Analytical Biochemistry
VL  - vol. 369
DO  - http://dx.doi.org/10.1016/j.ab.2007.07.009
ER  - 
TY  - CHAP
AU  - Hof, D.
AU  - Pruijn, G.J.M.
AU  - Venrooij, W.J.W. van
AU  - Raats, J.M.H.
PY  - 2007
UR  - https://hdl.handle.net/2066/36610
PB  - Hauppauge NY, U.S.A. : Nova Science Publishers
TI  - The role of cell death-specific modifications in breaking tolerance to self-antigens
EP  - 202
SN  - 1600215092
SP  - 179
CT  - Kettleworth, C.R. (ed.), Cell apoptosis research advances
ER  - 
TY  - JOUR
AU  - Welting, T.J.M.
AU  - Peters, F.M.A.
AU  - Hensen, S.M.M.
AU  - Doorn, N.L. van
AU  - Kikkert, B.J.
AU  - Raats, J.M.H.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2007
UR  - https://hdl.handle.net/2066/34671
TI  - Heterodimerization regulates RNase MRP/RNase P association, localization, and expression of Rpp20 and Rpp25
EP  - 75
SN  - 1355-8382
IS  - iss. 1
SP  - 65
JF  - Rna : a Publication of the Rna Society
VL  - vol. 13
DO  - https://doi.org/10.1261/rna.237807
ER  - 
TY  - JOUR
AU  - Welting, T.J.M.
AU  - Mattijssen, S.
AU  - Peters, F.M.
AU  - Doorn, N.L. van
AU  - Dekkers, L.
AU  - Venrooij, W.J.W. van
AU  - Heus, H.A.
AU  - Bonafe, L.
AU  - Pruijn, G.J.M.
PY  - 2007
UR  - https://hdl.handle.net/2066/35020
AB  - Cartilage-hair hypoplasia (CHH) is caused by mutations in the gene encoding the RNA component of RNase MRP. Currently it is unknown how these mutations affect the function of this endoribonuclease. In this study we investigated the effect of mutations in the P3 domain on protein binding and RNA folding. Our data demonstrate that a number of P3 nucleotide substitutions reduced the efficiency of its interaction with Rpp25 and Rpp20, two protein subunits binding as a heterodimer to this domain. The CHH-associated 40G>A substitution, as well as the replacement of residue 47, almost completely abrogated Rpp25 and Rpp20 binding in different assays. Also other CHH-associated P3 mutations reduced the efficiency by which the RNase MRP RNA is bound by Rpp25-Rpp20. These data demonstrate that the most important residues for binding of the Rpp25-Rpp20 dimer reside in the apical stem-loop of the P3 domain. Structural analyses by NMR not only showed that this loop may adopt a pseudo-triloop structure, but also demonstrated that the 40G>A substitution alters the folding of this part of the P3 domain. Our data are the first to provide insight into the molecular mechanism by which CHH-associated mutations affect the function of RNase MRP.
TI  - Cartilage-hair hypoplasia-associated mutations in the RNase MRP P3 domain affect RNA folding and ribonucleoprotein assembly
EP  - 466
SN  - 0006-3002
IS  - iss. 3
SP  - 455
JF  - Biochimica et Biophysica Acta
VL  - vol. 1783
ER  - 
TY  - JOUR
AU  - Raijmakers, R.
AU  - Vogelzangs, J.H.P.
AU  - Raats, J.M.H.
AU  - Panzenbeck, M.
AU  - Corby, M.
AU  - Jiang, H.
AU  - Thibodeau, M.
AU  - Haynes, N.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
AU  - Werneburg, B.
PY  - 2006
UR  - https://hdl.handle.net/2066/35888
TI  - Experimental autoimmune encephalomyelitis induction in peptidylarginine ase 2 knockout mice
EP  - 226
SN  - 0021-9967
IS  - iss. 2
SP  - 217
JF  - Journal of Comparative Neurology
VL  - vol. 498
ER  - 
TY  - JOUR
AU  - Vannini, A.
AU  - Cheung, K.
AU  - Fusconi, M.
AU  - Stammen-Vogelzangs, J.
AU  - Drenth, J.P.H.
AU  - Dall'aglio, A.C.
AU  - Bianchi, F.B.
AU  - Bakker-Jonges, L.E.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
AU  - Zendman, A.J.W.
PY  - 2006
UR  - https://hdl.handle.net/2066/187165
TI  - Anti-CCP2 positivity in non-ra disease samples: citrulline-dependent or not?
SN  - 0003-4967
JF  - Annals of the Rheumatic Diseases
VL  - vol. Sep 2006;
ER  - 
TY  - JOUR
AU  - Bronner, I.M.
AU  - Meulen, M.F. van der
AU  - Visser, M. de
AU  - Kalmijn, S.
AU  - Venrooij, W.J.W. van
AU  - Voskuyl, A.E.
AU  - Dinant, H.J.
AU  - Linssen, W.H.
AU  - Wokke, J.H.J.
AU  - Hogendijk, J.E.
PY  - 2006
UR  - https://hdl.handle.net/2066/35680
TI  - Long-term outcome in polymyositis and dermatomyositis
EP  - 1461
SN  - 0003-4967
IS  - iss. 11
SP  - 1456
JF  - Annals of the Rheumatic Diseases
VL  - vol. 65
DO  - https://doi.org/10.1136/ard.2005.045690
ER  - 
TY  - JOUR
AU  - Zendman, A.J.W.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2006
UR  - https://hdl.handle.net/2066/34914
TI  - Use and significance of anti-CCP autoantibodies in rheumatoid arthritis
EP  - 25
SN  - 1462-0324
IS  - iss. 1
SP  - 20
JF  - Rheumatology
VL  - vol. 45
ER  - 
TY  - JOUR
AU  - Venrooij, W.J.W. van
AU  - Zendman, A.J.W.
AU  - Pruijn, G.J.M.
PY  - 2006
UR  - https://hdl.handle.net/2066/36060
TI  - Autoantibodies to citrullinated antigens in (early) rheumatoid arthritis
EP  - 41
SN  - 1568-9972
IS  - iss. 1
SP  - 37
JF  - Autoimmunity Reviews
VL  - vol. 6
DO  - https://doi.org/10.1016/j.autrev.2006.03.008
ER  - 
TY  - JOUR
AU  - Hengstman, G.J.D.
AU  - Vree Egberts, W.T.M.
AU  - Seelig, H.P.
AU  - Lundberg, I.E.
AU  - Moutsopoulos, H.M.
AU  - Doria, A.
AU  - Mosca, M.
AU  - Vencovsky, J.
AU  - Venrooij, W.J.W. van
AU  - Engelen, B.G.M. van
PY  - 2006
UR  - https://hdl.handle.net/2066/35996
AB  - OBJECTIVES: To assess the clinical implications of autoantibodies directed against different parts of the Mi-2 beta autoantigen in patients with myositis. METHODS: A systematic assessment of the clinical, laboratory, and histological characteristics of 48 anti-Mi-2 positive patients from six European centres was made. Anti-Mi-2 autoantibodies were determined with an ELISA using four overlapping fragments spanning the entire amino acid sequence of the autoantigen. Data were compared with results for a large group of anti-Mi-2 negative patients with myositis published previously. RESULTS: Anti-Mi-2 autoantibodies were found in dermatomyositis, polymyositis, and inclusion body myositis. In general, myositis with anti-Mi-2 autoantibodies was characterised by relatively mild disease, sometimes accompanied by extra-muscular symptoms, including arthralgia, arthritis, Raynaud's phenomenon, and interstitial lung disease. Cardiac disease was not seen, and treatment response was fair. No differences were found between patients with autoantibodies to different fragments of the Mi-2 beta antigen, except for a potentially increased risk of cancer in patients with antibodies directed to the N-terminal fragment of the autoantigen. CONCLUSIONS: Anti-Mi-2 autoantibodies are not a marker of a specific subtype of myositis. No significant differences between patients with autoantibodies to different fragments of the Mi-2 beta autoantigen are found, with the possible exception of an increased risk of cancer in patients with antibodies to the N-terminal fragment.
TI  - Clinical characteristics of patients with myositis and autoantibodies to different fragments of the Mi-2 beta antigen.
EP  - 245
SN  - 0003-4967
IS  - iss. 2
SP  - 242
JF  - Annals of the Rheumatic Diseases
VL  - vol. 65
ER  - 
TY  - JOUR
AU  - Hengstman, G.J.D.
AU  - Laak, H.J. ter
AU  - Vree Egberts, W.T.M.
AU  - Lundberg, I.E.
AU  - Moutsopoulos, H.M.
AU  - Vencovsky, J.
AU  - Doria, A.
AU  - Mosca, M.
AU  - Venrooij, W.J.W. van
AU  - Engelen, B.G.M. van
PY  - 2006
UR  - https://hdl.handle.net/2066/36099
TI  - Anti-signal recognition particle autoantibodies: marker of a necrotising hy
EP  - 1638
SN  - 0003-4967
IS  - iss. 12
SP  - 1635
JF  - Annals of the Rheumatic Diseases
VL  - vol. 65
DO  - https://doi.org/10.1136/ard.2006.052191
ER  - 
TY  - JOUR
AU  - Hengstman, G.J.D.
AU  - Laak, H.J. ter
AU  - Vree Egberts, W.T.M.
AU  - Lundberg, I.E.
AU  - Moutsopoulos, H.M.
AU  - Vencovsky, J.
AU  - Doria, A.
AU  - Mosca, M.
AU  - Venrooij, W.J.W. van
AU  - Engelen, B.G.M. van
PY  - 2006
UR  - https://hdl.handle.net/2066/36100
AB  - OBJECTIVE: To elucidate the clinical importance of the anti-signal recognition particle (SRP) autoantibody in patients with myositis. METHODS: Retrospective systematic assessment of the clinical, laboratory and histological characteristics of 23 anti-SRP-positive patients from six European centres. Data were compared with a large group of anti-SRP-negative patients with myositis published previously. RESULTS: Clinically, patients with anti-SRP autoantibodies often had a severe symmetric proximal muscle weakness resulting in marked disability, dysphagia and highly elevated levels of serum creatine kinase. Three patients had typical dermatomyositis rashes. The disease was associated with the occurrence of extramuscular signs and symptoms including interstitial lung disease. No association was found with an increased risk of cardiac involvement, and the disease carried a reasonably favourable prognosis with most patients responding to treatment. None of the patients had the typical histological features of myositis. Most muscle biopsy specimens showed the presence of necrotic muscle fibres and no inflammatory infiltrates. CONCLUSIONS: Anti-SRP autoantibodies are associated with a syndrome of a necrotising myopathy in the spectrum of immune-mediated myopathies that differs from typical polymyositis. Further studies are needed to elucidate the pathogenesis and to clarify the role of the anti-SRP autoantibodies in this unique disease.
TI  - Anti-signal recognition particle autoantibodies: marker of a necrotising myopathy.
EP  - 1638
SN  - 0003-4967
IS  - iss. 12
SP  - 1635
JF  - Annals of the Rheumatic Diseases
VL  - vol. 65
DO  - https://doi.org/10.1136/ard.2006.052191
ER  - 
TY  - JOUR
AU  - Hengstman, G.J.D.
AU  - Vree Egberts, W.T.M.
AU  - Seelig, H.P.
AU  - Lundberg, I.E.
AU  - Moutsopoulos, H.M.
AU  - Doria, A.
AU  - Mosca, M.
AU  - Vencovsky, J.
AU  - Venrooij, W.J.W. van
AU  - Engelen, B.G.M. van
PY  - 2006
UR  - https://hdl.handle.net/2066/187176
TI  - Clinical characteristics of patients with myositis and autoantibodies to ent fragments of the Mi-2 beta antigen
EP  - 245
SN  - 0003-4967
IS  - iss. 2
SP  - 242
JF  - Annals of the Rheumatic Diseases
VL  - vol. 65
ER  - 
TY  - JOUR
AU  - Welting, T.J.M.
AU  - Kikkert, B.J.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2006
UR  - https://hdl.handle.net/2066/35927
TI  - Differential association of protein subunits with the human RNase MRP and RNase lexes
EP  - 1382
SN  - 1355-8382
IS  - iss. 7
SP  - 1373
JF  - Rna : a Publication of the Rna Society
VL  - vol. 12
DO  - https://doi.org/10.1261/rna.2293906
ER  - 
TY  - GEN
AU  - Venrooij, W.J. van
PY  - 2005
SN  - 9090200053
UR  - https://hdl.handle.net/2066/27000
PB  - Nijmegen : Radboud Universiteit Nijmegen
TI  - RA, RA, wat is dat?
PS  - 23 p.
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/27000/27000.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Raijmakers, R.
AU  - Vogelzangs, J.H.P.
AU  - Croxford, J.L.
AU  - Wesseling, P.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2005
UR  - https://hdl.handle.net/2066/32325
AB  - Immunization of mammals with central nervous system (CNS)-derived proteins or peptides induces experimental autoimmune encephalomyelitis (EAE), a disease resembling the human autoimmune disease multiple sclerosis (MS). Both diseases are accompanied by destruction of a part of the of the myelin sheaths, which surround neurites in the CNS. Previous studies in MS have described alterations in the citrullination of myelin basic protein, one of the main protein constituents of the myelin sheath. Here, we show that, also during the development of EAE in mice, hypercitrullination occurs in the areas of the spinal cord that show the highest degree of inflammation and that myelin basic protein and glial fibrillary acidic protein are among the hypercitrullinated proteins. We conclude that hypercitrullination of myelin proteins in the CNS is a common phenomenon in demyelinating disease. Hypercitrullination may cause conformational changes in proteins, so the affected proteins may be involved in the pathogenesis of CNS autoimmune disease by acting as autoreactive T-cell epitopes. This is the first report in which hypercitrullination of CNS proteins in EAE is described and in which proteins other than myelin basic protein are reported to be citrullinated during autoimmune-mediated CNS inflammation.
TI  - Citrullination of central nervous system proteins during the development of experimental autoimmune encephalomyelitis.
EP  - 253
SN  - 0021-9967
IS  - iss. 3
SP  - 243
JF  - Journal of Comparative Neurology
VL  - vol. 486
DO  - http://dx.doi.org/10.1002/cne.20529
ER  - 
TY  - JOUR
AU  - Pruijn, G.J.M.
AU  - Vossenaar, E.R.
AU  - Drijfhout, J.W.
AU  - Venrooij, W.J.W. van
AU  - Zendman, A.J.W.
PY  - 2005
UR  - https://hdl.handle.net/2066/33294
TI  - Anti-CCP antibody detection facilitates early diagnosis and prognosis of rheumatoid arthritis
EP  - 7
SN  - 1573-3971
IS  - iss. 1
SP  - 1
JF  - Current Rheumatology Reviews
VL  - vol. 1
ER  - 
TY  - JOUR
AU  - Lundberg, K.
AU  - Nijenhuis, S.
AU  - Vossenaar, E.R.
AU  - Palmblad, K.
AU  - Venrooij, W.J.W. van
AU  - Klareskog, L.
AU  - Zendman, A.J.W.
AU  - Harris, H.E.
PY  - 2005
UR  - https://hdl.handle.net/2066/32323
TI  - Citrullinated proteins have increased immunogenicity and arthritogenicity and their presence in arthritic joints correlates with disease severity
EP  - R467
SN  - 1478-6354
IS  - iss. 3
SP  - R458
JF  - Arthritis Research & Therapy
VL  - vol. 7
DO  - http://dx.doi.org/10.1186/ar1697
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/32323/32323.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Raijmakers, R.
AU  - Vogelzangs, J.H.P.
AU  - Croxford, J.L.
AU  - Wesseling, P.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2005
UR  - https://hdl.handle.net/2066/32324
TI  - Citrullination of central nervous system proteins during the development of experimental autoimmune encephalomyelitis
EP  - 253
SN  - 0021-9967
IS  - iss. 3
SP  - 243
JF  - Journal of Comparative Neurology
VL  - vol. 486
DO  - http://dx.doi.org/10.1002/cne.20529
ER  - 
TY  - JOUR
AU  - Huebner, W.
AU  - Kidd, B.A.
AU  - Tomooka, B.H.
AU  - Lee, B.J.
AU  - Bruce, B.
AU  - Fries, J.F.
AU  - Sonderstrup, G.
AU  - Monach, P.
AU  - Drijfhout, J.W.
AU  - Venrooij, W.J.W. van
AU  - Utz, P.J.
AU  - Genovese, M.C.
AU  - W.H., R.
PY  - 2005
UR  - https://hdl.handle.net/2066/33295
TI  - Antigen microarrays profiling of autoantibodies in rheumatoid arthritis
EP  - 2655
SN  - 0004-3591
IS  - iss. 9
SP  - 2645
JF  - Arthritis and Rheumatism
VL  - vol. 52
DO  - https://doi.org/10.1002/art.21269
ER  - 
TY  - CHAP
AU  - Zendman, A.J.W.
AU  - Vossenaar, E.R.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2005
UR  - https://hdl.handle.net/2066/58637
PB  - Lengerich : Pabst Science Publishers
TI  - Anti-CCP antibodies a specific and early marker for rheumatoid arthritis
EP  - 329
SP  - 320
CT  - Conrad, K.; Sack, U. (ed.), Autoimmunity, Autoantigens, Autoantibodies
ER  - 
TY  - JOUR
AU  - Hengstman, G.J.D.
AU  - Brenk, L. van
AU  - Vree Egberts, W.T.M.
AU  - Kooi, E.L. van der
AU  - Borm, G.F.
AU  - Padberg, G.W.A.M.
AU  - Venrooij, W.J.W. van
AU  - Engelen, B.G.M. van
PY  - 2005
UR  - https://hdl.handle.net/2066/32585
AB  - Myositis specific autoantibodies (MSAs) are proven to be specific for myositis compared with other inflammatory connective tissue diseases. Their specificity compared, however, with other neuromuscular disorders, which are included in the differential diagnosis of patients in whom the diagnosis myositis is under consideration, is unknown. We prospectively screened sera from 107 patients with various neuromuscular disorders for the most common MSAs and compared the results with the findings in a group of 97 myositis patients, published previously. Special attention was paid to patients with facioscapulohumeral muscular dystrophy (FSHD), an autosomal dominant muscle disease with marked inflammation in skeletal muscle tissue.Only one patient in the neuromuscular disorders group tested positive for an MSA, compared with 41 in the myositis group, resulting in a specificity of 99%. None of the FSHD patients tested positive. We conclude that the tested MSAs are highly specific for myositis and that they are not merely associated with muscle inflammation.
