Physiology and pathophysiology of aquaporins.
Mulders
S M
SM
Department of Cell Physiology, University of Nijmegen, The Netherlands.
van Lieburg
A F
AF
Monnens
L A
LA
Knoers
N V
NV
Deen
P M
PM
van Os
C H
CH
D000595:Amino Acid Sequence; D000818:Animals; D051398:Aquaporin 1; D051399:Aquaporin 2; D051400:Aquaporin 3; D051401:Aquaporin 4; D051402:Aquaporin 5; D051403:Aquaporin 6; D020346:Aquaporins; D001789:Blood Group Antigens; D002874:Chromosome Mapping; D006801:Humans; D007473:Ion Channels / Q000737:chemistry / Q000235:genetics* / Q000502:physiology*; D008565:Membrane Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D017384:Sequence Deletion; D013329:Structure-Activity Relationship
C496020:AQP1 protein, human; C496023:AQP2 protein, human; C496027:AQP3 protein, human; C496030:AQP4 protein, human; C496036:AQP5 protein, human; D051399:Aquaporin 2; D051401:Aquaporin 4; D051402:Aquaporin 5; D051403:Aquaporin 6; D020346:Aquaporins; D001789:Blood Group Antigens; D007473:Ion Channels; D008565:Membrane Proteins; D051398:Aquaporin 1; D051400:Aquaporin 3