Purified TMEM16A is sufficient to form Ca2+-activated Cl - channels

Proceedings of the National Academy of Sciences of the United States of America

Volumn 110, Issue 48, 2013, Pages 19354-19359

  Terashima, Hiroyuki ^a,b   Picollo, Alessandra ^a   Accardi, Alessio ^a  

^a WEILL CORNELL MEDICAL COLLEGE   (United States)

^b OSAKA UNIVERSITY   (Japan)

Author keywords

Anoctamin; Ion channels; Membrane protein; Reconstitution

Indexed keywords

CALCIUM ACTIVATED CHLORIDE CHANNEL; CALMODULIN; GLUTARALDEHYDE; LIPOSOME; PROTEIN; PROTEOLIPOSOME; TMEM16A PROTEIN; UNCLASSIFIED DRUG; VALINOMYCIN;

ARTICLE; CHLORIDE CURRENT; CHLORIDE TRANSPORT; DIMERIZATION; ELECTRIC POTENTIAL; GEL PERMEATION CHROMATOGRAPHY; HUMAN; MASS SPECTROMETRY; MOLECULAR WEIGHT; PATCH CLAMP; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; WESTERN BLOTTING;

ANOCTAMIN; ION CHANNELS; MEMBRANE PROTEIN; RECONSTITUTION;

ANIMALS; BIOLOGICAL TRANSPORT; CALMODULIN; CHLORIDE CHANNELS; CHROMATOGRAPHY, GEL; HUMANS; ION CHANNEL GATING; MUTAGENESIS; NEOPLASM PROTEINS; PLASMIDS; SEQUENCE ANALYSIS, DNA; SF9 CELLS; SPODOPTERA;

EID: 84888323395     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1312014110     Document Type: Article

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