TI  - High specificity of myositis specific autoantibodies for myositis compared with other neuromuscular disorders.
EP  - 537
SN  - 0340-5354
IS  - iss. 5
SP  - 534
JF  - Journal of Neurology
VL  - vol. 252
DO  - https://doi.org/10.1007/s00415-005-0683-5
ER  - 
TY  - JOUR
AU  - Hengstman, G.J.D.
AU  - Van Brenk, L.
AU  - Vree Egberts, W.T.M.
AU  - Kooi, E.L. van der
AU  - Borm, G.F.
AU  - Padberg, G.W.A.M.
AU  - Venrooij, W.J.W. van
AU  - Engelen, B.G.M. van
PY  - 2005
UR  - https://hdl.handle.net/2066/32584
TI  - High specificity of myositis specific autoantibodies for myositis compared with other neuromuscular disorders
EP  - 537
SN  - 0340-5354
IS  - iss. 5
SP  - 534
JF  - Journal of Neurology
VL  - vol. 252
DO  - https://doi.org/10.1007/s00415-005-0683-5
ER  - 
TY  - JOUR
AU  - Hof, D.
AU  - Cheung, K.
AU  - Rooij, D.J.R.A.M. de
AU  - Hoogen, F.H.J. van den
AU  - Pruijn, G.J.M.
AU  - Venrooij, W.J.W. van
AU  - Raats, J.M.H.
PY  - 2005
UR  - https://hdl.handle.net/2066/164896
TI  - Autoantibodies specific for apoptotic U1-70K are superior serological markers for mixed connective tissue disease
EP  - R309
SN  - 1478-6354
IS  - iss. 2
SP  - R302
JF  - Arthritis Research & Therapy
VL  - vol. 7
DO  - https://doi.org/10.1186/ar1490
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/164896/164896.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Hof, D.
AU  - Cheung, K.
AU  - Rooij, D.J.R.A.M. de
AU  - Hoogen, F.H.J. van den
AU  - Pruijn, G.J.M.
AU  - Venrooij, W.J.W. van
AU  - Raats, J.M.H.
PY  - 2005
UR  - https://hdl.handle.net/2066/33255
AB  - Modifications occurring on autoantigens during cell death have been proposed to have a role in the initiation of autoimmune diseases. Patients suffering from mixed connective tissue disease (MCTD) produce autoantibodies directed to U1 small nuclear ribonucleoprotein (snRNP), and antibodies against a 70 kDa protein component, the U1-70K (70K) protein, are the most prominent. During apoptosis, 70K is cleaved by caspase-3 to a 40 kDa product, which remains associated with the complex. Autoantibodies preferentially recognizing the apoptotic form of 70K have been described previously, and an apoptosis-specific epitope on 70K has been identified. This study shows that 29 of 53 (54%) MCTD sera preferentially recognize the apoptotic form of 70K over intact 70K. Moreover, we show that antibodies directed to an apoptosis-specific epitope on 70K are more specifically associated with MCTD than other anti-70K antibodies, suggesting that apoptotic 70K is a better antigen for the detection of these antibodies in MCTD patients. Longitudinal analysis of 12 MCTD patients showed in several patients that early sera are relatively enriched with antibodies recognizing an apoptosis-specific epitope, and that the levels of these apoptosis-specific antibodies decrease in time. These findings indicate that the early detection of apoptotic 70K is of considerable interest for anti-U1 snRNP-positive patients.
TI  - Autoantibodies specific for apoptotic U1-70K are superior serological markers for mixed connective tissue disease.
EP  - 9
SN  - 1478-6354
IS  - iss. 2
SP  - R302
JF  - Arthritis Research & Therapy
VL  - vol. 7
DO  - https://doi.org/10.1186/ar1490
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/33255/33255.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Vossenaar, E.R.
AU  - Zendman, A.J.W.
AU  - Raijmakers, R.
AU  - Weiting, T.J.
AU  - Heijden, A.G. van der
AU  - Horstman, W.A.M.
AU  - Cheung, K.
AU  - Vogelzangs, J.H.P.
AU  - Nijenhuis, S.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2004
UR  - https://hdl.handle.net/2066/58471
TI  - Features of the citrullinating peptidylarginine deiminase enzymes
EP  - S6
SN  - 1478-6354
IS  - iss. suppl. 1
SP  - S5
JF  - Arthritis Research & Therapy
VL  - vol. 6
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/58471/58471.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Lundberg, K.
AU  - Nijenhuis, S.
AU  - Vossenaar, E.R.
AU  - Klareskog, L.
AU  - Venrooij, W.J.W. van
AU  - Harris, H.E.
PY  - 2004
UR  - https://hdl.handle.net/2066/60098
TI  - Citrullinated proteins in arthritis: presence in joints and effects on immunogenicity
EP  - S7
SN  - 1478-6354
SP  - S7
JF  - Arthritis Research & Therapy
VL  - vol. 6
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/60098/60098.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Vossenaar, E.R.
AU  - Despres, N.
AU  - Lapointe, E.
AU  - Heijden, A.G. van der
AU  - Lora, M.
AU  - Senshu, T.
AU  - Venrooij, W.J.W. van
AU  - Menard, H.A.
PY  - 2004
UR  - https://hdl.handle.net/2066/58941
AB  - Antibodies directed to the Sa antigen are highly specific for rheumatoid arthritis ( RA) and can be detected in approximately 40% of RA sera. The antigen, a doublet of protein bands of about 50 kDa, is present in placenta and in RA synovial tissue. Although it has been stated that the Sa antigen is citrullinated vimentin, experimental proof for this claim has never been published. In this study, we investigated the precise nature of the antigen. Peptide sequences that were obtained from highly purified Sa antigen were unique to vimentin. Recombinant vimentin, however, was not recognized by anti-Sa reference sera. In vivo, vimentin is subjected to various post-translational modifications, including citrullination. Since antibodies to citrullinated proteins are known to be highly specific for RA, we investigated whether Sa is citrullinated and found that Sa indeed is citrullinated vimentin. Anti-Sa antibodies thus belong to the family of anticitrullinated protein/peptide antibodies. The presence of the Sa antigen in RA synovial tissue, and the recent observation that vimentin is citrullinated in dying human macrophages, make citrullinated vimentin an interesting candidate autoantigen in RA and may provide new insights into the potential role of citrullinated synovial antigens and the antibodies directed to them in the pathophysiology of RA.
TI  - Rheumatoid arthritis specific anti-Sa antibodies target citrullinated vimentin
EP  - R150
SN  - 1478-6354
IS  - iss. 2
SP  - R142
JF  - Arthritis Research & Therapy
VL  - vol. 6
DO  - http://dx.doi.org/10.1186/ar1149
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/58941/58941.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Raijmakers, R.
AU  - Renz, M.
AU  - Wiemann, C
AU  - Egberts, W.V.
AU  - Seelig, H.P.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2004
UR  - https://hdl.handle.net/2066/59043
AB  - OBJECTIVE: To compare the autoantigenicity of the recently described N-terminally elongated PM-Scl-75 protein with that of PM-Scl-100 and the originally defined PM-Scl-75 polypeptide, and to determine its value for analyzing sera from patients with the polymyositis (PM)/scleroderma overlap syndrome. METHODS: Serum samples obtained from patients with the PM/scleroderma overlap syndrome and from patients with several other diseases were analyzed for the presence of autoantibodies reactive with recombinant PM-Scl-100 and PM-Scl-75 (both the original and the longer form) proteins, in an enzyme-linked immunosorbent assay (ELISA). RESULTS: Autoantibodies recognizing the longer PM-Scl-75 protein isoform were detected in 28% of the patients with PM/scleroderma. This percentage is slightly higher than that for PM-Scl-100 (25%) and is significantly higher than that for the previously defined PM-Scl-75 protein (11%). In addition, we identified a significant number of patients who had anti-PM-Scl-75 but not anti-PM-Scl-100 antibodies. This finding contrasts with what has been previously reported for the shorter version of the PM-Scl-75 protein. CONCLUSION: Our data indicate that use of the long PM-Scl-75 isoform in addition to PM-Scl-100 in ELISAs significantly increases the number of patients in whom anti-PM-Scl autoantibodies can be detected.
TI  - PM-Scl-75 is the main autoantigen in patients with the polymyositis/scleroderma overlap syndrome.
EP  - 569
SN  - 0004-3591
IS  - iss. 2
SP  - 565
JF  - Arthritis and Rheumatism
VL  - vol. 50
DO  - http://dx.doi.org/10.1002/art.20056
ER  - 
TY  - JOUR
AU  - Vossenaar, E.R.
AU  - Radstake, T.R.D.J.
AU  - Heijden, A.G. van der
AU  - Mansum, M.A. van
AU  - Dieteren, C.E.J.
AU  - Rooij, D.J.R.A.M. de
AU  - Barrera Rico, P.
AU  - Zendman, A.J.W.
AU  - Venrooij, W.J.W. van
PY  - 2004
UR  - https://hdl.handle.net/2066/58497
AB  - BACKGROUND: Antibodies directed to proteins containing the non-standard amino acid citrulline, are extremely specific for rheumatoid arthritis (RA). Peptidylcitrulline can be generated by post-translational conversion of arginine residues. This process, citrullination, is catalysed by a group of calcium dependent peptidylarginine deiminase (PAD) enzymes. OBJECTIVE: To investigate the expression and activity of four isotypes of PAD in peripheral blood and synovial fluid cells of patients with RA. RESULTS: The data presented here show that citrullination of proteins by PAD enzymes is a process regulated at three levels: transcription-in peripheral blood PAD2 and PAD4 mRNAs are expressed predominantly in monocytes; PAD4 mRNA is not detectable in macrophages, translation-translation of PAD2 mRNA is subject to differentiation stage-specific regulation by its 3' UTR, and activation-the PAD proteins are only activated when sufficient Ca(2+) is available. Such high Ca(2+) concentrations are normally not present in living cells. In macrophages, which are abundant in the inflamed RA synovium, vimentin is specifically citrullinated after Ca(2+) influx. CONCLUSION: PAD2 and PAD4 are the most likely candidate PAD isotypes for the citrullination of synovial proteins in RA. Our results indicate that citrullinated vimentin is a candidate autoantigen in RA.
TI  - Expression and activity of citrullinating peptidylarginine deiminase enzymes in monocytes and macrophages.
EP  - 381
SN  - 0003-4967
IS  - iss. 4
SP  - 373
JF  - Annals of the Rheumatic Diseases
VL  - vol. 63
ER  - 
TY  - JOUR
AU  - Vossenaar, E.R.
AU  - Depres, N.
AU  - Lora, M.
AU  - Heijden, A.G. van der
AU  - Lapointe, E.
AU  - Zendman, A.J.W.
AU  - Senshu, T.
AU  - Venrooij, W.J.W. van
AU  - Menard, H.A.
PY  - 2004
UR  - https://hdl.handle.net/2066/57944
TI  - The rheumatoid arthritis specific Sa antigen is citrullinated vimentin
EP  - S8
SN  - 1478-6354
IS  - iss. suppl. 1
SP  - S8
JF  - Arthritis Research & Therapy
VL  - vol. 6
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/57944/57944.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Vossenaar, E.R.
AU  - Smeets, TJ
AU  - Kraan, M.C.
AU  - Raats, J.M.H.
AU  - Venrooij, W.J.W. van
AU  - Tak, P.P.
PY  - 2004
UR  - https://hdl.handle.net/2066/57135
AB  - OBJECTIVE: Antibodies directed toward citrullinated proteins (e.g., anti-cyclic citrullinated peptide antibodies) are highly specific for rheumatoid arthritis (RA) and are produced locally at the site of inflammation. Although the presence of citrullinated proteins in rheumatoid synovium has been described in the literature, it is uncertain whether their presence is specific for RA. The present study was undertaken to investigate this. METHODS: The local production of the anti-citrullinated protein antibodies was investigated by comparing the concentration of the antibodies (corrected for the total amount of IgG present) in paired samples of serum and synovial fluid from RA patients. The presence of citrullinated proteins in the synovial tissue was investigated by immunohistochemical analysis of synovial tissue from RA patients and from patients with other arthropathies, using a variety of specific antibodies to citrullinated proteins. RESULTS: In RA patients, anti-citrullinated protein antibodies constituted a 1.4-fold higher proportion of IgG in synovial fluid compared with serum, which is indicative of a local production of the antibodies. Immunohistochemical staining of citrullinated proteins was observed in the lining layer, the sublining layer, and in extravascular fibrin deposits in inflamed synovial tissue from RA as well as non-RA patients. CONCLUSION: The presence of citrullinated proteins in the inflamed synovium is not specific for RA, but rather, it may be an inflammation-associated phenomenon. The high specificity of the anti-citrullinated protein antibodies is, therefore, most likely the result of an abnormal humoral response to these proteins.
TI  - The presence of citrullinated proteins is not specific for rheumatoid synovial tissue.
EP  - 3494
SN  - 0004-3591
IS  - iss. 11
SP  - 3485
JF  - Arthritis and Rheumatism
VL  - vol. 50
DO  - http://dx.doi.org/10.1002/art.20584
ER  - 
TY  - JOUR
AU  - Fouraux, M.A.
AU  - Deneka, M.
AU  - Ivan, V.
AU  - Heijden, A.G. van der
AU  - Raymackers, J
AU  - Suylekom, D van
AU  - Venrooij, W.J.W. van
AU  - Sluijs, P. van der
AU  - Pruijn, G.J.M.
PY  - 2004
UR  - https://hdl.handle.net/2066/57913
AB  - We describe the characterization of an 80-kDa protein cross-reacting with a monoclonal antibody against the human La autoantigen. The 80-kDa protein is a variant of rabip4 with an N-terminal extension of 108 amino acids and is expressed in the same cells. For this reason, we named it rabip4'. rabip4' is a peripheral membrane protein, which colocalized with internalized transferrin and EEA1 on early endosomes. Membrane association required the presence of the FYVE domain and was perturbed by the phosphatidylinositol 3-kinase inhibitor wortmannin. Expression of a dominant negative rabip4' mutant reduced internalization and recycling of transferrin from early endosomes, suggesting that it may be functionally linked to rab4 and rab5. In agreement with this, we found that rabip4' colocalized with the two GTPases on early endosomes and bound specifically and simultaneously to the GTP form of both rab4 and rab5. We conclude that rabip4' may coordinate the activities of rab4 and rab5, regulating membrane dynamics in the early endosomal system.
TI  - Rabip4' is an effector of rab5 and rab4 and regulates transport through early endosomes.
EP  - 624
SN  - 1059-1524
IS  - iss. 2
SP  - 611
JF  - Molecular Biology of the Cell
VL  - vol. 15
DO  - https://doi.org/10.1091/mbc.E03-05-0343
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/57913/57913.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Granneman, S.
AU  - Vogelzangs, J.H.P.
AU  - Luhrmann, R
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
AU  - Watkins, N.J.
PY  - 2004
UR  - https://hdl.handle.net/2066/59313
AB  - In the nucleolus the U3 snoRNA is recruited to the 80S pre-rRNA processing complex in the dense fibrillar component (DFC). The U3 snoRNA is found throughout the nucleolus and has been proposed to move with the preribosomes to the granular component (GC). In contrast, the localization of other RNAs, such as the U8 snoRNA, is restricted to the DFC. Here we show that the incorporation of the U3 snoRNA into the 80S processing complex is not dependent on pre-rRNA base pairing sequences but requires the B/C motif, a U3-specific protein-binding element. We also show that the binding of Mpp10 to the 80S U3 complex is dependent on sequences within the U3 snoRNA that base pair with the pre-rRNA adjacent to the initial cleavage site. Furthermore, mutations that inhibit 80S complex formation and/or the association of Mpp10 result in retention of the U3 snoRNA in the DFC. From this we propose that the GC localization of the U3 snoRNA is a direct result of its active involvement in the initial steps of ribosome biogenesis.
TI  - Role of pre-rRNA base pairing and 80S complex formation in subnucleolar localization of the U3 snoRNP.
EP  - 8610
SN  - 0270-7306
IS  - iss. 19
SP  - 8600
JF  - Molecular and Cellular Biology
VL  - vol. 24
DO  - https://doi.org/10.1128/MCB.24.19.8600-8610.2004
ER  - 
TY  - JOUR
AU  - Gaalen, F.A. van
AU  - Aken, J.B. van
AU  - Huizinga, T.W.J.
AU  - Schreuder, G.M.T.
AU  - Breedveld, F.C.
AU  - Zanelli, E.
AU  - Venrooij, W.J.W. van
AU  - Verweij, C.L.
AU  - Toes, R.E.
AU  - Vries, R.R.P. de
PY  - 2004
UR  - https://hdl.handle.net/2066/58480
AB  - Objective. The functional role of HLA class II molecules in the pathogenesis of rheumatoid arthritis (RA) is unclear. HLA class II molecules are involved in the interaction between T and B lymphocytes required for long-lived B cell responses and generation of high-affinity IgG antibodies. We undertook this study to investigate the relationship between HLA class II gene polymorphisms and RA-specific IgG antibodies against cyclic citrullinated peptides (anti-CCP antibodies). Methods. High-resolution HLA-DR and DQ typing and anti-CCP-2 antibody testing were performed on 268 RA patients from the Early Arthritis Clinic cohort at the Department of Rheumatology of the Leiden University Medical Center. The presence of anti-CCP antibodies was analyzed in carriers of the different DR and DQ alleles. Disease progression was measured over a period of 4 years by scoring radiographs of the hands and feet using the Sharp/van der Heijde method. Results. Carriership of the individual alleles HLA-DRBt*0401, DRB1*1001, DQB1*0302, and DQBI*0501 was associated with the presence of antiCCP antibodies. Carriers of DQ-DR genotypes containing proposed RA susceptibility alleles were significantly more often anti-CCP antibody positive. Carriership of one or two HLA-DRB1 shared epitope (SE) alleles was significantly associated with production of anti-CCP antibodies (odds ratio [OR] 3.3, 95% confidence interval [95% CI] 1.8-6.0 and OR 13.3, 95% CI 4.6-40.4, respectively). An increased rate of joint destruction was observed in SE+, anti-CCP+ patients (mean Sharp score 7.6 points per year) compared with that in SE-, anti-CCP+ patients (2.4 points per year) (P = 0.04), SE+, anti-CCP- patients (1.6 points per year) (P < 0.001), and SE-, anti-CCP- patients (1.6 points per year) (11 < 0.001). Conclusion. HLA class II RA susceptibility alleles are associated with production of anti-CCP antibodies. Moreover, more severe disease progression is found in RA patients with both anti-CCP antibodies and SE alleles.
