N-terminal inactivation domains of βsubunits are protected from trypsin digestion by binding within the antechamber of BK channels

Journal of General Physiology

Volumn 133, Issue 3, 2009, Pages 263-282

  Zhang, Zhe ^a   Zeng, Xu Hui ^a   Xia, Xiao Ming ^a   Lingle, Christopher J ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ACTIVATED POTASSIUM CHANNEL; LARGE CONDUCTANCE CALCIUM ACTIVATED POTASSIUM CHANNEL; TRYPSIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; NONHUMAN; PROTEIN EXPRESSION; PROTEIN STRUCTURE; STOCHASTIC MODEL;

AMINO ACID MOTIFS; ANIMALS; CALCIUM CHANNEL BLOCKERS; ELECTROPHYSIOLOGY; HUMANS; ION CHANNEL GATING; LARGE-CONDUCTANCE CALCIUM-ACTIVATED POTASSIUM CHANNEL ALPHA SUBUNITS; LARGE-CONDUCTANCE CALCIUM-ACTIVATED POTASSIUM CHANNEL BETA SUBUNITS; MICE; MUTATION; OOCYTES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; TRYPSIN; XENOPUS LAEVIS;

EID: 64549088411     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.200810079     Document Type: Article

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