Asp433 in the closing gate of ASIC1 determines stability of the open state without changing properties of the selectivity filter or Ca 2+ block

Journal of General Physiology

Volumn 137, Issue 3, 2011, Pages 289-297

  Li, Tianbo ^a   Yang, Youshan ^a   Canessa, Cecilia M ^a  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASIC CHANNEL; ASPARTIC ACID; CALCIUM; GLYCINE; NERVE PROTEIN; SODIUM CHANNEL;

ANIMAL; ARTICLE; CELL MEMBRANE POTENTIAL; CHANNEL GATING; CHEMISTRY; GENETICS; KINETICS; LAMPREY; METABOLISM; PATCH CLAMP; PH; POINT MUTATION; PROTEIN CONFORMATION; STRUCTURE ACTIVITY RELATION; XENOPUS LAEVIS;

ANIMALS; ASPARTIC ACID; CALCIUM; GLYCINE; HYDROGEN-ION CONCENTRATION; ION CHANNEL GATING; KINETICS; LAMPREYS; MEMBRANE POTENTIALS; NERVE TISSUE PROTEINS; PATCH-CLAMP TECHNIQUES; POINT MUTATION; PROTEIN CONFORMATION; SODIUM CHANNELS; STRUCTURE-ACTIVITY RELATIONSHIP; XENOPUS LAEVIS;

EID: 79952158534     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201010576     Document Type: Article

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