TI  - Association between HLA class II genes and autoantibodies to cyclic citrullinated peptides (CCPs) influences the severity of rheumatoid arthritis
EP  - 2121
SN  - 0004-3591
IS  - iss. 7
SP  - 2113
JF  - Arthritis and Rheumatism
VL  - vol. 50
DO  - https://doi.org/10.1002/art.20316
ER  - 
TY  - JOUR
AU  - Wiik, A.S.
AU  - Gordon, T.P.
AU  - Kavanaugh, A.
AU  - Lahita, R.G.
AU  - Reeves, W.
AU  - Venrooij, W.J.W. van
AU  - Wilson, M.R.
AU  - Fritzler, M.
PY  - 2004
UR  - https://hdl.handle.net/2066/57247
TI  - Cutting edge diagnostics in rheumatology: The role of patients, clinicians, and laboratory scientists in optimizing the use of autoimmune serology
EP  - 298
SN  - 0004-3591
IS  - iss. 2
SP  - 291
JF  - Arthritis and Rheumatism
VL  - vol. 51
DO  - https://doi.org/10.1002/art.20229
ER  - 
TY  - PAT
AU  - Drijfhout, J.W.
AU  - Rutjes, F.P.J.T.
AU  - Blaauw, R.H.
AU  - Pruijn, G.J.M.
AU  - Venrooij, W.J.W. van
AU  - Raats, J.M.H.
PY  - 2004
UR  - https://hdl.handle.net/2066/59200
PB  - [S.l. : s.n.]
TI  - Peptidylarginine deiminase (PAD) inhibitors
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/59200/59200.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Venrooij, W.J.W. van
AU  - Zendman, A.J.W.
AU  - Nijenhuis, S.
AU  - Vossenaar, E.R.
AU  - Wiik, A.W.
AU  - Pruijn, G.J.M.
PY  - 2004
UR  - https://hdl.handle.net/2066/58174
TI  - Antibodies to cyclic citrullinated peptides (anti-CCP) are specific for the diagnosis and prognosis of (early) rheumatoid arthritis
EP  - 7
IS  - iss. 2
SP  - 3
VL  - vol. 11
ER  - 
TY  - CHAP
AU  - Vasishta, A.
AU  - Venrooij, W.J.W. van
PY  - 2004
UR  - https://hdl.handle.net/2066/60170
PB  - Oxford : Clinical Publishing
TI  - Anti-CCP2: a marker with a high diagnostic potential for the detection of (early) rheumatoid arthritis
EP  - 97
SP  - 85
CT  - Madhok, R.;  Capell, H. (ed.), The year in Rheumatic disorders
ER  - 
TY  - CHAP
AU  - Raijmakers, R.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2004
UR  - https://hdl.handle.net/2066/58288
PB  - Lengerich : Pabst Science Publishers
TI  - Autoimmunity and post-translational modifications in multiple sclerosis
EP  - 298
SP  - 290
CT  - Conrad, K.; Sack, U. (ed.), Autoimmunity, Autoantigens, Autoantibodies
ER  - 
TY  - JOUR
AU  - Zandbelt, M.
AU  - Vogelzangs, J.H.P.
AU  - Putte, L.B.A. van de
AU  - Venrooij, W.J.W. van
AU  - Hoogen, F.H.J. van den
PY  - 2004
UR  - https://hdl.handle.net/2066/58157
TI  - Anti-alpha-fodrin antibodies do not add much to the diagnosis of Sjogren's syndrome.
EP  - 8
SN  - 1478-6354
IS  - iss. 1
SP  - R33
JF  - Arthritis Research & Therapy
VL  - vol. 6
DO  - https://doi.org/10.1186/ar1021
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/58157/58157.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Hengstman, G.J.D.
AU  - Engelen, B.G.M. van
AU  - Venrooij, W.J.W. van
PY  - 2004
UR  - https://hdl.handle.net/2066/58714
AB  - PURPOSE OF REVIEW: Defined autoantibodies are found in about half of the patients with myositis. Traditionally, these autoantibodies have been divided into myositis specific autoantibodies (MSAs) and myositis associated autoantibodies. Several studies have shown that MSAs are associated with specific clinical characteristics and can aid our understanding of the pathophysiology of myositis. RECENT FINDINGS: Recent studies suggest that some MSAs are markers of specific inflammatory muscle diseases (e.g., anti-SRP for an immune-mediated necrotizing myopathy) and not just of myositis in general. Furthermore, new insights are emerging about the pathophysiology of MSAs, in particular anti-Jo-1. Based on these new insights, an alternative hypothesis of the formation of anti-Jo-1 autoantibodies is presented in which the immune system itself rather than muscle is the site of antigen presentation. SUMMARY: The recognition that some MSAs are markers of specific disease entities that were once commonly referred to as (poly)myositis, aids the development of better disease definitions. The changing insights in the function of the Jo-1 antigen and the emergence of new hypotheses on the formation of the Jo-1 antibody, open new avenues for future research aimed at unraveling the mystery of myositis.
TI  - Myositis specific autoantibodies: changing insights in pathophysiology and clinical associations.
EP  - 699
SN  - 1040-8711
IS  - iss. 6
SP  - 692
JF  - Current Opinion in Rheumatology
VL  - vol. 16
ER  - 
TY  - JOUR
AU  - Venrooij, W.J.W. van
AU  - Vossenaar, E.R.
AU  - Zendman, A.J.W.
PY  - 2004
UR  - https://hdl.handle.net/2066/60169
TI  - Anti-CCP antibodies: the new rheumatoid factor in the serology of rheumatoid arthritis.
EP  - 9
SN  - 1568-9972
IS  - iss. suppl 1
SP  - S17
JF  - Autoimmunity Reviews
VL  - vol. 3 Suppl 1
ER  - 
TY  - JOUR
AU  - Venrooij, W.J.W. van
AU  - Vossenaar, E.R.
PY  - 2004
UR  - https://hdl.handle.net/2066/60174
TI  - Anti-CCP abs in the management and pathogenesis of RA
EP  - 14
SN  - 1373-1580
SP  - 12
JF  - Clinical Laboratory International
VL  - vol. 28
ER  - 
TY  - JOUR
AU  - Vossenaar, E.R.
AU  - Venrooij, W.J.W. van
PY  - 2004
UR  - https://hdl.handle.net/2066/60093
AB  - Antibodies directed to citrullinated proteins (e.g. anti-CCP [cyclic citrullinated peptide] antibodies) are highly specific for rheumatoid arthritis (RA). These antibodies are produced at the site of inflammation in RA, and therefore citrullinated antigens are also expected to be present in the inflamed synovium. We discuss literature showing that the presence of citrullinated proteins in the synovium is not specific for RA. The RA-specific antibodies are therefore most likely the result of an abnormal immune response that specifically occurs in RA patients. It was recently shown that presence of anti-CCP antibodies precedes the onset of clinical symptoms of RA by years. It thus appears that it may take years for initial events that cause the generation of anti-CCP antibodies to develop into full-blown disease.
TI  - Citrullinated proteins: sparks that may ignite the fire in rheumatoid arthritis
EP  - 111
SN  - 1478-6354
IS  - iss. 3
SP  - 107
JF  - Arthritis Research & Therapy
VL  - vol. 6
DO  - https://doi.org/10.1186/ar1184
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/60093/60093.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Vossenaar, E.R.
AU  - Zendman, A.J.W.
AU  - Venrooij, W.J.W. van
PY  - 2004
UR  - https://hdl.handle.net/2066/60094
TI  - Citrullination, a possible functional link between susceptibility genes and rheumatoid arthritis
EP  - 5
SN  - 1478-6354
IS  - iss. part 1
SP  - 1
JF  - Arthritis Research & Therapy
VL  - vol. 6
DO  - https://doi.org/10.1186/ar1027
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/60094/60094.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Venrooij, W.J.W. van
AU  - Vossenaar, E.R.
AU  - Zendman, A.J.W.
PY  - 2004
UR  - https://hdl.handle.net/2066/60113
TI  - CCP2: a specific and sensitive test for the detection of (early) rheumatoid arthritis
EP  - 67
SN  - 1344-3372
SP  - 57
JF  - Autoantibodies and Autoimmunity
VL  - vol. 11
ER  - 
TY  - JOUR
AU  - Zendman, A.J.W.
AU  - Vossenaar, E.R.
AU  - Venrooij, W.J.W. van
PY  - 2004
UR  - https://hdl.handle.net/2066/60138
TI  - Autoantibodies to citrullinated (poly)peptides: a key diagnostic and prognostic marker for rheumatoid arthritis.
EP  - 299
SN  - 0891-6934
IS  - iss. 4
SP  - 295
JF  - Autoimmunity
VL  - vol. 37
DO  - https://doi.org/10.1080/08916930410001708733
ER  - 
TY  - JOUR
AU  - Nijenhuis, S.
AU  - Zendman, A.J.W.
AU  - Vossenaar, E.R.
AU  - Pruijn, G.J.M.
AU  - Venrooij, W.J.W. van
PY  - 2004
UR  - https://hdl.handle.net/2066/58385
AB  - Rheumatoid arthritis (RA) is a common, systemic autoimmune disease of which the exact etiology is not known. In the past 10 years, substantial progress has been made in the identification of the antigens specifically recognized by the autoantibodies of RA patients. A central factor in this respect is citrullination, a form of post-translational modification that is strongly associated with autoimmunity in RA. Here, we summarize and discuss our current knowledge on (i) autoantibody systems in RA, (ii) the occurrence of peptidylarginine deiminases and (iii) citrullinated proteins in natural and diseased environments, and (iv) genetic factors involved in RA that may influence the generation and presentation of citrullinated proteins and the resulting antibody production against these modified proteins. Citrullination of proteins may play a key role in the initiation and/or the progression of RA. The onset of citrulline-specific autoimmunity in RA is probably mediated by both environmental and genetic factors, and future studies will learn whether therapeutic intervention at the level of citrullination may provide new possibilities to treat RA.
TI  - Autoantibodies to citrullinated proteins in rheumatoid arthritis: clinical performance and biochemical aspects of an RA-specific marker.
EP  - 34
SN  - 0009-8981
IS  - iss. 1-2
SP  - 17
JF  - Clinica Chimica Acta
VL  - vol. 350
DO  - https://doi.org/10.1016/j.cccn.2004.07.016
ER  - 
TY  - JOUR
AU  - Berglin, E.
AU  - Padyukov, L.
AU  - Sundin, U.
AU  - Hallmans, G.
AU  - Stenlund, H.
AU  - Venrooij, W.J.W. van
AU  - Klareskog, L.
AU  - Dahlqvist, S.R.
PY  - 2004
UR  - https://hdl.handle.net/2066/57325
AB  - Antibodies against cyclic citrullinated peptide (CCP) and rheumatoid factors (RFs) have been demonstrated to predate the onset of rheumatoid arthritis ( RA) by years. A nested case control study was performed within the Northern Sweden Health and Disease study cohort to analyse the presence of shared epitope ( SE) genes, defined as HLA-DRB1* 0404 or DRB1* 0401, and of anti-CCP antibodies and RFs in individuals who subsequently developed RA. Patients with RA were identified from among blood donors whose samples had been collected years before the onset of symptoms. Controls matched for age, sex, and date of sampling were selected randomly from the same cohort. The SE genes were identified by polymerase chain reaction sequence-specific primers. Anti-CCP2 antibodies and RFs were determined using enzyme immunoassays. Fifty-nine individuals with RA were identified as blood donors, with a median antedating time of 2.0 years interquartile range 0.9 - 3.9 years) before presenting with symptoms of RA. The sensitivity for SE as a diagnostic indicator for RA was 60% and the specificity was 64%. The corresponding figures for anti-CCP antibodies were 37% and 98%, and for RFs, 17 - 42% and 94%, respectively. In a logistic regression analysis, SE ( odds ratio [OR] = 2.35), anti-CCP antibodies ( OR = 15.9), and IgA-RF ( OR = 6.8) significantly predicted RA. In a combination model analysis, anti-CCP antibodies combined with SE had the highest OR (66.8, 95% confidence interval 8.3 - 539.4) in predicting RA, compared with anti-CCP antibodies without SE ( OR = 25.01, 95% confidence interval 2.8 - 222.2) or SE without anti-CCP antibodies ( OR = 1.9, 95% confidence interval 0.9 - 4.2). This study showed that the presence of anti-CCP antibodies together with SE gene carriage is associated with a very high relative risk for future development of RA.
TI  - A combination of autoantibodies to cyclic citrullinated peptide (CCP) and HLA-DRB1 locus antigens is strongly associated with future onset of rheumatoid arthritis
EP  - R308
SN  - 1478-6354
IS  - iss. 4
SP  - R303
JF  - Arthritis Research & Therapy
VL  - vol. 6
DO  - https://doi.org/10.1186/ar1187
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/57325/57325.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Gaalen, F.A. van
AU  - Linn-Rasker, S.P.
AU  - Venrooij, W.J.W. van
AU  - Jong, B.A. de
AU  - Breedveld, F.C.
AU  - Verweij, C.L.
AU  - Toes, R.E.
AU  - Huizinga, T.W.J.
PY  - 2004
UR  - https://hdl.handle.net/2066/58352
AB  - Objective. Rheumatoid arthritis (RA) is a common, severe, chronic inflammatory joint disease. Since the disease may initially be indistinguishable from other forms of arthritis, early diagnosis can be difficult. Autoantibodies seen in RA can be detected years before clinical symptoms develop. In an inception cohort of patients with recent-onset arthritis, we undertook this study to assess the predictive value of RA-specific autoantibodies to cyclic citrullinated peptides (CCPs) in patients with undifferentiated arthritis (UA). Methods. Anti-CCP2 antibody tests were performed at baseline in 936 consecutive, newly referred patients with recent-onset arthritis. Patients who could not be properly classified 2 weeks after inclusion were categorized as having UA. Patients with UA were followed up for 3 years and evaluated for progression of their disease to RA as defined by the American College of Rheumatology (ACR) 1987 revised criteria. Results. Three hundred eighteen of 936 patients with recent-onset arthritis were classified as having UA and were available for analysis. After 3 years of followup, 127 of 318 UA patients (40%) had been classified as having RA. RA had developed in 63 of 249 patients (25%) with a negative anti-CCP test and in 64 of 69 patients (93%) with a positive anti-CCP test (odds ratio 37.8 [95% confidence interval 13.8-111.9]). Multivariate analysis of the presence of anti-CCP antibodies and parameters from the ACR criteria identified polyarthritis, symmetric arthritis, erosions on radiographs, and anti-CCP antibodies As significant predictors of RA. Conclusion. Testing for anti-CCP antibodies in UA allows accurate prediction of a substantial number of patients who will fulfill the ACR criteria for RA.
TI  - Autoantibodies to cyclic citrullinated peptides predict progression to rheumatoid arthritis in patients with undifferentiated arthritis - A prospective cohort study
EP  - 715
SN  - 0004-3591
IS  - iss. 3
SP  - 709
JF  - Arthritis and Rheumatism
VL  - vol. 50
DO  - https://doi.org/10.1002/art.20044
ER  - 
TY  - JOUR
AU  - Vossenaar, E.R.
AU  - Boekel, M.A.M. van
AU  - Venrooij, W.J.W. van
AU  - Lopez-Hoyoz, M.
AU  - Merino, J.
AU  - Merino, R.
AU  - Joosten, L.A.B.
PY  - 2004
UR  - https://hdl.handle.net/2066/57611
TI  - Absence of citrulline-specific autoantibodies in animal models of autoimmunity.
EP  - 2372
SN  - 0004-3591
IS  - iss. 7
SP  - 2370
JF  - Arthritis and Rheumatism
VL  - vol. 50
DO  - https://doi.org/10.1002/art.20296
ER  - 
TY  - JOUR
AU  - Welting, T.J.M.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2004
UR  - https://hdl.handle.net/2066/58699
AB  - The eukaryotic ribonuclease for mitochondrial RNA processing (RNase MRP) is mainly located in the nucleoli and belongs to the small nucleolar ribonucleoprotein (snoRNP) particles. RNase MRP is involved in the processing of pre-rRNA and the generation of RNA primers for mitochondrial DNA replication. A closely related snoRNP, which shares protein subunits with RNase MRP and contains a structurally related RNA subunit, is the pre-tRNA processing factor RNase P. Up to now, 10 protein subunits of these complexes have been described, designated hPop1, hPop4, hPop5, Rpp14, Rpp20, Rpp21, Rpp25, Rpp30, Rpp38 and Rpp40. To get more insight into the assembly of the human RNase MRP complex we studied protein-protein and protein-RNA interactions by means of GST pull-down experiments. A total of 19 direct protein-protein and six direct protein-RNA interactions were observed. The analysis of mutant RNase MRP RNAs showed that distinct regions are involved in the direct interaction with protein subunits. The results provide insight into the way the protein and RNA subunits assemble into a ribonucleoprotein particle. Based upon these data a new model for the architecture of the human RNase MRP complex was generated.
TI  - Mutual interactions between subunits of the human RNase MRP ribonucleoprotein complex.
EP  - 2146
SN  - 0305-1048
IS  - iss. 7
SP  - 2138
JF  - Nucleic Acids Research
VL  - vol. 32
DO  - https://doi.org/10.1093/nar/gkh539
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/58699/58699.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Venrooij, W.J.W. van
AU  - Putte, L.B.A. van de
AU  - Hoogen, F.H.J. van den
PY  - 2003
UR  - https://hdl.handle.net/2066/138788
TI  - Anti-cyclic citrullinated peptide antibody in early rheumatoid arthritis:comment on the editorial by Scott.
EP  - 858
SN  - 0004-3591
IS  - iss. 3
SP  - 857
JF  - Arthritis and Rheumatism
VL  - vol. 48
ER  - 
TY  - JOUR
AU  - Hengstman, G.J.D.
