Silke Haerteis

Plasmin in nephrotic urine activates the epithelial sodium channel.

The delta-subunit of the epithelial sodium channel (ENaC) enhances channel activity and alters proteolytic ENaC activation.

Cholesterol depletion of the plasma membrane prevents activation of the epithelial sodium channel (ENaC) by SGK1.

Functional characterization of a partial loss-of-function mutation of the epithelial sodium channel (ENaC) associated with atypical cystic fibrosis.

Atomic force microscopy reveals the architecture of the epithelial sodium channel (ENaC).

Four subunits (αβγδ) of the epithelial sodium channel (ENaC) are expressed in the human eye in various locations.

An inhibitory peptide derived from the α-subunit of the epithelial sodium channel (ENaC) shows a helical conformation.

Proteolytic activation of the epithelial sodium channel (ENaC) by the cysteine protease cathepsin-S.

Plasmin and chymotrypsin have distinct preferences for channel activating cleavage sites in the γ subunit of the human epithelial sodium channel.

A mutation in the β-subunit of ENaC identified in a patient with cystic fibrosis-like symptoms has a gain-of-function effect.

Pharmacological and electrophysiological characterization of the human bile acid-sensitive ion channel (hBASIC).

Proteolytic Activation of the Human Epithelial Sodium Channel by Trypsin IV and Trypsin I Involves Distinct Cleavage Sites.

Sensitisation of TRPV4 by PAR2 is independent of intracellular calcium signalling and can be mediated by the biased agonist neutrophil elastase.