Intrinsic voltage dependence of the epithelial Na+ channel is masked by a conserved transmembrane domain tryptophan.
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Voltage-dependent gating underlies loss of ENaC function in Pseudohypoaldosteronism type 1.ENaC structure and function in the wake of a resolved structure of a family member.Structural mechanisms underlying the function of epithelial sodium channel/acid-sensing ion channel.In vivo and ex vivo analysis of tubule function.Pseudohypoaldosteronism type 1 and Liddle's syndrome mutations that affect the single-channel properties of the epithelial Na+ channel.Dietary K+ and Cl- independently regulate basolateral conductance in principal and intercalated cells of the collecting duct.Deficient transient receptor potential vanilloid type 4 function contributes to compromised [Ca2+]i homeostasis in human autosomal-dominant polycystic kidney disease cells.
P2860
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P2860
Intrinsic voltage dependence of the epithelial Na+ channel is masked by a conserved transmembrane domain tryptophan.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 20 July 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Intrinsic voltage dependence o ...... ansmembrane domain tryptophan.
@en
Intrinsic voltage dependence o ...... ansmembrane domain tryptophan.
@nl
type
label
Intrinsic voltage dependence o ...... ansmembrane domain tryptophan.
@en
Intrinsic voltage dependence o ...... ansmembrane domain tryptophan.
@nl
prefLabel
Intrinsic voltage dependence o ...... ansmembrane domain tryptophan.
@en
Intrinsic voltage dependence o ...... ansmembrane domain tryptophan.
@nl
P2093
P2860
P50
P356
P1476
Intrinsic voltage dependence o ...... ransmembrane domain tryptophan
@en
P2093
Elena Mironova
Eunan Hendron
Nina Boiko
Oleh Pochynyuk
Qiusheng Tong
Volodymyr Kucher
P2860
P304
25512-25521
P356
10.1074/JBC.M109.015917
P407
P577
2009-07-20T00:00:00Z