AU  - Venrooij, W.J.W. van
AU  - Hoogen, F.H.J. van den
AU  - Engelen, B.G.M. van
PY  - 2003
UR  - https://hdl.handle.net/2066/138795
AB  - In three women, aged 60, 45 and 38 years, who presented with exertional dyspnoea (due to lung fibrosis) and Raynaud's phenomenon, dermatomyopathy and Raynaud's phenomenon, and symmetrical arthralgia and myalgia, respectively, the anti-synthetase syndrome was diagnosed. The anti-synthetase syndrome consists of myositis, idiopathic interstitial lung disease, polyarthritis and Raynaud's phenomenon. The syndrome is characterised by the presence of autoantibodies directed against aminoacyl-tRNA synthetases. A thorough knowledge of this syndrome is required to anticipate manifestations of the disease, which can sometimes be masked and are not always part of the treating physician's field of specialty. The patients were treated with immunosuppressive therapy (azathioprine, prednisone, methotrexate) and recovered considerably.
TI  - [The anti-synthetase syndrome: muscle disease and multisystem disorder at the same time]
EP  - 1489
SN  - 0028-2162
IS  - iss. 31
SP  - 1485
JF  - Nederlands Tijdschrift voor Geneeskunde
VL  - vol. 147
ER  - 
TY  - JOUR
AU  - Granneman, S.
AU  - Gallagher, J.E.
AU  - Vogelzangs, J.H.P.
AU  - Horstman, W.A.M.
AU  - Venrooij, W.J.W. van
AU  - Baserga, S.J.
AU  - Pruijn, G.J.M.
PY  - 2003
UR  - https://hdl.handle.net/2066/185193
AB  - Ribosome biogenesis requires a vast number of trans-acting factors many of which are required for the chemical modification and processing of the pre-rRNA component. The U3 snoRNP complex is required for the early cleavage steps in pre-rRNA processing. We have cloned cDNAs encoding the human and mouse homologs of the yeast U3 snoRNP-associated proteins Imp3 and Imp4. Both human proteins localize to nucleoli and interact with the U3 snoRNA. The results of complementation experiments show that, in contrast to mouse Imp4, mouse Imp3 can partially alleviate the growth defect of the corresponding yeast null strain, indicating that the role of Imp3 in pre-rRNA processing is evolutionarily conserved. The results of density gradient centrifugation experiments show that, in contrast to hU3-55K, the human Imp3 and Imp4 proteins predominantly interact with the U3 snoRNA in 60-80S ribonucleoprotein complexes. In addition, we have found that hImp3, hImp4 and hMpp10 can form a stable hetero-trimeric complex in vitro, which is generated by direct interactions of both hImp3 and hImp4 with hMpp10. The analysis of hImp3 and hImp4 mutants indicated that their binding to hMpp10 correlates with their nucleolar accumulation, strongly suggesting that the formation of the ternary complex of hImp3, hImp4 and hMpp10 is required for their association with nucleolar components.
TI  - The human Imp3 and Imp4 proteins form a ternary complex with hMpp10, which only interacts with the U3 snoRNA in 60-80S ribonucleoprotein complexes.
EP  - 1887
SN  - 0305-1048
IS  - iss. 7
SP  - 1877
JF  - Nucleic Acids Research
VL  - vol. 31
DO  - http://dx.doi.org/10.1093/nar/gkg300
ER  - 
TY  - JOUR
AU  - Raats, J.M.H.
AU  - Roeffen, W.F.G.
AU  - Litjens, S.
AU  - Bulduk, I.
AU  - Mans, G.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2003
UR  - https://hdl.handle.net/2066/186332
AB  - Using the recombinant La (SS-B) protein or a phosphorylated peptide derived thereof 27 La-specific human recombinant autoantibodies were selected from anti-La-positive systemic lupus erythematosus and systemic sclerosis patient-derived combinatorial phage display antibody libraries. Binding of these anti-La antibodies to various isoforms of the La protein present in normal and apoptotic cell extracts was analysed by Western blotting. Twenty-four of the selected antibodies recognize most, if not all isoforms of La, whereas three are exclusively reactive with the protein phosphorylated at serine-366. Sequence analysis of the selected antibodies showed a restricted spectrum of diversity in their VH germline gene usage. Remarkably, the recombinant antibodies recognizing exclusively the phosphoserine-366-containing isoform of La displayed a spleckled nucleoplasmic staining pattern in immunofluorescence analysis of HeLa and HEp-2 cells. This pattern differed markedly from those obtained with anti-La antibodies recognizing all isoforms of the La protein. Colocalization experiments with marker antibodies for spliceosomal UsnRNPs and RNA polymerase III subunits revealed that the anti-phosphorylated La antibodies stain the same nucleoplasmic speckles as anti-UsnRNP antibodies. In contrast to anti-UsnRNP antibodies the anti-phosphorylated La antibodies did not stain the Cajal bodies. In addition, no colocalization of phosphorylated La with RNA polymerase III was observed. Potential functional implications of the accumulation of phosphorylated La in nucleoplasmic speckles are discussed.
TI  - Human recombinant anti-La (SS-B) autoantibodies demonstrate the accumulation of phosphoserine-366-containing la isoforms in nucleoplasmic speckles.
EP  - 141
SN  - 0171-9335
IS  - iss. 3
SP  - 131
JF  - European Journal of Cell Biology
VL  - vol. 82
ER  - 
TY  - JOUR
AU  - Vossenaar, E.R.
AU  - Nijenhuis, S.
AU  - Helsen, M.M.A.
AU  - Heijden, A.G. van der
AU  - Senshu, T.
AU  - Berg, W.B. van den
AU  - Venrooij, W.J.W. van
AU  - Joosten, L.A.B.
PY  - 2003
UR  - https://hdl.handle.net/2066/134329
AB  - OBJECTIVE: Antibodies directed to citrulline-containing proteins are highly specific for rheumatoid arthritis (RA) and can be detected in up to 80% of patients with RA. Citrulline is a nonstandard amino acid that can be incorporated into proteins only by posttranslational modification of arginine by peptidylarginine deiminase (PAD) enzymes. The objective of this study was to investigate the presence of anticitrulline antibodies, PAD enzymes, and citrullinated antigens in mouse models of both acute and chronic destructive arthritis: streptococcal cell wall (SCW)-induced arthritis and collagen-induced arthritis (CIA), respectively. METHODS: Synovial tissue biopsy specimens were obtained from naive mice, mice with CIA, and mice with SCW-induced arthritis. The expression of messenger RNA (mRNA) for PAD enzymes was analyzed by reverse transcriptase-polymerase chain reaction; the presence of PAD proteins and their products (citrullinated proteins) was analyzed by Western blotting and by immunolocalization. The presence of anticitrullinated protein antibodies was investigated by an anti-cyclic citrullinated peptide (anti-CCP) enzyme-linked immunosorbent assay (ELISA) and an ELISA using in vitro citrullinated fibrinogen. RESULTS: In both mouse models, PAD type 2 (PAD2) mRNA was present in the synovium but was not translated into PAD2 protein. In contrast, PAD4 mRNA, although absent from healthy synovium, was readily transcribed and translated by polymorphonuclear neutrophils infiltrating the synovial tissue during inflammation. As a consequence, several synovial proteins were subjected to citrullination. One of these proteins was identified as fibrin, which has been reported to be citrullinated also in synovium of patients with RA. Although generation of citrullinated antigens during synovial inflammation in the mice was eminent, no anti-CCP antibodies could be detected. CONCLUSION: Citrullination of synovial antigens is an active process during joint inflammation in both mice and humans, but the induction of autoantibodies directed to these proteins is a more specific phenomenon, detectable only in human RA patients.
TI  - Citrullination of synovial proteins in murine models of rheumatoid arthritis.
EP  - 2500
SN  - 0004-3591
IS  - iss. 9
SP  - 2489
JF  - Arthritis and Rheumatism
VL  - vol. 48
DO  - http://dx.doi.org/10.1002/art.11229
ER  - 
TY  - JOUR
AU  - Malmegrim de Farias, K.C.
AU  - Saelens, X.
AU  - Pruijn, G.J.M.
AU  - Vandenabeele, P.
AU  - Venrooij, W.J.W. van
PY  - 2003
UR  - https://hdl.handle.net/2066/187507
AB  - Recent studies have implicated the dying cell as a potential reservoir of modified autoantigens that might initiate and drive systemic autoimmunity in susceptible hosts. The spliceosomal Sm proteins are recognized by the so-called anti-Sm autoantibodies, an antibody population found exclusively in patients suffering from systemic lupus erythematosus. We have studied the effects of apoptosis on the Sm proteins and demonstrate that one of the Sm proteins, the Sm-F protein, is proteolytically cleaved in apoptotic cells. Cleavage of the Sm-F protein generates a 9-kDa apoptotic fragment, which remains associated with the U snRNP complexes in apoptotic cells. Sm-F cleavage is dependent on caspase activation and the cleavage site has been located near the C-terminus, EEED(81) downward arrow G. Use of different caspase inhibitors suggests that besides caspase-8 other caspases are implicated in Sm-F cleavage. A C-terminally truncated mutant of the Sm-F protein, representing the modified form of the protein, is capable of forming an Sm E-F-G complex in vitro that is recognized by many anti-Sm patient sera.
TI  - Caspase-mediated cleavage of the U snRNP-associated Sm-F protein during apoptosis.
EP  - 579
SN  - 1350-9047
IS  - iss. 5
SP  - 570
JF  - Cell Death and Differentiation
VL  - vol. 10
DO  - https://doi.org/10.1038/sj.cdd.4401196
ER  - 
TY  - JOUR
AU  - Raats, J.M.H.
AU  - Wijnen, E.M.
AU  - Pruijn, G.J.M.
AU  - Hoogen, F.H.J. van den
AU  - Venrooij, W.J.W. van
PY  - 2003
UR  - https://hdl.handle.net/2066/138793
AB  - OBJECTIVE: To isolate and characterize monoclonal autoantibodies (Mab) directed to citrullinated antigens from patients with rheumatoid arthritis (RA). METHODS: Using lymphocytes from bone marrow or peripheral blood from RA patients, we constructed antibody fragment libraries representing the antibody repertoire of these individuals. Antibody fragments recognizing a citrulline-containing peptide were selected from these patient libraries. Individual antibody clones were analyzed for germline gene usage and reactivity toward citrullinated (auto)-antigens. RESULTS: Sequence analysis of the cDNA encoding the 21 distinct antibody fragments that were obtained revealed a restricted germline gene usage. Individual antibody clones were positive in both antiperinuclear factor (APF) and antikeratin antibody (AKA) tests, stained citrullinated filaggrin and fibrinogen on Western blots, and reacted with subsets of citrulline-containing peptides in ELISA, but not with noncitrullinated peptides. CONCLUSION: Our report describes the first recombinant human Mab fragments reactive with citrulline-containing peptides. The restricted germline gene usage of these antibodies, and the fact that the VH alleles used are not present in all individuals, may indicate the existence of a genetic predisposition for the development of anticitrulline antibodies in individuals with these germline alleles. The selected antibody clones may facilitate studies on the role of these autoantibodies and their target antigens in the development of RA.
TI  - Recombinant human monoclonal autoantibodies specific for citrulline-containing peptides from phage display libraries derived from patients with rheumatoid arthritis.
EP  - 1711
SN  - 0315-162X
IS  - iss. 8
SP  - 1696
JF  - The Journal of Rheumatology
VL  - vol. 30
ER  - 
TY  - JOUR
AU  - Raijmakers, R.
AU  - Egberts, W.V.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2003
UR  - https://hdl.handle.net/2066/186428
AB  - The exosome is a complex of 3' --> 5' exoribonucleases that functions in a variety of cellular processes, all concerning the processing or degradation of RNA. Paradoxically, the previously described cDNA for the human autoantigenic exosome subunit PM/Scl-75 (Alderuccio, F., Chan, E. K., and Tan, E. M. (1991) J. Exp. Med. 173, 941-952) encodes a polypeptide that failed to interact with the exosome complex. Here, we describe the cloning of a more complete cDNA for PM/Scl-75 encoding 84 additional amino acids at its N terminus. We show that only the longer polypeptide is able to associate with the exosome complex. This interaction is most likely mediated by protein-protein interactions with two other exosome subunits, hRrp46p and hRrp41p, one of which was confirmed in a mammalian two-hybrid system. In addition we show that the putative nuclear localization signal present in the C-terminal region of PM/Scl-75 is sufficient, although not essential for nuclear localization of the protein. Moreover, the deletion of this element abrogated the nucleolar accumulation of PM/Scl-75, although its association with the exosome was not disturbed. This suggests that this basic element of PM/Scl-75 plays a role in targeting the exosome to the nucleolus.
TI  - The association of the human PM/Scl-75 autoantigen with the exosome is dependent on a newly identified N terminus.
EP  - 30704
SN  - 1083-351X
IS  - iss. 33
SP  - 30698
JF  - Journal of Biological Chemistry
VL  - vol. 278
DO  - https://doi.org/10.1074/jbc.M302488200
ER  - 
TY  - JOUR
AU  - Eenennaam, H. van
AU  - Vogelzangs, J.H.P.
AU  - Lugtenberg, T.M.
AU  - Hoogen, F.H.J. van den
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2002
UR  - https://hdl.handle.net/2066/138797
AB  - OBJECTIVE: To characterize the molecular identity of the Th/To autoantigen, which is targeted by autoantibodies in scleroderma and which is associated with the human RNase MRP and RNase P ribonucleoprotein complexes. METHODS: Proteins immunoprecipitated by anti-Th/To+ patient antisera from biotinylated total HeLa cell extracts were analyzed by immunoblotting. The association of autoantigenic proteins with the RNase MRP complex was analyzed by reconstitution experiments and ultraviolet crosslinking. The reactivity of patient sera with all known RNase MRP/RNase P proteins was analyzed by immunoprecipitation of the individual recombinant proteins. RESULTS: The previously defined Th40 autoantigen appeared to be identical to the Rpp38 protein. Paradoxically, Rpp38 did not bind to the P3 domain of the RNase MRP RNA, as suggested by previously published data for Th40, and only half of the anti-Th/To+ sera contained anti-Rpp38 reactivity. Two other RNase MRP/RNase P subunits, Rpp20 and Rpp25, were found to interact with the P3 domain. The previously reported 40-kd species associated with this domain appeared to consist of Rpp20 and/or Rpp25 associated with a nuclease-resistant RNA fragment. Finally, we demonstrated that almost all tested anti-Th/To+ patient sera contained autoantibodies to Rpp25 and hPop1, indicating that these proteins harbor the most frequently targeted Th/To determinants. CONCLUSION: Our data unequivocally define the identity of the Th/To autoantigen and demonstrate that Th/To autoepitopes are found on several protein subunits of RNase MRP/RNase P.
TI  - Identity of the RNase MRP- and RNase P-associated Th/To autoantigen.
EP  - 3272
SN  - 0004-3591
IS  - iss. 12
SP  - 3266
JF  - Arthritis and Rheumatism
VL  - vol. 46
DO  - http://dx.doi.org/10.1002/art.10673
ER  - 
TY  - JOUR
AU  - Raijmakers, R.
AU  - Egberts, W.V.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2002
UR  - https://hdl.handle.net/2066/186665
AB  - The exosome is a complex of 3'--&gt;5' exoribonucleases, which functions in a variety of cellular processes, all requiring the processing or degradation of RNA. Here we present a model for the assembly of the six human RNase PH-like exosome subunits into a hexameric ring structure. In part, this structure is on the basis of the evolutionarily related bacterial degradosome, the core of which consists of three copies of the PNPase protein, each containing two RNase PH domains. In our model three additional exosome subunits, which contain S1 RNA-binding domains, are positioned on the outer surface of this ring. Evidence for this model was obtained by the identification of protein-protein interactions between individual exosome subunits in a mammalian two-hybrid system. In addition, the results of co-immunoprecipitation assays indicate that at least two copies of hRrp4p and hRrp41p are associated with a single exosome, suggesting that at least two of these ring structures are present in this complex. Finally, the identification of a human gene encoding the putative human counterpart of the bacterial PNPase protein is described, which suggests that the exosome is not the eukaryotic equivalent of the bacterial degradosome, although they do share similar functional activities.
TI  - Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring.
EP  - 663
SN  - 0022-2836
IS  - iss. 4
SP  - 653
JF  - Journal of Molecular Biology
VL  - vol. 323
DO  - http://dx.doi.org/10.1016/S0022-2836(02)00947-6
ER  - 
TY  - JOUR
AU  - Malmegrim de Farias, K.C.
AU  - Pruijn, G.J.M.
AU  - Venrooij, W.J.W. van
PY  - 2002
UR  - https://hdl.handle.net/2066/187317
AB  - Recent studies have implicated the dying cell as a potential reservoir of modified autoantigens that may initiate and drive systemic autoimmunity in susceptible hosts. The uridine-rich small nuclear ribonucleoprotein complex is a common target for autoantibodies present in the serum of patients with systemic lupus erythematosus and SLE-overlap syndromes. Four modifications occurring in this complex during apoptosis have been described to date: the caspase-mediated cleavage of the U1-70K protein, the U1 RNA and the Sm-F protein, and the association with hyperphosphorylated SR proteins. In addition, the U1 snRNP complex has been shown to translocate from its normal subcellular localization to apoptotic bodies near the surface of cells undergoing apoptosis. This redistribution might facilitate exposure of the modified components of the U1 snRNP complex to the immune system when the clearance of apoptotic cell remnants is somehow disturbed. The modifications in the U1 snRNP components during apoptosis might represent the initial epitopes to which an immune response is generated and may be the trigger for the production of autoantibodies to this complex in patients with SLE or SLE-overlap syndromes. Therefore, it can be hypothesized that the exposure of elevated levels of apoptotically modified U1 snRNP to the immune system of a genetically susceptible individual might lead to the breaking of immunologic tolerance towards the U1 snRNP complex.
TI  - The fate of the U1 snRNP autoantigen during apoptosis: implications for systemic autoimmunity.
EP  - 712
SN  - 1565-1088
IS  - iss. 9
SP  - 706
JF  - Imaj
VL  - vol. 4
ER  - 
TY  - JOUR
AU  - Robinson, W.H.
AU  - DiGennaro, C.
AU  - Hueber, W.
AU  - Haab, B.B.
AU  - Kamachi, M.
AU  - Dean, E.J.
AU  - Fournel, S.
AU  - Fong, D.
AU  - Genovese, M.C.
AU  - Vegvar, H.E. de
AU  - Skriner, K.
AU  - Hirschberg, D.L.
AU  - Morris, R.I.
AU  - Muller, S.
AU  - Pruijn, G.J.M.
AU  - Venrooij, W.J.W. van
AU  - Smolen, J.S.
AU  - Brown, P.
AU  - Steinman, L.
AU  - Utz, P.J.
