ENaC structure and function in the wake of a resolved structure of a family member

Our understanding of epithelial Na(+) channel (ENaC) structure and function has been profoundly impacted by the resolved structure of the homologous acid-sensing ion channel 1 (ASIC1). The structure of the extracellular and pore regions provide insight into channel assembly, processing, and the abil...

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Veröffentlicht in:	American journal of physiology. Renal physiology 2011-10, Vol.301 (4), p.F684-F696
Hauptverfasser:	Kashlan, Ossama B, Kleyman, Thomas R
Format:	Artikel
Sprache:	eng
Schlagworte:	Acid Sensing Ion Channels Amiloride - pharmacology Amino Acid Sequence Animals Chlorides - physiology Conserved Sequence Diuretics Epithelial Sodium Channels - drug effects Epithelial Sodium Channels - physiology Humans Ion Channel Gating - drug effects Ion Channel Gating - physiology Ions Mice Molecular Sequence Data Nerve Tissue Proteins - drug effects Nerve Tissue Proteins - physiology Physiology Plasma Rats Reviews Sequence Homology, Amino Acid Sodium Channel Blockers - pharmacology Sodium Channels - drug effects Sodium Channels - physiology Structure-Activity Relationship
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