The Amiloride-Sensitive Na+ Channel: From Primary Structure to Function
about
The NH(2) terminus of the epithelial sodium channel contains an endocytic motif.Functional domains within the degenerin/epithelial sodium channel (Deg/ENaC) superfamily of ion channels.Genetic models of mechanotransduction: the nematode Caenorhabditis elegans.Translational activation and repression by distinct elements within the 5'-UTR of ENaC alpha-subunit mRNA.External nickel inhibits epithelial sodium channel by binding to histidine residues within the extracellular domains of alpha and gamma subunits and reducing channel open probability.
P2860
The Amiloride-Sensitive Na+ Channel: From Primary Structure to Function
description
wetenschappelijk artikel
@nl
наукова стаття, опублікована в жовтні 1997
@uk
name
The Amiloride-Sensitive Na+ Channel: From Primary Structure to Function
@en
The Amiloride-Sensitive Na+ Channel: From Primary Structure to Function
@nl
type
label
The Amiloride-Sensitive Na+ Channel: From Primary Structure to Function
@en
The Amiloride-Sensitive Na+ Channel: From Primary Structure to Function
@nl
prefLabel
The Amiloride-Sensitive Na+ Channel: From Primary Structure to Function
@en
The Amiloride-Sensitive Na+ Channel: From Primary Structure to Function
@nl
P2093
P50
P1476
The Amiloride-Sensitive Na+ Channel: From Primary Structure to Function
@en
P2093
Anne Galibert
Guy Champigny
Michel Lazdunski
Nicolas Voilley
Stéphane Renard
Sylvie Coscoy
P304
P356
10.1016/S0300-9629(97)00066-2
P577
1997-10-01T00:00:00Z