PY  - 2002
UR  - https://hdl.handle.net/2066/176280
AB  - We constructed miniaturized autoantigen arrays to perform large-scale multiplex characterization of autoantibody responses directed against structurally diverse autoantigens, using submicroliter quantities of clinical samples. Autoantigen microarrays were produced by attaching hundreds of proteins, peptides and other biomolecules to the surface of derivatized glass slides using a robotic arrayer. Arrays were incubated with patient serum, and spectrally resolvable fluorescent labels were used to detect autoantibody binding to specific autoantigens on the array. We describe and characterize arrays containing the major autoantigens in eight distinct human autoimmune diseases, including systemic lupus erythematosus and rheumatoid arthritis. This represents the first report of application of such technology to multiple human disease sera, and will enable validated detection of antibodies recognizing autoantigens including proteins, peptides, enzyme complexes, ribonucleoprotein complexes, DNA and post-translationally modified antigens. Autoantigen microarrays represent a powerful tool to study the specificity and pathogenesis of autoantibody responses, and to identify and define relevant autoantigens in human autoimmune diseases.
TI  - Autoantigen microarrays for multiplex characterization of autoantibody responses.
EP  - 301
SN  - 1078-8956
IS  - iss. 3
SP  - 295
JF  - Nature Medicine
VL  - vol. 8
DO  - https://doi.org/10.1038/nm0302-295
ER  - 
TY  - JOUR
AU  - Eenennaam, H. van
AU  - Vogelzangs, J.H.P.
AU  - Bisschops, L.L.A.
AU  - Boome, L.C. te
AU  - Seelig, H.P.
AU  - Renz, M.
AU  - Brouwer, R.
AU  - Pluk, W.L.L.P.
AU  - Hoogen, F.H.J. van den
AU  - Rooij, D.J.R.A.M. de
AU  - Pruijn, G.J.M.
AU  - Venrooij, W.J.W. van
PY  - 2002
UR  - https://hdl.handle.net/2066/138796
AB  - Sera from patients suffering from systemic autoimmune diseases such as systemic lupus erythematosus (SLE) and systemic sclerosis (SSc) have been shown to contain reactivities to nuclear components. Autoantibodies specifically targeting nucleolar antigens are found most frequently in patients suffering from SSc or SSc overlap syndromes. We determined the prevalence and clinical significance of autoantibodies directed to nucleolar RNA-protein complexes, the so-called small nucleolar ribonucleoprotein complexes (snoRNPs). A total of 172 patient sera with antinucleolar antibodies were analysed by immunoprecipitation. From 100 of these patients clinical information was obtained by chart review. Autoantibodies directed to snoRNPs were detected not only in patients suffering from SSc and primary Raynaud's phenomenon (RP), but also in patients suffering from SLE, rheumatoid arthritis (RA) and myositis (PM/DM). Antibodies against box C/D small snoRNPs can be subdivided in antifibrillarin positive and antifibrillarin negative reactivity. Antifibrillarin-positive patient sera were associated with a poor prognosis in comparison with antifibrillarin negative (reactivity with U3 or U8 snoRNP only) patient sera. Anti-Th/To autoantibodies were associated with SSc, primary RP and SLE and were found predominantly in patients suffering from decreased co-diffusion and oesophagus motility and xerophthalmia. For the first time autoantibodies that recognize box H/ACA snoRNPs are described, identifying this class of snoRNPs as a novel autoantigenic activity. Taken together, our data show that antinucleolar patient sera directed to small nucleolar ribonucleoprotein complexes are found frequently in other diseases than SSc and that categorization of diagnoses and clinical manifestations based on autoantibody profiles seems particularly informative in patient sera recognizing box C/D snoRNPs.
TI  - Autoantibodies against small nucleolar ribonucleoprotein complexes and their clinical associations.
EP  - 540
SN  - 0009-9104
IS  - iss. 3
SP  - 532
JF  - Clinical and Experimental Immunology
VL  - vol. 130
DO  - https://doi.org/10.1046/j.1365-2249.2002.01991.x
ER  - 
TY  - JOUR
AU  - Fouraux, M.A.
AU  - Bouvet, P.
AU  - Verkaart, S.A.J.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2002
UR  - https://hdl.handle.net/2066/121576
AB  - Ro RNPs are evolutionarily conserved, small cytoplasmic RNA-protein complexes with an unknown function. In human cells, Ro RNPs consist of one of the four hY RNAs and two core proteins: Ro60 and La. Recently, the association of hnRNP I and hnRNP K with particles containing hY1 and hY3 RNAs has been described. The association of three other proteins, namely calreticulin, Ro52 and RoBPI, with (subsets of) the Ro RNPs is still controversial. To gain more insight into the composition and function of the Ro RNPs, we have immunopurified these particles from HeLa cell extracts using monoclonal antibodies against Ro60 and La. Using this approach, we have identified the RNA-binding protein nucleolin as a novel subunit of Ro RNP particles containing hY1 or hY3 RNA, but not hY4 and hY5 RNA. Using an in vitro hY RNA-binding assay we established that the internal pyrimidine-rich loop of hY1 and hY3 RNA is essential for the association of nucleolin. The binding is critically dependent on the presence of all four RNP motifs of nucleolin, but not of the C-terminal RGG-box. Moreover, we demonstrate that, in contrast to nucleolin and hnRNP K, nucleolin and hnRNP I can bind simultaneously to the internal pyrimidine-rich loop of hY1 RNA. We postulate that nucleolin functions in the biogenesis and/or trafficking of hY1 and hY3 RNPs through the nucleolus and subsequent transport to the cytoplasm.
TI  - Nucleolin associates with a subset of the human Ro ribonucleoprotein complexes.
EP  - 488
SN  - 0022-2836
IS  - iss. 3
SP  - 475
JF  - Journal of Molecular Biology
VL  - vol. 320
DO  - https://doi.org/10.1016/S0022-2836(02)00518-1
ER  - 
TY  - JOUR
AU  - Brouwer, R.
AU  - Vree Egberts, W.T.M.
AU  - Hengstman, G.J.D.
AU  - Raijmakers, R.
AU  - Engelen, B.G.M. van
AU  - Seelig, H.P.
AU  - Renz, M.
AU  - Mierau, R.
AU  - Genth, E.
AU  - Pruijn, G.J.M.
AU  - Venrooij, W.J.W. van
PY  - 2002
UR  - https://hdl.handle.net/2066/186494
AB  - The autoantigenic polymyositis/scleroderma (PM/Scl) complex was recently shown to be the human homologue of the yeast exosome, which is an RNA-processing complex. Our aim was to assess whether, in addition to targeting the known autoantigens PM/Scl-100 and PM/Scl-75, autoantibodies also target recently identified components of the PM/Scl complex. The prevalence of autoantibodies directed to six novel human exosome components (hRrp4p, hRrp40p, hRrp41p, hRrp42p, hRrp46p, hCsl4p) was determined in sera from patients with idiopathic inflammatory myopathy (n = 48), scleroderma (n = 11), or the PM/Scl overlap syndrome (n = 10). The sera were analyzed by enzyme-linked immunosorbent assays and western blotting using the affinity-purified recombinant proteins. Our results show that each human exosome component is recognized by autoantibodies. The hRrp4p and hRrp42p components were most frequently targeted. The presence of autoantibodies directed to the novel components of the human exosome was correlated with the presence of the anti-PM/Scl-100 autoantibody in the sera of patients with idiopathic inflammatory myopathy (IIM), as was previously found for the anti-PM/Scl-75 autoantibody. Other clear associations between autoantibody activities were not found. These results further support the conception that the autoimmune response may initially be directed to PM/Scl-100, whereas intermolecular epitope spreading may have caused the autoantibody response directed to the associated components.
TI  - Autoantibodies directed to novel components of the PM/Scl complex, the human exosome.
EP  - 138
SN  - 1478-6354
IS  - iss. 2
SP  - 134
JF  - Arthritis Research & Therapy
VL  - vol. 4
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/186494/186494.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Granneman, S.
AU  - Pruijn, G.J.M.
AU  - Horstman, W.A.M.
AU  - Venrooij, W.J.W. van
AU  - Luhrmann, R
AU  - Watkins, N.J.
PY  - 2002
UR  - https://hdl.handle.net/2066/185501
AB  - The 15.5K protein directly binds to the 5' stem-loop of the U4 small nuclear RNA, the small nucleolar (sno) RNA box C/D motif, and the U3 snoRNA-specific box B/C motif. The box B/C motif has also been shown to be essential for the association of the U3 small nucleolar ribonucleoprotein-specific protein hU3-55K. We therefore set out to determine how 15.5K and hU3-55K recognize the box B/C motif. By using an in vitro assembly assay, we show that hU3-55K effectively binds a sub-fragment of the U3 snoRNA surrounding the B/C motif that we have named the U3BC RNA. The association of hU3-55K with the U3BC RNA is dependent on the binding of 15.5K to the box B/C motif. The association of hU3-55K with the U3BC RNA was found to be also dependent on a conserved RNA structure that flanks the box B/C motif. Furthermore, we show that hU3-55K, a WD 40 repeat containing protein, directly cross-links to the U3BC RNA. Our data support a new structural model of the box B/C region of the U3 snoRNA in which the box B/C motif is base-paired to form a structure highly similar to that of both the U4 5' stem-loop and the box C/D motif.
TI  - The hU3-55K protein requires 15.5K binding to the box B/C motif as well as flanking RNA elements for its association with the U3 small nucleolar RNA in Vitro.
EP  - 48500
SN  - 1083-351X
IS  - iss. 50
SP  - 48490
JF  - Journal of Biological Chemistry
VL  - vol. 277
DO  - https://doi.org/10.1074/jbc.M206631200
ER  - 
TY  - JOUR
AU  - Hengstman, G.J.D.
AU  - Brouwer, R.
AU  - Vree Egberts, W.T.M.
AU  - Seelig, H.P.
AU  - Jongen, P.J.H.
AU  - Venrooij, W.J.W. van
AU  - Engelen, B.G.M. van
PY  - 2002
UR  - https://hdl.handle.net/2066/186508
AB  - The idiopathic inflammatory myopathies (IIM) are a heterogeneous group of systemic diseases that include the familiar disease entities of dermatomyositis (DM), polymyositis (PM), and inclusion body myositis (IBM). A subset of patients has unique autoantibodies which are specific for IIM (myositis specific autoantibodies; MSAs). We studied the clinical and serological characteristics of IIM in 125 Dutch patients. Sera were analysed by immunoblotting, enzyme-linked immunosorbent assay, and immunoprecipitation. The most frequently encountered MSA was the anti-Jo-1 autoantibody (20%), followed by anti-tRNAHis (6%), anti-Mi-2 (6%), and anti-SRP (4%). The presence of certain MSAs was clearly associated with specific clinical characteristics. Anti-Jo-1 and anti-tRNAHis were associated with the anti-synthetase syndrome, anti-SRP with PM with severe myalgia and arthralgia and a moderate response to immunosuppressive treatment. A novel finding was the presence of anti-Mi-2, not only in DM, but also in PM. MSAs were frequently present in DM/PM sera, but were hardly ever detected in the sera of IBM patients. The few IBM patients with MSAs demonstrated a significant response to immunosuppressive treatment. It can be concluded that MSAs define specific clinical syndromes within the spectrum of IIM and that they can assist in the differential diagnosis and treatment plan of these enigmatic disorders by virtually excluding IBM by their presence, and by potentially identifying a subgroup of steroid-responsive IBM patients.
TI  - Clinical and serological characteristics of 125 Dutch myositis patients. Myositis specific autoantibodies aid in the differential diagnosis of the idiopathic inflammatory myopathies.
EP  - 75
SN  - 0340-5354
IS  - iss. 1
SP  - 69
JF  - Journal of Neurology
VL  - vol. 249
DO  - https://doi.org/10.1007/PL00007850
ER  - 
TY  - JOUR
AU  - Eenennaam, H. van
AU  - Heijden, A.G. van der
AU  - Janssen, R.J.T.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2001
UR  - https://hdl.handle.net/2066/143784
AB  - The RNase MRP and RNase P ribonucleoprotein particles both function as endoribonucleases, have a similar RNA component, and share several protein subunits. RNase MRP has been implicated in pre-rRNA processing and mitochondrial DNA replication, whereas RNase P functions in pre-tRNA processing. Both RNase MRP and RNase P accumulate in the nucleolus of eukaryotic cells. In this report we show that for three protein subunits of the RNase MRP complex (hPop1, hPop4, and Rpp38) basic domains are responsible for their nucleolar accumulation and that they are able to accumulate in the nucleolus independently of their association with the RNase MRP and RNase P complexes. We also show that certain mutants of hPop4 accumulate in the Cajal bodies, suggesting that hPop4 traverses through these bodies to the nucleolus. Furthermore, we characterized a deletion mutant of Rpp38 that preferentially associates with the RNase MRP complex, giving a first clue about the difference in protein composition of the human RNase MRP and RNase P complexes. On the basis of all available data on nucleolar localization sequences, we hypothesize that nucleolar accumulation of proteins containing basic domains proceeds by diffusion and retention rather than by an active transport process. The existence of nucleolar localization sequences is discussed.
TI  - Basic domains target protein subunits of the RNase MRP complex to the nucleolus independently of complex association.
EP  - 3689
SN  - 1059-1524
IS  - iss. 11
SP  - 3680
JF  - Molecular Biology of the Cell
VL  - vol. 12
DO  - http://dx.doi.org/10.1091/mbc.12.11.3680
ER  - 
TY  - JOUR
AU  - Rutjes, S.A.
AU  - Lund, E.
AU  - Heijden, A.G. van der
AU  - Grimm, C
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2001
UR  - https://hdl.handle.net/2066/143797
AB  - Ro RNPs are small cytoplasmic RNA-protein complexes of unknown function that have been found in all metazoan cells studied so far. In human cells, Ro RNPs consist of one of four small RNA molecules, termed hY RNAs and at least two well-characterized proteins, Ro60 and La. In previous Xenopus laevis oocyte microinjection studies, we showed that an intact Ro60 binding site (Stem-loop 1) is a prerequisite for efficient nuclear export of hY1 RNA, whereas an intact La-binding site promotes nuclear retention (Simons et al. RNA, 1996, 2:264-273). Here we present evidence that the distal half (Stem 2) of the conserved base-paired stem structure found in all hY RNAs also plays a critical role in the export process. A minimal RNA molecule containing this region, L1S2 RNA, competes effectively for the export of full-length hY1 RNAs and is itself exported very rapidly in a Ro60-independent and RanGTP-dependent manner. Mutational analyses of this RNA shows that a 5'/3' terminal double-stranded stem structure (>10 bp) of no specific nucleotide sequence constitutes a novel nuclear export element (NEE). Cross-competition studies indicate that this type of NEE may also be involved in export of other classes of RNAs. Like full-length hY1 RNA, L1S2 RNA also competes for export of ET-202 RNA, an RNA that was selected for its efficient nuclear export in the presence of the nuclear transport inhibitor, VSV Matrix protein (Grimm et al. Proc Natl Acad Sci USA, 1997, 94:10122-10127). However, export of L1S2 RNA is strongly inhibited by VSV-M protein, showing that these RNAs use partially overlapping, but not identical export pathways. We propose that export of Y RNAs is mediated by two contiguous cis-acting elements in the 5'/3' double-stranded stem region that is conserved between different Y RNAs.
TI  - Identification of a novel cis-acting RNA element involved in nuclear export of hY RNAs.
EP  - 752
SN  - 1355-8382
IS  - iss. 5
SP  - 741
JF  - Rna : a Publication of the Rna Society
VL  - vol. 7
DO  - http://dx.doi.org/10.1017/S1355838201002503
ER  - 
TY  - JOUR
AU  - Ridanpaa, M
AU  - Eenennaam, H. van
AU  - Pelin, K.
AU  - Chadwick, R.
AU  - Johnson, C
AU  - Yuan, B.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
AU  - Salmela, R.
AU  - Rockas, S.
AU  - Makitie, O.
AU  - Tollervey, D.
AU  - Chapelle, A. dela
PY  - 2001
UR  - https://hdl.handle.net/2066/185709
AB  - The recessively inherited developmental disorder, cartilage-hair hypoplasia (CHH) is highly pleiotropic with manifestations including short stature, defective cellular immunity, and predisposition to several cancers. The endoribonuclease RNase MRP consists of an RNA molecule bound to several proteins. It has at least two functions, namely, cleavage of RNA in mitochondrial DNA synthesis and nucleolar cleaving of pre-rRNA. We describe numerous mutations in the untranslated RMRP gene that cosegregate with the CHH phenotype. Insertion mutations immediately upstream of the coding sequence silence transcription while mutations in the transcribed region do not. The association of protein subunits with RNA appears unaltered. We conclude that mutations in RMRP cause CHH by disrupting a function of RNase MRP RNA that affects multiple organ systems.
TI  - Mutations in the RNA component of RNase MRP cause a pleiotropic human disease, cartilage-hair hypoplasia.
EP  - 203
SN  - 0092-8674
IS  - iss. 2
SP  - 195
JF  - Cell
VL  - vol. 104
DO  - https://doi.org/10.1016/S0092-8674(01)00205-7
ER  - 
TY  - JOUR
AU  - Brouwer, R.
AU  - Pruijn, G.J.M.
AU  - Venrooij, W.J.W. van
PY  - 2001
UR  - https://hdl.handle.net/2066/186939
AB  - The anti-PM/Scl autoantibodies are known to characterize a subset of autoimmune patients with myositis, scleroderma (Scl), and the PM/Scl overlap syndrome. The major autoantigens that are recognized by anti-PM/Scl autoantibodies are designated PM/Scl-100 and PM/Scl-75. These autoantigens have been reported to associate into a large complex consisting of 11 to 16 proteins and to play a role in ribosome synthesis. Recently, it was discovered that the PM/Scl complex is the human counterpart of the yeast (Saccharomyces cerevisiae) exosome, which is an RNA-processing complex consisting of 11 3' --> 5' exoribonucleases. To date, 10 human exosome components have been identified, although only some of these were studied in more detail. In this review, we discuss some recent advances in the characterization of the PM/Scl complex.
TI  - The human exosome: an autoantigenic complex of exoribonucleases in myositis and scleroderma.
EP  - 106
SN  - 1478-6354
IS  - iss. 2
SP  - 102
JF  - Arthritis Research & Therapy
VL  - vol. 3
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/186939/186939.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Brouwer, R.
AU  - Hengstman, G.J.D.
