Functionality of aquaporin-2 missense mutants in recessive nephrogenic diabetes insipidus

Pflugers Archiv European Journal of Physiology

Volumn 442, Issue 1, 2001, Pages 73-77

  Marr, N ^b   Kamsteeg, E J ^b   Van Raak, M ^b   Van Os, C H ^b   Deen, P M T ^a  

^a RADBOUD UNIVERSITY NIJMEGEN   (Netherlands)

^b RADBOUD UNIVERSITY MEDICAL CENTER   (Netherlands)

Author keywords

Oocytes; Trafficking; Water permeability

Indexed keywords

AMINO ACID; AQUAPORIN 2; MANNOSE;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; KIDNEY COLLECTING TUBULE; MISSENSE MUTATION; MOLECULAR INTERACTION; NEPHROGENIC DIABETES INSIPIDUS; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN GLYCOSYLATION; WATER PERMEABILITY;

AMINO ACID SEQUENCE; ANIMALS; AQUAPORIN 2; AQUAPORIN 6; AQUAPORINS; CELL MEMBRANE; CELL MEMBRANE PERMEABILITY; DIABETES INSIPIDUS, NEPHROGENIC; ENDOPLASMIC RETICULUM; FEMALE; GENE EXPRESSION; GLYCOSYLATION; IMMUNOBLOTTING; MANNOSE; MOLECULAR SEQUENCE DATA; MUTATION, MISSENSE; OOCYTES; OSMOSIS; TRANSFECTION; WATER; XENOPUS LAEVIS;

EID: 0035046505     PISSN: 00316768     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004240000498     Document Type: Article

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5. An impaired routing of wild-type aquaporin-2 after tetramerization with an aquaporin-2 mutant explains dominant nephrogenic diabetes insipidus
6. An aquaporin-2 water channel mutant which causes autosomal dominant nephrogenic diabetes insipidus is retained in the Golgi complex
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