The membrane protein Pannexin1 forms two open-channel conformations depending on the mode of activation

Science Signaling

Volumn 7, Issue 335, 2014, Pages

  Wang, Junjie ^a   Ambrosi, Cinzia ^b   Qiu, Feng ^a   Jackson, David G ^a   Sosinsky, Gina ^b,c   Dahl, Gerhard ^a  

^a UNIVERSITY OF MIAMI MILLER SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMINO ACID; MEMBRANE PROTEIN; PANNEXIN 1; POTASSIUM ION; UNCLASSIFIED DRUG; GAP JUNCTION PROTEIN; NERVE PROTEIN; PANX1 PROTEIN, MOUSE; POTASSIUM;

ANIMAL CELL; ARTICLE; CELL MEMBRANE; CONDUCTANCE; CURRENT CLAMP TECHNIQUE; ELECTRIC POTENTIAL; EXTRACELLULAR CALCIUM; FEMALE; GAP JUNCTION; MEMBRANE CHANNEL; MEMBRANE CURRENT; MEMBRANE PERMEABILITY; MEMBRANE STEADY POTENTIAL; NONHUMAN; OOCYTE; PROTEIN CONFORMATION; VOLTAGE CLAMP TECHNIQUE; XENOPUS; ACTIVE TRANSPORT; ANIMAL; CELL MEMBRANE PERMEABILITY; DRUG EFFECTS; GENETICS; METABOLISM; MOUSE; PHYSIOLOGY; SIGNAL TRANSDUCTION; XENOPUS LAEVIS;

ADENOSINE TRIPHOSPHATE; ANIMALS; BIOLOGICAL TRANSPORT, ACTIVE; CELL MEMBRANE PERMEABILITY; CONNEXINS; MICE; NERVE TISSUE PROTEINS; POTASSIUM; SIGNAL TRANSDUCTION; XENOPUS LAEVIS;

EID: 84906827762     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2005431     Document Type: Article

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