AU  - Vree Egberts, W.T.M.
AU  - Ehrfeld, H.
AU  - Bozic, B.
AU  - Ghirardello, A.
AU  - Grondal, G.
AU  - Hietarinta, M.
AU  - Isenberg, D.A.
AU  - Kalden, J.R.
AU  - Lundberg, I.
AU  - Moutsopoulos, H.M.
AU  - Roux-Lombard, P.
AU  - Vencovsky, J.
AU  - Wikman, A.
AU  - Seelig, H.P.
AU  - Engelen, B.G.M. van
AU  - Venrooij, W.J.W. van
PY  - 2001
UR  - https://hdl.handle.net/2066/185568
AB  - OBJECTIVE: To determine the prevalence of myositis specific autoantibodies (MSAs) and several myositis associated autoantibodies (MAAs) in a large group of patients with myositis. METHODS: A total of 417 patients with myositis from 11 European countries (198 patients with polymyositis (PM), 181 with dermatomyositis (DM), and 38 with inclusion body myositis (IBM)) were serologically analysed by immunoblot, enzyme linked immunosorbent assay (ELISA) and/or immunoprecipitation. RESULTS: Autoantibodies were found in 232 sera (56%), including 157 samples (38%) which contained MSAs. The most commonly detected MSA was anti-Jo-1 (18%). Other anti-synthetase, anti-Mi-2, and anti-SRP autoantibodies were found in 3%, 14%, and 5% of the sera, respectively. A relatively high number of anti-Mi-2 positive PM sera were found (9% of PM sera). The most commonly detected MAA was anti-Ro52 (25%). Anti-PM/Scl-100, anti-PM/Scl-75, anti-Mas, anti-Ro60, anti-La, and anti-U1 snRNP autoantibodies were present in 6%, 3%, 2%, 4%, 5%, and 6% of the sera, respectively. Remarkable associations were noticed between anti-Ro52 and anti-Jo-1 autoantibodies and, in a few sera, also between anti-Jo-1 and anti-SRP or anti-Mi-2 autoantibodies. CONCLUSIONS: The incidence of most of the tested autoantibody activities in this large group of European patients is in agreement with similar studies of Japanese and American patients. The relatively high number of PM sera with anti-Mi-2 reactivity may be explained by the use of multiple recombinant fragments spanning the complete antigen. Furthermore, our data show that some sera may contain more than one type of MSA and confirm the strong association of anti-Ro52 with anti-Jo-1 reactivity.
TI  - Autoantibody profiles in the sera of European patients with myositis.
EP  - 23
SN  - 0003-4967
IS  - iss. 2
SP  - 116-
JF  - Annals of the Rheumatic Diseases
VL  - vol. 60
DO  - https://doi.org/10.1136/ard.60.2.116
ER  - 
TY  - JOUR
AU  - Brouwer, R.
AU  - Allmang, C.
AU  - Raijmakers, R.
AU  - Aarssen, Y.A.W.G. van
AU  - Egberts, W.V.
AU  - Petfalski, E.
AU  - Venrooij, W.J.W. van
AU  - Tollervey, D.
AU  - Pruijn, G.J.M.
PY  - 2001
UR  - https://hdl.handle.net/2066/186951
AB  - The yeast exosome is a complex of 3' --> 5' exoribonucleases. Sequence analysis identified putative human homologues for exosome components, although several were found only as expressed sequence tags. Here we report the cloning of full-length cDNAs, which encode putative human homologues of the Rrp40p, Rrp41p, and Rrp46p components of the exosome. Recombinant proteins were expressed and used to raise rabbit antisera. In Western blotting experiments, these decorated HeLa cell proteins of the predicted sizes. All three human proteins were enriched in the HeLa cells nucleus and nucleolus, but were also clearly detected in the cytoplasm. Size exclusion chromatography revealed that hRrp40p, hRrp41p, and hRrp46p were present in a large complex. This cofractionated with the human homologues of other exosome components, hRrp4p and PM/Scl-100. Anti-PM/Scl-positive patient sera coimmunoprecipitated hRrp40p, hRrp41p, and hRrp46p demonstrating their physical association. The immunoprecipitated complex exhibited 3' --> 5' exoribonuclease activity in vitro. hRrp41p was expressed in yeast and shown to suppress the lethality of genetic depletion of yeast Rrp41p. We conclude that hRrp40p, hRrp41p, and hRrp46p represent novel components of the human exosome complex.
TI  - Three novel components of the human exosome.
EP  - 6184
SN  - 1083-351X
IS  - iss. 9
SP  - 6177
JF  - Journal of Biological Chemistry
VL  - vol. 276
DO  - https://doi.org/10.1074/jbc.M007603200
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/186951/186951.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Eenennaam, H. van
AU  - Lugtenberg, T.M.
AU  - Vogelzangs, J.H.P.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2001
UR  - https://hdl.handle.net/2066/216408
AB  - The RNase MRP and RNase P particles both function as endoribonucleases. RNase MRP has been implicated in the processing of precursor-rRNA, whereas RNase P has been shown to function in the processing of pre-tRNA. Both ribonucleoprotein particles have an RNA component that can be folded into a similar secondary structure and share several protein components. We have identified human, rat, mouse, cow, and Drosophila homologues of the Pop5p protein subunit of the yeast RNase MRP and RNase P complexes. The human Pop5 cDNA encodes a protein of 163 amino acids with a predicted molecular mass of 18.8 kDa. Polyclonal antibodies raised against recombinant hPop5 identified a 19-kDa polypeptide in HeLa cells and showed that hPop5 is associated with both RNase MRP and RNase P. Using affinity-purified anti-hPop5 antibodies, we demonstrated that the endogenous hPop5 protein is localized in the nucleus and accumulates in the nucleolus, which is consistent with its association with RNase MRP and RNase P. Catalytically active RNase P was partially purified from HeLa cells, and hPop5 was shown to be associated with it. Finally, the evolutionarily conserved acidic C-terminal tail of hPop5 appeared to be required neither for complex formation nor for RNase P activity.
TI  - hPop5, a protein subunit of the human RNase MRP and RNase P endoribonucleases.
EP  - 31641
SN  - 1083-351X
IS  - iss. 34
SP  - 31635
JF  - Journal of Biological Chemistry
VL  - vol. 276
DO  - https://doi.org/10.1074/jbc.M103399200
ER  - 
TY  - JOUR
AU  - Hengstman, G.J.D.
AU  - Engelen, B.G.M. van
AU  - Vree Egberts, W.T.M.
AU  - Venrooij, W.J.W. van
PY  - 2001
UR  - https://hdl.handle.net/2066/191674
AB  - Myositis-specific autoantibodies (MSAs) are found in almost half the patients with an idiopathic inflammatory myopathy (IIM). Several clinical and epidemiological studies have suggested that MSAs are associated with specific clinical characteristics. Some of these associations are well-defined and are of clinical significance ( eg, anti-Jo-1 and the anti-synthetase syndrome), others are less well established and can cause unnecessary anxiety for both patients and physicians ( eg, anti-SRP and cardiac involvement). In this review, an overview is given of the various MSAs, their biochemical background, their clinical usefulness, and the promises they hold for a better understanding of IIM.
TI  - Myositis-specific autoantibodies: overview and recent developments.
EP  - 82
SN  - 1040-8711
IS  - iss. 6
SP  - 476-
JF  - Current Opinion in Rheumatology
VL  - vol. 13
DO  - https://doi.org/10.1097/00002281-200111000-00004
ER  - 
TY  - JOUR
AU  - Roeffen, W.F.G.
AU  - Raats, J.M.H.
AU  - Teelen, K.A.E.M.
AU  - Hoet, R.M.A.
AU  - Eling, W.M.C.
AU  - Venrooij, W.J.W. van
AU  - Sauerwein, R.W.
PY  - 2001
UR  - https://hdl.handle.net/2066/216407
AB  - We report the first construction of two combinatorial human phage display libraries derived from malaria-immune patients. Specific single-chain Fv fragments (scFv) against Pfs48/45, a gamete surface protein of the sexual stages of Plasmodium falciparum, were selected and analyzed extensively. The selected scFv reacted with the surface of extracellular sexual forms of the parasite and showed Pfs48/45 reactivity on immunoblot. The scFv inhibit binding of human malaria sera to native Pfs48/45 from gametocytes. Moreover, the scFv bind to target epitopes of Pfs48/45 exposed in natural infections. Sequence analysis of eight scFv clones specific for epitope III of Pfs48/45 revealed that these clones could be divided into one V(H) family-derived germ-line gene (V(H)1) and two V(L) family segments (V(L)2 and V(K)I).
TI  - Recombinant human antibodies specific for the Pfs48/45 protein of the malaria parasite Plasmodium falciparum.
EP  - 19811
SN  - 1083-351X
IS  - iss. 23
SP  - 19807
JF  - Journal of Biological Chemistry
VL  - vol. 276
DO  - https://doi.org/10.1074/jbc.M100562200
ER  - 
TY  - JOUR
AU  - Eenennaam, H. van
AU  - Jarrous, N.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2000
UR  - https://hdl.handle.net/2066/185867
AB  - In the past decade, important advances have been made in our knowledge of the composition of human RNase MRP and RNase P complexes. Both ribonucleoprotein particles function as endonucleases and contain RNA components that are structurally related. RNase MRP has been suggested to be involved in the processing of precursor rRNA; RNase P, in the maturation of tRNA. Here we give an overview of current data on the structure and function of human RNase MRP and RNase P particles, with emphasis on their molecular composition. At present, seven protein subunits, probably all associated with both ribonucleoprotein particles, have been isolated and their corresponding cDNAs cloned. Although no known structural motifs can be identified in the amino acid sequences of these proteins, the majority is clearly rich in basic residues. For two protein subunits, a cluster of basic amino acids have been shown to be involved in nucleolar accumulation, whereas another protein, which lacks such a region, probably enters the nucleolus by way of a piggyback mechanism. The binding regions for several of the protein subunits on the RNA have been identified, and the data have been used to create a putative structural model for the RNase MRP particle. The rather obscure situation concerning the association of the autoantigenic Th-40 protein and its possible relationship with one of the subunits, Rpp38, is discussed.
TI  - Architecture and function of the human endonucleases RNase P and RNase MRP.
EP  - 272
SN  - 1521-6543
IS  - iss. 4
SP  - 265
JF  - International Union of Biochemistry and Molecular Biology Life
VL  - vol. 49
ER  - 
TY  - JOUR
AU  - Clemens, M.J.
AU  - Venrooij, W.J.W. van
AU  - Putte, L.B.A. van de
PY  - 2000
UR  - https://hdl.handle.net/2066/186996
TI  - Apoptosis and Autoimmunity
EP  - 133
SN  - 1350-9047
SP  - 131
JF  - Cell Death and Differentiation
VL  - vol. 7
PS  - 3 p.
ER  - 
TY  - JOUR
AU  - Rodenburg, R.J.T.
AU  - Ganga, A.
AU  - Lent, P.L.E.M. van
AU  - Putte, L.B.A. van de
AU  - Venrooij, W.J.W. van
PY  - 2000
UR  - https://hdl.handle.net/2066/187200
TI  - The antiinflammatory drug sulfasalazine inhibits tumor necrosis factor a  expression in macrophages by inducing apoptis
EP  - 1950
SN  - 0004-3591
IS  - iss. 9
SP  - 1941
JF  - Arthritis and Rheumatism
VL  - vol. 43
PS  - 10 p.
DO  - http://dx.doi.org/10.1002/1529-0131(200009)43:9&lt;1941::AID-ANR4&gt;3.0.CO;2-O
ER  - 
TY  - JOUR
AU  - Lawley, W.
AU  - Doherty, A
AU  - Denniss, S
AU  - Chauhan, D
AU  - Pruijn, G.J.M.
AU  - Venrooij, W.J.W. van
AU  - Lunec, J
AU  - Herbert, K
PY  - 2000
UR  - https://hdl.handle.net/2066/184613
AB  - OBJECTIVE: In vitro treatment with ultraviolet B (UVB) induces relocalization of lupus autoantigens to the cell surface. We have addressed the relationship between autoantigen relocalization, accumulation of intracellular reactive oxygen species (ROS) and the induction of apoptosis following UVA and UVB exposure. METHODS: Human primary keratinocytes were exposed in vitro to doses of UVA and UVB equivalent to 0.01-4 times the minimal erythemal dose. The cellular locations of Ro60, Ro52, Sm, U2-B" and La were determined using monoclonal antibodies. ROS accumulation and apoptosis induction were assessed using the intracellular ROS probe 2'7'-dichlorodihydrofluorescein diacetate, and the viability stains Hoechst 33342 and propidium iodide. RESULTS: UV treatment induced the relocalization of all five autoantigens investigated and an accumulation of ROS. UVA and UVB induced necrosis and apoptosis, respectively. CONCLUSION: These data suggest that both UVA and UVB induce ROS within keratinocytes but have significantly different effects upon autoantigen relocalization and cell viability.
TI  - Rapid lupus autoantigen relocalization and reactive oxygen species accumulation following ultraviolet irradiation of human keratinocytes.
EP  - 261
SN  - 1462-0324
IS  - iss. 3
SP  - 253
JF  - Rheumatology
VL  - vol. 39
DO  - http://dx.doi.org/10.1093/rheumatology/39.3.253
ER  - 
TY  - JOUR
AU  - Broekhuis, C.H.
AU  - Neubauer, G.
AU  - Heijden, A.G. van der
AU  - Mann, M.
AU  - Proud, C.G.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2000
UR  - https://hdl.handle.net/2066/187036
AB  - The La (SS-B) autoantigen is an evolutionarily conserved phosphoprotein which plays an important role, most likely as an RNA chaperone, in various processes, such as the biosynthesis and maturation of RNA polymerase III transcripts in the cell nucleus and (internal) initiation of translation in the cytoplasm. In this study, the phosphorylation state of this protein from human HeLa and HEp-2 cells was characterized by high-resolution two-dimensional IEF/SDS-PAGE analysis, and phosphorylation sites were mapped by nanoelectrospray mass spectrometry. Furthermore, the effect of phosphorylation at the sites identified on the subcellular distribution of the protein was studied by site-directed mutagenesis. At least 14 isoelectric isoforms were discerned on 2-D gels with La protein from both types of cells. Metabolic labeling in combination with alkaline phosphatase treatment revealed that only a limited number of these isoforms could be attributed to phosphorylation. Four phosphorylation sites, Thr-302, Ser-325, Thr-362, and Ser-366, were mapped by mass spectrometric analysis of the isolated La protein from HeLa cells or the carboxy-terminal half of this protein. The analysis of mutants of La, in which the respective phosphorylated residues were replaced by either a neutral (alanine) or an acidic (aspartate) residue, by microinjection into Xenopus laevis oocytes on the one hand and transfection of HEp-2 cells on the other hand revealed that the subcellular distribution of this protein was not affected by these amino acid substitutions. These results strongly suggest that the signals that determine the subcellular distribution of this protein are not regulated by (de)phosphorylation of the target residues examined.
TI  - Detailed analysis of the phosphorylation of the human La (SS-B) autoantigen. (De)phosphorylation does not affect its subcellular distribution.
EP  - 3033
SN  - 0006-2960
IS  - iss. 11
SP  - 3023
JF  - Biochemistry
VL  - vol. 39
DO  - http://dx.doi.org/10.1021/bi992308c
ER  - 
TY  - JOUR
AU  - Schellekens, G.A.
AU  - Visser, H.K.A.
AU  - Jong, B.A.W. de
AU  - Hoogen, F.H.J. van den
AU  - Hazes, J.M.W.
AU  - Breedveld, F.C.
AU  - Venrooij, W.J.W. van
PY  - 2000
UR  - https://hdl.handle.net/2066/138810
TI  - The diagnostic properties of rheumatoid arthritis antibodies recognizing a cyclic citrullinated peptide
EP  - 163
SN  - 0004-3591
IS  - iss. 1
SP  - 155
JF  - Arthritis and Rheumatism
VL  - vol. 43
PS  - 9 p.
DO  - https://doi.org/10.1002/1529-0131(200001)43:1<155::AID-ANR20>3.0.CO;2-3
ER  - 
TY  - JOUR
AU  - Hengstman, G.J.D.
AU  - Venrooij, W.J.W. van
AU  - Vencovsky, J.
AU  - Moutsopoulos, H.M.
AU  - Engelen, B.G.M. van
PY  - 2000
UR  - https://hdl.handle.net/2066/187503
TI  - The relative prevalence of dermatomyositis and polymyositis in Europe exhibits a latitudinal gradient.
EP  - 142
SN  - 0003-4967
SP  - 141
JF  - Annals of the Rheumatic Diseases
VL  - vol. 59
DO  - https://doi.org/10.1136/ard.59.2.141
ER  - 
TY  - JOUR
AU  - Hengstman, G.J.D.
AU  - Venrooij, W.J.W. van
AU  - Vree Egberts, W.T.M.
AU  - Engelen, B.G.M. van
PY  - 2000
UR  - https://hdl.handle.net/2066/191675
TI  - Clinical and serological characteristics of myositis: myositis specific autoantibodies aid in the differential diagnosis of the idiopathic inflammatory myopathies.
SN  - 0028-3878
IS  - iss. suppl.3
SP  - A240
JF  - Neurology
VL  - vol. 54
ER  - 
TY  - JOUR
AU  - Teunissen, S.W.
AU  - Kruithof, M.J.
AU  - Farris, A.D.
AU  - Harley, J.B.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 2000
UR  - https://hdl.handle.net/2066/184433
AB  - In this study, phylogenetically conserved structural features of the Ro RNP associated Y RNAs were investigated. The human, iguana, and frog Y3 and Y4 RNA sequences have been determined previously and the respective RNAs were subjected to enzymatic and chemical probing to obtain structural information. For all of the analyzed RNAs, the probing data were used to compose secondary structures, which partly deviate from previously predicted structures. Our results confirm the existence of two stem structures, which are also found at similar positions in hY1 and hY5 RNA. For the remaining parts of hY3 and hY4 RNA the secondary structures differ from those previously proposed based upon computer predictions. What might be more important is that certain parts of the RNAs appear to be flexible, i.e., to adopt several conformations. Another striking feature is that a characteristic pyrimidine-rich region, present in every Y RNA known, is single-stranded in all secondary structures. This may suggest that this region is readily available for base pairing inter-actions with other cellular nucleic acids, which might be important for the as yet unknown function of the RNAs.
TI  - Conserved features of Y RNAs: a comparison of experimentally derived secondary structures.
