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Browsing by Author Sluijs, P. van der
Showing results 1 to 10 of 10
| Full Text | Issue Date | Title | Author(s) | | 2011 | A platform for complementation and characterization of familial haemophagocytic lymphohistiocytosis 3 mutations. | Elstak, E.; Jong, A.S. de; Sluijs, P. van der |
| 2009 | LIP5 interacts with aquaporin 2 and facilitates its lysosomal degradation. | Balkom, B.W.M. van; Boone, M.; Hendriks, G.; Kamsteeg, E.J.; Robben, J.H., et al |
| 2009 | LIP5 interacts with aquaporin 2 and facilitates its lysosomal degradation | Balkom, B.W.M. van; Boone, M.; Hendriks, G.; Kamsteeg, E.J.; Robben, J.H., et al |
| 2009 | p.R254Q mutation in the aquaporin-2 water channel causing dominant nephrogenic diabetes insipidus is due to a lack of arginine vasopressin-induced phosphorylation. | Savelkoul, P.J.M.; Mattia, F.P. de; Li, Y.; Kamsteeg, E.J.; Konings, I.B.M., et al |
| 2006 | Lys63-linked short-chain ubiquitination regulates aquaporin-2 endocytosis from the apical membrane. | Kamsteeg, E.J.; Hendriks, G.; Boone, M.; Konings, I.B.M.; Oorschot, V., et al |
| 2005 | Lack of arginine vasopressin-induced phosphorylation of aquaporin-2 mutant AQP2-R254L explains dominant nephrogenic diabetes insipidus. | Mattia, F.P. de; Savelkoul, P.J.M.; Kamsteeg, E.J.; Konings, I.B.M.; Sluijs, P. van der, et al |
| 2004 | Role of cytoplasmic termini in sorting and shuttling of the aquaporin-2 water channel | Balkom, B.W.M. van; Graat, M.P.J.; Raak, M.M.J.P. van; Hofman, E.; Sluijs, P. van der, et al |
| 2004 | A novel mechanism in recessive nephrogenic diabetes insipidus: wild-type aquaporin-2 rescues the apical membrane expression of intracellularly retained AQP2-P262L. | Mattia, F.P. de; Savelkoul, P.J.M.; Bichet, D.G.; Kamsteeg, E.J.; Konings, I.B.M., et al |
| 2004 | Glycosylation is important for cell surface expression of the water channel aquaporin-2 but is not essential for tetramerization in the endoplasmic reticulum. | Hendriks, G.; Koudijs, M.; Balkom, B.W.M. van; Oorschot, V.; Klumperman, J., et al |
| 2004 | Rabip4' is an effector of rab5 and rab4 and regulates transport through early endosomes. | Fouraux, M.A.; Deneka, M.; Ivan, V.; Heijden, A.G. van der; Raymackers, J., et al |
Showing results 1 to 10 of 10
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