The contact region between three domains of the extracellular loop of ASIC1a is critical for channel function

Journal of Biological Chemistry

Volumn 285, Issue 18, 2010, Pages 13816-13826

  Bargeton, Benoîte ^a   Kellenberger, Stephan ^a  

^a UNIVERSITY OF LAUSANNE   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

ACID-SENSING ION CHANNELS; CHANNEL FUNCTIONS; CHANNEL OPENING; CONFORMATIONAL CHANGE; CONSERVED REGIONS; CONTACT REGIONS; CONTACT ZONE; CURRENT AMPLITUDE; CYS RESIDUES; EXTRACELLULAR; EXTRACELLULAR LOOPS; PH DEPENDENCE; PH-DEPENDENT; SULFHYDRYL;

ACIDS; METHANE;

PH EFFECTS;

ACID SENSING ION CHANNEL; ACID SENSING ION CHANNEL 1A; CADMIUM; CYSTEINE; THIOL REAGENT; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CHANNEL GATING; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ION CONDUCTANCE; NONHUMAN; OOCYTE; PH; PRIORITY JOURNAL; PROTEIN EXPRESSION; SITE DIRECTED MUTAGENESIS;

ANIMALS; HUMANS; HYDROGEN-ION CONCENTRATION; ION CHANNEL GATING; MESYLATES; MUTATION; NERVE TISSUE PROTEINS; PEPTIDE MAPPING; PROTEIN ENGINEERING; PROTEIN STRUCTURE, TERTIARY; SODIUM CHANNELS; XENOPUS LAEVIS;

EID: 77951523610     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.086843     Document Type: Article

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