EP  - 619
SN  - 0305-1048
IS  - iss. 2
SP  - 610
JF  - Nucleic Acids Research
VL  - vol. 28
DO  - http://dx.doi.org/10.1093/nar/28.2.610
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/184433/184433.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Kroot, E.J.A.
AU  - Jong, B.A.W. de
AU  - Leeuwen, M.A. van
AU  - Swinkels, H.L.
AU  - Hoogen, F.H.J. van den
AU  - Hof, M.A. van 't
AU  - Putte, L.B.A. van de
AU  - Rijswijk, M.H. van
AU  - Venrooij, W.J.W. van
AU  - Riel, P.L.C.M. van
PY  - 2000
UR  - https://hdl.handle.net/2066/138811
TI  - The prognostic value of anticyclic citrullinated peptide antibody in patients with recent-onset rheumatoid arthritis
EP  - 1835
SN  - 0004-3591
SP  - 1831
JF  - Arthritis and Rheumatism
VL  - vol. 43
PS  - 5 p.
DO  - https://doi.org/10.1002/1529-0131(200008)43:8<1831::AID-ANR19>3.0.CO;2-6
ER  - 
TY  - JOUR
AU  - Degen, W.G.J.
AU  - Aarssen, Y.A.W.G. van
AU  - Pruijn, G.J.M.
AU  - Utz, P.J.
AU  - Venrooij, W.J.W. van
PY  - 2000
UR  - https://hdl.handle.net/2066/187655
AB  - During apoptosis, the U1-70K protein, a component of the spliceosomal U1 snRNP complex, is specifically cleaved by the enzyme caspase-3, converting it into a C-terminally truncated 40-kDa fragment. In this study, we show that the 40-kDa U1-70K fragment is still associated with the complete U1 snRNP complex, and that no obvious modifications occur with the U1 snRNP associated proteins U1A, U1C and Sm-B/B'. Furthermore, it is described for the first time that the U1 snRNA molecule, which is the backbone of the U1 snRNP complex, is modified during apoptosis by the specific removal of the first 5 - 6 nucleotides including the 2,2, 7-trimethylguanosine (TMG) cap. The observations that U1 snRNA cleavage is very specific (no such modifications were detected for the other U snRNAs tested) and that U1 snRNA cleavage is markedly inhibited in the presence of caspase inhibitors, indicate that an apoptotically activated ribonuclease is responsible for the specific modification of U1 snRNA during apoptosis.
TI  - The fate of U1 snRNP during anti-Fas induced apoptosis: specific cleavage of the U1 snRNA molecule.
EP  - 79
SN  - 1350-9047
IS  - iss. 1
SP  - 70
JF  - Cell Death and Differentiation
VL  - vol. 7
DO  - https://doi.org/10.1038/sj.cdd.4400617
ER  - 
TY  - JOUR
AU  - Degen, W.G.J.
AU  - Pruijn, G.J.M.
AU  - Raats, J.M.H.
AU  - Venrooij, W.J.W. van
PY  - 2000
UR  - https://hdl.handle.net/2066/224004
AB  - Autoimmune diseases are frequently characterized by the presence of autoantibodies directed against nucleic acid-protein complexes present in the nucleus of the cell. The mechanisms by which these autoantigenic molecules escape immunological tolerance are largely unknown, although a number of recent observations suggest that modified self-proteins generated during apoptosis may play an important role in the development of autoimmunity. It has been hypothesized that the recognition of these modified self-proteins by the immune system may promote autoantibody production. While apoptosis is specifically characterized by posttranslational modification of proteins, recent findings also show that nucleic acids are modified. This review summarizes the specific cleavages of some of these key nucleic acids, i.e. chromosomal DNA, ribosomal RNA and small structural RNAs (U1 snRNA, Y RNA), in apoptotic cells.
TI  - Caspase-dependent cleavage of nucleic acids.
EP  - 627
SN  - 1350-9047
IS  - iss. 7
SP  - 616
JF  - Cell Death and Differentiation
VL  - vol. 7
DO  - https://doi.org/10.1038/sj.cdd.4400672
ER  - 
TY  - JOUR
AU  - Farris, A.D.
AU  - Koelsch, G.
AU  - Pruijn, G.J.M.
AU  - Venrooij, W.J.W. van
AU  - Harley, J.B.
PY  - 1999
UR  - https://hdl.handle.net/2066/184732
AB  - Y RNAs are small 'cytoplasmic' RNAs which are components of the Ro ribonucleoprotein (RNP) complex. The core of this complex, which is found in the cell nuclei of higher eukaryotes as well as the cytoplasm, is composed of a complex between the 60 kDa Ro protein and Y RNAs. Human cells contain four distinct Y RNAs (Y1, Y3, Y4 and Y5), while other eukaryotes contain a variable number of Y RNA homologues. When detected in a particular species, the Ro RNP has been present in every cell type within that particular organism. This characteristic, along with its high conservation among vertebrates, suggests an important function for Ro RNP in cellular metabolism; however, this function has not yet been definitively elucidated. In order to identify conserved features of Y RNA sequences and structures which may be directly involved in Ro RNP function, a phylogenetic comparative analysis of Y RNAs has been performed. Sequences of Y RNA homologues from five vertebrate species have been obtained and, together with previously published Y RNA sequences, used to predict Y RNA secondary structures. A novel RNA secondary structure comparison algorithm, the suboptimal RNA analysis program, has been developed and used in conjunction with available algorithms to find phylogenetically conserved secondary structure models for YI, Y3 and Y4 RNAs. Short, conserved sequences within the Y RNAs have been identified and are invariant among vertebrates, consistent with a direct role for Y RNAs in Ro function. A subset of these are located wholly or partially in looped regions in the Y3 and Y4 RNA predicted model structures, in accord with the possibility that these Y RNAs base pair with other cellular nucleic acids or are sites of interaction between the Ro RNP and other macromolecules.
TI  - Conserved features of Y RNAs revealed by automated phylogenetic secondary structure analysis.
EP  - 1078
SN  - 0305-1048
IS  - iss. 4
SP  - 1070
JF  - Nucleic Acids Research
VL  - vol. 27
DO  - http://dx.doi.org/10.1093/nar/27.4.1070
ER  - 
TY  - JOUR
AU  - Pluk, W.L.L.P.
AU  - Eenennaam, H. van
AU  - Rutjes, S.A.
AU  - Pruijn, G.J.M.
AU  - Venrooij, W.J.W. van
PY  - 1999
UR  - https://hdl.handle.net/2066/187504
AB  - The eukaryotic nucleolus contains a large number of small RNA molecules that, in the form of small nucleolar ribonucleoprotein complexes (snoRNPs), are involved in the processing and modification of pre-rRNA. One of the snoRNPs that has been shown to possess enzymatic activity is the RNase MRP. RNase MRP is an endoribonuclease involved in the formation of the 5' end of 5.8S rRNA. In this study the association of the hPop1 protein with the RNase MRP complex was investigated. The hPop1 protein seems not to be directly bound to the RNA component, but requires nt 1-86 and 116-176 of the MRP RNA to associate with the RNase MRP complex via protein-protein interactions. UV crosslinking followed by ribonuclease treatment and immunoprecipitation with anti-Th/To antibodies revealed three human proteins of about 20, 25, and 40 kDa that can associate with the RNase MRP complex. The 20- and 25-kDa proteins appear to bind to stem-loop I of the MRP RNA whereas the 40-kDa protein requires the central part of the MRP RNA (nt 86-176) for association with the RNase MRP complex. In addition, we show that the human RNase P proteins Rpp30 and Rpp38 are also associated with the RNase MRP complex. Expression of Vesicular Stomatitis Virus- (VSV) tagged versions of these proteins in HeLa cells followed by anti-VSV immunoprecipitation resulted in coprecipitation of both RNase P and RNase MRP complexes. Furthermore, UV crosslinking followed by anti-Th/To and anti-Rpp38 immunoprecipitation revealed that the 40-kDa protein we detected in UV crosslinking is probably identical to Rpp38.
TI  - RNA-protein interactions in the human RNase MRP ribonucleoprotein complex.
EP  - 524
SN  - 1355-8382
IS  - iss. 4
SP  - 512
JF  - Rna : a Publication of the Rna Society
VL  - vol. 5
DO  - http://dx.doi.org/10.1017/S1355838299982079
ER  - 
TY  - JOUR
AU  - Rutjes, S.A.
AU  - Utz, P.J.
AU  - Heijden, A.G. van der
AU  - Broekhuis, C.H.
AU  - Venrooij, W.J.W. van
AU  - Pruijn, G.J.M.
PY  - 1999
UR  - https://hdl.handle.net/2066/186150
AB  - In the past few years, a role for apoptotic processes in the development of autoimmune diseases has been suggested. An increasing number of cellular proteins, which are modified during apoptosis, has been described, and many of these proteins have been identified as autoantigens. We have studied the effects of apoptosis on the La protein in more detail and for the first time demonstrate that this autoantigen is rapidly dephosphorylated after the induction of apoptosis. Dephosphorylation of the La protein was observed after induction of apoptosis by several initiators and in various cell types. Furthermore, we demonstrate that at least a subset of the La protein is proteolytically cleaved in vivo, generating a 45 kDa fragment. Dephosphorylation as well as cleavage of La is inhibited by ZnSO4 as well as by several tetrapeptide caspase inhibitors, indicating that these processes require the activation of caspases. Dephosphorylation of La is inhibited by low concentrations of okadaic acid, suggesting that a PP2A-like phosphatase is involved. Generation of the 45 kDa fragment is consistent with proteolytic cleavage at amino acids 371 and/or 374. The possible significance of the apoptotic changes in the La protein for autoantibody production is discussed.
TI  - The La (SS-B) autoantigen, a key protein in RNA biogenesis, is dephosphorylated and cleaved early during apoptosis.
EP  - 986
SN  - 1350-9047
IS  - iss. 10
SP  - 976
JF  - Cell Death and Differentiation
VL  - vol. 6
DO  - https://doi.org/10.1038/sj.cdd.4400571
ER  - 
TY  - JOUR
AU  - Rodenburg, R.J.T.
AU  - Hoogen, F.H.J. van den
AU  - Barrera Rico, P.
AU  - Venrooij, W.J.W. van
AU  - Putte, L.B.A. van de
PY  - 1999
UR  - https://hdl.handle.net/2066/138816
TI  - Superinduction of interleukin in 8 mRNA in activated monocyte derived macrophages from rheumatoid arthritis patients.
EP  - 652
SN  - 0003-4967
SP  - 648
JF  - Annals of the Rheumatic Diseases
VL  - vol. 58
PS  - 5 p.
DO  - https://doi.org/10.1136/ard.58.10.648
ER  - 
TY  - JOUR
AU  - Hoet, R.M.A.
AU  - Pieffers, M.
AU  - Stassen, H.W.S.
AU  - Raats, J.M.H.
AU  - Wildt, R.M.T. de
AU  - Pruijn, G.J.M.
AU  - Hoogen, F.H.J. van den
AU  - Venrooij, W.J.W. van
PY  - 1999
UR  - https://hdl.handle.net/2066/138818
TI  - The Importance of the Light Chain for the Epitope Specificity of Human Anti-U1 Small Nuclear RNA Autoantibodies Present in Systemic Lupus Erythematosus Patients
EP  - 3312
SN  - 0019-2805
SP  - 3304
JF  - Immunology
VL  - vol. 163
PS  - 9 p.
ER  - 
TY  - JOUR
AU  - Rodenburg, R.J.T.
AU  - Hoogen, F.H.J. van den
AU  - Putte, L.B.A. van de
AU  - Venrooij, W.J.W. van
PY  - 1998
UR  - https://hdl.handle.net/2066/138831
TI  - Peripheral blood monocytes of rheumatoid arthritis patients do not express elevated TNF a, IL-1B and IL-8 mRNA levels. A comparison of monocyte isolation procedures
EP  - 175
SN  - 0022-1759
SP  - 169
JF  - Journal of Immunological Methods
VL  - vol. 221
PS  - 7 p.
DO  - http://dx.doi.org/10.1016/S0022-1759(98)00183-5
ER  - 
TY  - JOUR
AU  - Rodenburg, R.J.T.
AU  - Brinkhuis, R.F.
AU  - Peek, R.
AU  - Westphal, J.R.
AU  - Hoogen, F.H.J. van den
AU  - Venrooij, W.J.W. van
AU  - Putte, L.B.A. van de
PY  - 1998
UR  - https://hdl.handle.net/2066/138825
TI  - Expression of macrophage-derived chemokine (MDC)mRNA in macrophages is enhanced by interleukin-1B, tumor necrosis factor a, and lipopolysaccharide
EP  - 611
SN  - 0741-5400
SP  - 606
JF  - Journal of Leukocyte Biology
VL  - vol. 63
PS  - 6 p.
DO  - http://dx.doi.org/10.1002/jlb.63.5.606
ER  - 
TY  - JOUR
AU  - Hengstman, G.J.D.
AU  - Engelen, B.G.M. van
AU  - Badrising, U.A.
AU  - Hoogen, F.H.J. van den
AU  - Venrooij, W.J.W. van
PY  - 1998
UR  - https://hdl.handle.net/2066/138834
TI  - Presence of the anti-Jo1 autoantibody excludes inclusion body myositis
EP  - 423
SN  - 0364-5134
SP  - 423
JF  - Annals of Neurology
VL  - vol. 44
PS  - 1 p.
ER  - 
TY  - JOUR
AU  - Kuppevelt, A.H.M.S.M. van
AU  - Dennissen, M.A.B.A.
AU  - Venrooij, W.J.W. van
AU  - Hoet, R.M.A.
AU  - Veerkamp, J.H.
PY  - 1998
UR  - https://hdl.handle.net/2066/123031
AB  - Detailed analysis of various heparan sulfate (HS) species is seriously hampered by a lack of appropriate tools, such as antibodies. We adopted phage display technology to generate anti-HS antibodies. A "single pot" semisynthetic human antibody phage display library was subjected to four rounds of selection on HS from bovine kidney using panning methodology. Three different phage clones expressing anti-HS single chain variable fragment antibodies (HS4C3, HS4D10, and HS3G8) were isolated, with an amino acid sequence of the complementarity-determining region 3 of GRRLKD (VH3 gene, DP-38), SLRMNGCGAHQ (VH3 gene, DP-42), and YYHYKVN (VH1 gene, DP-8), respectively. The antibodies react with HS and heparin, but not with DNA or other glycosaminoglycans. Kd values for HS are about 0.1 microM. The three antibodies react differently toward various HS preparations and show different staining patterns on rat kidney sections, indicating recognition of different HS molecules. This also holds for two described mouse anti-HS IgMs (JM403 and 10E4; both generated by conventional hybridoma technique) and indicates the presence of at least 5 different HS species in the kidney. O- and N-sulfation are important for binding of HS to HS4C3 and HS3G8. The three single chain antibodies, but not JM403, block a basic fibroblast growth factor binding site of HS. It is concluded that phage display technology presents a powerful technique to generate antibodies specific for HS epitopes. This is the first time this technique has been successfully applied to obtain directly antibodies to (poly)saccharides.
TI  - Generation and application of type-specific anti-heparan sulfate antibodies using phage display technology. Further evidence for heparan sulfate heterogeneity in the kidney.
EP  - 12966
SN  - 1083-351X
IS  - iss. 21
SP  - 12960
JF  - Journal of Biological Chemistry
VL  - vol. 273
DO  - https://doi.org/10.1074/jbc.273.21.12960
ER  - 
TY  - JOUR
AU  - Kuppevelt, A.H.M.S.M. van
AU  - Dennissen, M.A.B.A.
AU  - Venrooij, W.J.W. van
AU  - Hoet, R.M.A.
AU  - Veerkamp, J.H.
PY  - 1998
UR  - https://hdl.handle.net/2066/123030
TI  - Generation and application of type-specific anti-heparan sulfate antibodies using phage display technology. Further evidence for heparan sulfate heterogeneity in the kidney
EP  - 12966
SN  - 1083-351X
SP  - 12960
JF  - Journal of Biological Chemistry
VL  - vol. 273
DO  - https://doi.org/10.1074/jbc.273.21.12960
ER  - 
TY  - JOUR
AU  - Hoet, R.M.A.
AU  - Raats, J.M.H.
AU  - Wildt, R.M.T. de
AU  - Dumortier, H.
AU  - Muller, S.H.
AU  - Hoogen, F.H.J. van den
AU  - Venrooij, W.J.W. van
PY  - 1998
UR  - https://hdl.handle.net/2066/138826
TI  - Human monoclonal autoantibody fragments from combinatorial antibody libraries directed to the U1snRNP associated U1C protein; epitope mapping, immunolocallization and V-gene usage
EP  - 1055
SN  - 0161-5890
SP  - 1045
JF  - Molecular Immunology
VL  - vol. 35
PS  - 11 p.
DO  - https://doi.org/10.1016/S0161-5890(98)00093-5
ER  - 
TY  - JOUR
AU  - Brouwer, R.
AU  - Vree Egberts, W.T.M.
AU  - Jongen, P.J.H.
AU  - Engelen, B.G.M. van
AU  - Venrooij, W.J.W. van
PY  - 1998
UR  - https://hdl.handle.net/2066/192842
TI  - Anti-Frequent occurrence of anti-tRNAhis autoantibodies that recognize a conformational epitope in sera of patients with myositis
EP  - 1437
SN  - 0004-3591
SP  - 1428
JF  - Arthritis and Rheumatism
VL  - vol. 41
DO  - https://doi.org/10.1002/1529-0131(199808)41:8<1428::AID-ART12>3.0.CO;2-J
ER  - 
TY  - JOUR
AU  - Huhn, P.
AU  - Pruijn, G.J.M.
AU  - Venrooij, W.J. van
AU  - Bachmann, M.
PY  - 1997
UR  - https://hdl.handle.net/2066/29563
PB  - Oxford univ press
TI  - Characterization of the autoantigen La (SS-B) as a dsRNA unwinding enzyme
EP  - 416
SN  - 0305-1048
IS  - iss. 2
SP  - 410
JF  - Nucleic Acids Research
VL  - vol. 25
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/29563/29563.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Wildt, R.M.T. de
AU  - Ruytenbeek, R.
AU  - Venrooij, W.J. van
AU  - Hoet, R.M.A.
