Identification by mass spectrometry and functional characterization of two phosphorylation sites of KCNQ2/KCNQ3 channels

Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 49, 2005, Pages 17828-17833

  Surti, Toral S ^a   Huang, Lan ^b   Jan, Yuh Nung ^a   Jan, Lily Y ^a   Cooper, Edward C ^c  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c HOSPITAL OF THE UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

KCNQ; M channel; Neuromodulation; Potassium channels; S4 S5 loop

Indexed keywords

POTASSIUM CHANNEL KCNQ1; POTASSIUM CHANNEL KCNQ2; POTASSIUM CHANNEL KCNQ3; UNCLASSIFIED DRUG;

ARTICLE; ELECTROPHYSIOLOGY; HUMAN; MASS SPECTROMETRY; MUTAGENESIS; MYELINATED NERVE; NERVE EXCITABILITY; NEUROMODULATION; NONHUMAN; POTASSIUM CURRENT; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN LIPID INTERACTION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; RANVIER NODE;

AMINO ACID SEQUENCE; ANIMALS; CHROMATOGRAPHY, AFFINITY; ELECTROPHYSIOLOGY; HUMANS; KCNQ2 POTASSIUM CHANNEL; KCNQ3 POTASSIUM CHANNEL; MASS SPECTROMETRY; MOLECULAR SEQUENCE DATA; MUTATION; OOCYTES; PATCH-CLAMP TECHNIQUES; PHOSPHORYLATION; PHOSPHOTHREONINE; PROTEIN BINDING; PROTEIN TRANSPORT; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; XENOPUS LAEVIS;

EID: 29144477159     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0509122102     Document Type: Article

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