N-terminal deletions of rKv1.4 channels affect the voltage dependence of channel availability

Pflugers Archiv European Journal of Physiology

Volumn 438, Issue 2, 1999, Pages 141-146

  Höllerer Beitz, Gerhild ^a   Schönherr, Roland ^a   Koenen, Michael ^b   Heinemann, Stefan H ^a  

^a FRIEDRICH SCHILLER UNIVERSITY JENA   (Germany)

^b MAX PLANCK INSTITUTE FOR MEDICAL RESEARCH   (Germany)

Author keywords

Activation; Inactivation; Mutagenesis; Potassium channels

Indexed keywords

CYSTEINE; POTASSIUM; POTASSIUM CHANNEL;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; GENE DELETION; MEMBRANE POTENTIAL; MUTAGENESIS; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; XENOPUS;

ANIMALS; ELECTROPHYSIOLOGY; KV1.4 POTASSIUM CHANNEL; MUTAGENESIS, SITE-DIRECTED; POTASSIUM CHANNELS; POTASSIUM CHANNELS, VOLTAGE-GATED; SEQUENCE DELETION; STRUCTURE-ACTIVITY RELATIONSHIP; XENOPUS;

EID: 0033040717     PISSN: 00316768     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004240050891     Document Type: Article

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