PY  - 1997
UR  - https://hdl.handle.net/2066/29233
PB  - Oxford univ press
TI  - Heavy chain CDR3 optimization of a germline encoded recombinant antibody fragment predisposed to bind the U1A protein
EP  - 841
SN  - 0269-2139
IS  - iss. 7
SP  - 835
JF  - Protein Engineering
VL  - vol. 10
ER  - 
TY  - JOUR
AU  - Brahms, H.
AU  - Raker, V.A.
AU  - Venrooij, W.J. van
AU  - Luhrmann, R.
PY  - 1997
UR  - https://hdl.handle.net/2066/28974
PB  - Lippincott-raven publ
TI  - A major, novel systemic lupus erythematosus autoantibody class recognizes the E, F, and G Sm snRNP proteins as an E-F-G complex but not in their denatured states
EP  - 682
SN  - 0004-3591
IS  - iss. 4
SP  - 672
JF  - Arthritis and Rheumatism
VL  - vol. 40
ER  - 
TY  - JOUR
AU  - Pruijn, G.J.M.
AU  - Simons, F.H.M.
AU  - Venrooij, W.J. van
PY  - 1997
UR  - https://hdl.handle.net/2066/28020
PB  - Wissenschaftliche verlag mbh
TI  - Intracellular localization and nucleocytoplasmic transport of Ro RNP components
EP  - 132
SN  - 0171-9335
IS  - iss. 2
SP  - 123
JF  - European Journal of Cell Biology
VL  - vol. 74
ER  - 
TY  - JOUR
AU  - Pruijn, G.J.M.
AU  - Schoute, F.
AU  - Thijssen, J.P.H.
AU  - Smeenk, R.J.T.
AU  - Venrooij, W.J. van
PY  - 1997
UR  - https://hdl.handle.net/2066/28019
PB  - Academic press ltd
TI  - Mapping of SLE-specific Sm B cell epitopes using murine monoclonal antibodies
EP  - 136
SN  - 0896-8411
IS  - iss. 2
SP  - 127
JF  - Journal of Autoimmunity
VL  - vol. 10
ER  - 
TY  - JOUR
AU  - Rutjes, S.A.
AU  - Egberts, W.T.M.V.
AU  - Jongen, P.
AU  - Hoogen, F. van den
AU  - Pruijn, G.J.M.
AU  - Venrooij, W.J. van
PY  - 1997
UR  - https://hdl.handle.net/2066/28090
PB  - Blackwell science ltd
TI  - Anti-Ro52 antibodies frequently co-occur with anti-Jo-1 antibodies in sera from patients with idiopathic inflammatory myopathy
EP  - 40
SN  - 0009-9104
IS  - iss. 1
SP  - 32
JF  - Clinical and Experimental Immunology
VL  - vol. 109
ER  - 
TY  - JOUR
AU  - Teunissen, S.W.M.
AU  - Gelder, C.W.G. van
AU  - Venrooij, W.J. van
PY  - 1997
UR  - https://hdl.handle.net/2066/28321
PB  - Amer chemical soc
TI  - Probing the 3' UTR structure of U1A mRNA and footprinting analysis of its complex with U1A protein
EP  - 1789
SN  - 0006-2960
IS  - iss. 7
SP  - 1782
JF  - Biochemistry
VL  - vol. 36
ER  - 
TY  - JOUR
AU  - Gunnewiek, J.M.T.K.
AU  - Aarssen, Y. van
AU  - Kemp, A. van der
AU  - Nelissen, R.
AU  - Pruijn, G.J.M.
AU  - Venrooij, W.J. van
PY  - 1997
UR  - https://hdl.handle.net/2066/29434
PB  - Academic press inc jnl-comp subscriptions
TI  - Nuclear accumulation of the U1 snRNP-specific protein C is due to diffusion and retention in the nucleus
EP  - 273
SN  - 0014-4827
IS  - iss. 1
SP  - 265
JF  - Experimental Cell Research
VL  - vol. 235
ER  - 
TY  - JOUR
AU  - Nelissen, R.L.H.
AU  - Gunnewiek, J.M.T.K.
AU  - Lambermon, M.H.L.
AU  - Venrooij, W.J. van
PY  - 1997
UR  - https://hdl.handle.net/2066/27882
PB  - Elsevier science bv
TI  - Cloning and characterization of two processed pseudogenes and the cDNA for the murine U1 snRNP-specific protein C
EP  - 278
SN  - 0378-1119
IS  - iss. 2
SP  - 273
JF  - Gene
VL  - vol. 184
ER  - 
TY  - JOUR
AU  - Wildt, R.M.T. de
AU  - Hoogen, F.H.J. van den
AU  - Venrooij, W.J. van
AU  - Hoet, R.M.A.
PY  - 1997
UR  - https://hdl.handle.net/2066/26147
TI  - Isolation and Characterization of single Anti-U1A-specific B Cells from Autoimmune patients.
EP  - 442
SN  - 0077-8923
SP  - 440
JF  - Annals of the New York Academy of Sciences
VL  - vol. 815
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/26147/26147___.PDF?sequence=1
ER  - 
TY  - JOUR
AU  - Wildt, R.M.T. de
AU  - Steenbakkers, P.
AU  - Pennings, A.H.M.
AU  - Hoogen, F.H.J. van den
AU  - Venrooij, W.J. van
AU  - Hoet, R.M.A.
PY  - 1997
UR  - https://hdl.handle.net/2066/25419
TI  - A New method for the analysis and production of monoclonal antibody fragments originating from single human B cells
EP  - 67
SN  - 0022-1759
SP  - 61
JF  - Journal of Immunological Methods
VL  - vol. 207
ER  - 
TY  - JOUR
AU  - Wildt, R.M.T. de
AU  - Steenbakkers, P.
AU  - Pennings, A.H.M.
AU  - Hoogen, F.H.J. van den
AU  - Venrooij, W.J. van
AU  - Hoet, R.M.A.
PY  - 1997
UR  - https://hdl.handle.net/2066/25683
TI  - A new method for the analysis and production of monoclonal antibody fragments originating from single human B cells
EP  - 67
SN  - 0022-1759
SP  - 61
JF  - Journal of Immunological Methods
VL  - vol. 207
ER  - 
TY  - JOUR
AU  - Ricchiuti, V.
AU  - Pruijn, G.J.M.
AU  - Thijssen, J.P.H.
AU  - Venrooij, W.J. van
AU  - Muller, S.
PY  - 1997
UR  - https://hdl.handle.net/2066/28054
PB  - Academic press ltd
TI  - Accessibility of epitopes on the 52-kD Ro/SSA protein (Ro52) and on the RoRNP associated Ro52 protein as determined by anti-peptide antibodies
EP  - 191
SN  - 0896-8411
IS  - iss. 2
SP  - 181
JF  - Journal of Autoimmunity
VL  - vol. 10
ER  - 
TY  - JOUR
AU  - Wildt, R.M.T. de
AU  - Steenbakkers, P.
AU  - Pennings, A.H.M.
AU  - Hoogen, F.H.J. van den
AU  - Venrooij, W.J.W. van
AU  - Hoet, R.M.A.
PY  - 1997
UR  - https://hdl.handle.net/2066/138838
TI  - A New method for the analysis and production of monoclonal antibody fragments originating from single human B cells
EP  - 67
SN  - 0022-1759
SP  - 61
JF  - Journal of Immunological Methods
VL  - vol. 207
PS  - 7 p.
DO  - https://doi.org/10.1016/S0022-1759(97)00108-7
ER  - 
TY  - JOUR
AU  - Wildt, R.M.T. de
AU  - Steenbakkers, P.
AU  - Pennings, A.H.M.
AU  - Hoogen, F.H.J. van den
AU  - Venrooij, W.J.W. van
AU  - Hoet, R.M.A.
PY  - 1997
UR  - https://hdl.handle.net/2066/138839
TI  - A new method for the analysis and production of monoclonal antibody fragments originating from single human B cells
EP  - 67
SN  - 0022-1759
SP  - 61
JF  - Journal of Immunological Methods
VL  - vol. 207
DO  - https://doi.org/10.1016/S0022-1759(97)00108-7
ER  - 
TY  - JOUR
AU  - Wildt, R.M.T. de
AU  - Hoogen, F.H.J. van den
AU  - Venrooij, W.J.W. van
AU  - Hoet, R.M.A.
PY  - 1997
UR  - https://hdl.handle.net/2066/138844
TI  - Isolation and Characterization of single AntiOU1A-specific B Cells from Autoimmune patients.
EP  - 442
SN  - 0077-8923
SP  - 440
JF  - Annals of the New York Academy of Sciences
VL  - vol. 815
DO  - https://doi.org/10.1111/j.1749-6632.1997.tb52097.x
ER  - 
TY  - JOUR
AU  - Lygerou, Z.
AU  - Pluk, H.
AU  - Venrooij, W.J. van
AU  - Seraphin, B.
PY  - 1996
UR  - https://hdl.handle.net/2066/27732
PB  - Oxford univ press united kingdom
TI  - hPop1: An autoantigenic protein subunit shared by the human RNase P and RNase MRP ribonucleoproteins
EP  - 5948
SN  - 0261-4189
IS  - iss. 21
SP  - 5936
JF  - EMBO Journal
VL  - vol. 15
ER  - 
TY  - JOUR
AU  - Simons, F.H.M.
AU  - Broers, F.J.M.
AU  - Venrooij, W.J. van
AU  - Pruijn, G.J.M.
PY  - 1996
UR  - https://hdl.handle.net/2066/28185
PB  - Academic press inc jnl-comp subscriptions
TI  - Characterization of cis-acting signals for nuclear import and retention of the La (SS-B) autoantigen
EP  - 236
SN  - 0014-4827
IS  - iss. 2
SP  - 224
JF  - Experimental Cell Research
VL  - vol. 224
ER  - 
TY  - JOUR
AU  - Will, C.L.
AU  - Rumpler, S.
AU  - Gunnewiek, J.K.
AU  - Venrooij, W.J. van
AU  - Luhrmann, R.
PY  - 1996
UR  - https://hdl.handle.net/2066/28862
PB  - Oxford univ press
TI  - In vitro reconstitution of mammalian U1 snRNPs active in splicing: The U1-C protein enhances the formation of early (E) spliceosomal complexes
EP  - 4623
SN  - 0305-1048
IS  - iss. 23
SP  - 4614
JF  - Nucleic Acids Research
VL  - vol. 24
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/28862/28862.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Venrooij, W.J. van
PY  - 1996
UR  - https://hdl.handle.net/2066/28700
PB  - Blackwell science ltd
TI  - Ribonucleoprotein complexes: Autoantigens in connective tissue diseases
EP  - SQ64
SN  - 0019-2805
SP  - SQ64
JF  - Immunology
VL  - Vol. 89
ER  - 
TY  - JOUR
AU  - Karwan, R.
AU  - Pluk, H.
AU  - Venrooij, W.J. van
PY  - 1996
UR  - https://hdl.handle.net/2066/29698
PB  - Kluwer academic publ
TI  - Introduction. RNase MRP/RNase P systems -
EP  - 67
SN  - 0301-4851
IS  - iss. 2-3
SP  - 67
JF  - Molecular Biology Reports
VL  - vol. 22
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/29698/29698___.PDF?sequence=1
ER  - 
TY  - JOUR
AU  - Peek, R.
AU  - Pruijn, G.J.M.
AU  - Venrooij, W.J. van
PY  - 1996
UR  - https://hdl.handle.net/2066/27940
PB  - Springer verlag
TI  - Interaction of the La (SS-B) autoantigen with small ribosomal subunits
EP  - 655
SN  - 0014-2956
IS  - iss. 2
SP  - 649
JF  - European Journal of Biochemistry
VL  - vol. 236
ER  - 
TY  - JOUR
AU  - Wilde, P.C.M. de
AU  - Kater, L.
AU  - Bodeutsch, C.
AU  - Hoogen, F.H.J. van den
AU  - Putte, L.B.A. van de
AU  - Venrooij, W.J. van
PY  - 1996
UR  - https://hdl.handle.net/2066/24082
TI  - Aberrant expression pattern of the SS-B/La antigen in the labial salivary glands of patients with Sjogren's syndrome
EP  - 791
SN  - 0004-3591
IS  - iss. 5
SP  - 783
JF  - Arthritis and Rheumatism
VL  - vol. 39
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/24082/24082.PDF?sequence=1
ER  - 
TY  - JOUR
AU  - Wilde, P.C.M. de
AU  - Kater, L.
AU  - Bodeutsch, C.
AU  - Hoogen, F.H.J. van den
AU  - Putte, L.B.A. van de
AU  - Venrooij, W.J.W. van
PY  - 1996
UR  - https://hdl.handle.net/2066/138849
TI  - Aberrant expression pattern of the SS-B/La antigen in the labial salivary glands of patients with Sjogren's syndrome
EP  - 791
SN  - 0004-3591
IS  - iss. 5
SP  - 783
JF  - Arthritis and Rheumatism
VL  - vol. 39
ER  - 
TY  - JOUR
AU  - Simons, F.H.M.
AU  - Rutjes, S.A.
AU  - Venrooij, W.J. van
AU  - Pruijn, G.J.M.
PY  - 1996
UR  - https://hdl.handle.net/2066/28186
PB  - Cambridge univ press
TI  - The interactions with Ro60 and La differentially affect nuclear export of hY1 RNA
EP  - 273
SN  - 1355-8382
IS  - iss. 3
SP  - 264
JF  - Rna : a Publication of the Rna Society
VL  - vol. 2
ER  - 
TY  - JOUR
AU  - Misaki, Y.
AU  - Venrooij, W.J. van
AU  - Pruijn, G.J.M.
PY  - 1995
UR  - https://hdl.handle.net/2066/27814
PB  - J rheumatol publ co
TI  - Prevalence and Characteristics of Anti-56k Annexin-Xi Autoantibodies in Systemic Autoimmune-Diseases
EP  - 102
SN  - 0315-162X
IS  - iss. 1
SP  - 97
JF  - The Journal of Rheumatology
VL  - vol. 22
ER  - 
TY  - JOUR
AU  - Pruijn, G.J.M.
AU  - Thijssen, J.P.H.
AU  - Smith, P.R.
AU  - Williams, D.G.
AU  - Venrooij, W.J. van
PY  - 1995
UR  - https://hdl.handle.net/2066/28021
PB  - Springer verlag
TI  - Anti-La Monoclonal-Antibodies Recognizing Epitopes within the Rna-Binding Domain of the La Protein Show Differential Capacities to Immunoprecipitate Rna-Associated La Protein
EP  - 619
SN  - 0014-2956
IS  - iss. 2
SP  - 611
JF  - European Journal of Biochemistry
VL  - vol. 232
ER  - 
TY  - JOUR
AU  - Venrooij, W.J. van
AU  - Pruijn, G.J.M.
PY  - 1995
UR  - https://hdl.handle.net/2066/28701
PB  - Current biology ltd
TI  - Ribonucleoprotein complexes as autoantigens
EP  - 824
SN  - 0952-7915
IS  - iss. 6
SP  - 819
JF  - Current Opinion in Immunology
VL  - vol. 7
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/28701/28701.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Gunnewiek, J.M.T.K.
AU  - Aarssen, Y. van
AU  - Wassenaar, R.
AU  - Legrain, P.
AU  - Venrooij, W.J. van
AU  - Nelissen, R.L.H.
PY  - 1995
UR  - https://hdl.handle.net/2066/29435
PB  - Oxford univ press united kingdom
TI  - Homodimerization of the human U1 snRNP-specific protein C
EP  - 4871
SN  - 0305-1048
IS  - iss. 23
SP  - 4864
JF  - Nucleic Acids Research
VL  - vol. 23
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/29435/29435.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Troster, H.
AU  - Bartsch, H.
AU  - Klein, R.
AU  - Metzger, T.E.
AU  - Pollak, G.
AU  - Semsei, I.
AU  - Schwemmle, M.
AU  - Pruijn, G.J.M.
AU  - Venrooij, W.J. van
AU  - Bachmann, M.
PY  - 1995
UR  - https://hdl.handle.net/2066/28364
PB  - Academic press ltd
TI  - Activation of a murine autoreactive B cell by immunization with human recombinant autoantigen La/SS-B: Characterization of the autoepitope
EP  - 842
SN  - 0896-8411
IS  - iss. 6
SP  - 825
JF  - Journal of Autoimmunity
VL  - vol. 8
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/28364/28364.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Venrooij, W.J.W. van
AU  - Kuijper-Lenstra, A.H.
AU  - Kramer, M.F.
PY  - 1973
UR  - https://hdl.handle.net/2066/142142
TI  - Interrelationship between amino acid pools and protein synthesis in the rat submandibular gland
EP  - 398
SN  - 0005-2787
IS  - iss. 2
SP  - 392
JF  - Biochimica et Biophysica Acta (Bba) - Nucleic Acids and Protein Synthesis
VL  - vol. 312
DO  - http://dx.doi.org/10.1016/0005-2787(73)90383-3
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/142142/142142.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Venrooij, W.J.W. van
AU  - Loon-Klaassen, L. van
PY  - 1973
UR  - https://hdl.handle.net/2066/142144
TI  - Intracellular amino acids and protein synthesis in Hela cells
EP  - 171
SN  - 0301-4851
IS  - iss. 3
SP  - 167
JF  - Molecular Biology Reports
VL  - vol. 1
DO  - http://dx.doi.org/10.1007/BF00357158
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/142144/142144.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Venrooij, W.J.W. van
AU  - Poort, C.
AU  - Geuze, J.J.
PY  - 1973
UR  - https://hdl.handle.net/2066/142906
TI  - The effects of fasting and feeding on the protein synthesis rate and polyribosomal profile of frog pepsinogenic cells
EP  - 909
SN  - 0021-9533
IS  - iss. 3
SP  - 903
JF  - Journal of Cell Science
VL  - vol. 12
L1  - https://repository.ubn.ru.nl/bitstream/handle/2066/142906/142906.pdf?sequence=1
ER  - 
TY  - JOUR
AU  - Hirsch, C.A.
AU  - Cox, M.A.
AU  - Venrooij, W.J.W. van
AU  - Henshaw, E.C.
PY  - 1973
UR  - https://hdl.handle.net/2066/144877
TI  - The Ribosome Cycle in Mammalian Protein Synthesis : II. ASSOCIATION OF THE NATIVE SMALLER RIBOSOMAL SUBUNIT WITH PROTEIN FACTORS
EP  - 4385
SN  - 1083-351X
IS  - iss. 12
SP  - 4377
JF  - Journal of Biological Chemistry
VL  - vol. 248
ER  -