Direct interaction of eag domains and cyclic nucleotide-binding homology domains regulate deactivation gating in hERG channels

Journal of General Physiology

Volumn 142, Issue 4, 2013, Pages 351-366

  Gianulis, Elena C ^a   Liu, Qiangni ^a   Trudeau, Matthew C ^a  

^a UNIVERSITY OF MARYLAND SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC NUCLEOTIDE; ERG1 POTASSIUM CHANNEL; POTASSIUM CHANNEL HERG;

ARTICLE; BINDING SITE; CHANNEL GATING; CHEMISTRY; FLUORESCENCE RESONANCE ENERGY TRANSFER; GENETICS; HEK293 CELL LINE; HUMAN; METABOLISM; MUTATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY;

BINDING SITES; ETHER-A-GO-GO POTASSIUM CHANNELS; FLUORESCENCE RESONANCE ENERGY TRANSFER; HEK293 CELLS; HUMANS; ION CHANNEL GATING; MUTATION; NUCLEOTIDES, CYCLIC; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 84885453003     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201310995     Document Type: Article

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