Closed-state inactivation in Kv4.3 isoforms is differentially modulated by protein kinase C

American Journal of Physiology - Cell Physiology

Volumn 297, Issue 5, 2009, Pages

  Xie, Chang ^a,b   Bondarenko, Vladimir E ^b,c   Morales, Michael J ^b   Strauss, Harold C ^b  

^a HUAZHONG UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

^b UNIVERSITY AT BUFFALO   (United States)

^c GEORGIA STATE UNIVERSITY   (United States)

Author keywords

Carboxy terminus; Open state inactivation; Recovery from closed state inactivation

Indexed keywords

AMINO ACID; ASPARTIC ACID; PHORBOL 13 ACETATE 12 MYRISTATE; POTASSIUM CHANNEL; POTASSIUM CHANNEL KV4.3; PROTEIN KINASE C; THREONINE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME INACTIVATION; MOLECULAR RECOGNITION; MUTATION; NONHUMAN; OOCYTE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; REGULATORY MECHANISM; XENOPUS;

ANIMALS; CONSENSUS SEQUENCE; ENZYME ACTIVATION; ION CHANNEL GATING; MODELS, MOLECULAR; PATCH-CLAMP TECHNIQUES; PHORBOL ESTERS; PROTEIN ISOFORMS; PROTEIN KINASE C; SHAL POTASSIUM CHANNELS; XENOPUS;

EID: 70449644671     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00144.2009     Document Type: Article

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