The mechanosensory protein MEC-6 is a subunit of the C. elegans touch-cell degenerin channel

Nature

Volumn 420, Issue 6916, 2002, Pages 669-673

  Chelur, Dattananda S ^a   Ernstrom, Glen G ^a   Goodman, Miriam B ^a,b   Yao, C Andrea ^a   Chen, Lei ^a   O'Hagan, Robert ^a   Chalfie, Martin ^a  

^a Och Spine at New York Presbyterian Hospitals   (United States)

^b STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; GENES; MUTAGENS; SENSORY PERCEPTION;

HEART DISEASES;

PROTEINS;

AMILORIDE; ARYLDIALKYLPHOSPHATASE; MEMBRANE PROTEIN; PROTEIN MEC 6; PROTEIN SUBUNIT; SODIUM; SODIUM CHANNEL; STOMATIN; UNCLASSIFIED DRUG; CAENORHABDITIS ELEGANS PROTEIN; DEGENERIN PROTEIN, C ELEGANS; HELMINTH PROTEIN; MEC 10 PROTEIN, C ELEGANS; MEC 2 PROTEIN, C ELEGANS; MEC 4 PROTEIN, C ELEGANS; MEC 6 PROTEIN, C ELEGANS; MEC-10 PROTEIN, C ELEGANS; MEC-2 PROTEIN, C ELEGANS; MEC-4 PROTEIN, C ELEGANS; MEC-6 PROTEIN, C ELEGANS;

GENE; PROTEIN;

ANIMAL CELL; ARTICLE; CAENORHABDITIS ELEGANS; CELL DEGENERATION; CONTROLLED STUDY; DEGENERIN CHANNEL; GENE EXPRESSION; GENE MUTATION; MECHANICAL STIMULATION; MEMBRANE CHANNEL; MUSCLE CELL; NEMATODE; NERVE CELL; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; SENSORY SYSTEM; SIGNAL TRANSDUCTION; SODIUM CURRENT; TOUCH; TOUCH CELL; ANIMAL; CHANNEL GATING; CHEMISTRY; CHO CELL; CYTOLOGY; DRUG EFFECT; ELECTRIC CONDUCTIVITY; ENZYME SPECIFICITY; GENE; GENE REPRESSION; GENETICS; HAMSTER; MECHANORECEPTOR; METABOLISM; MOLECULAR CLONING; NERVE FIBER; OOCYTE; PHYSIOLOGY; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; PROTEIN TRANSPORT; XENOPUS LAEVIS;

ANIMALIA; CAENORHABDITIS ELEGANS; INVERTEBRATA; MAMMALIA; NEMATODA;

ANIMALS; AXONS; CAENORHABDITIS ELEGANS; CAENORHABDITIS ELEGANS PROTEINS; CHO CELLS; CLONING, MOLECULAR; CRICETINAE; ELECTRIC CONDUCTIVITY; GENES, HELMINTH; HELMINTH PROTEINS; ION CHANNEL GATING; MECHANORECEPTORS; MEMBRANE PROTEINS; OOCYTES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; PROTEIN TRANSPORT; SODIUM; SODIUM CHANNELS; SUBSTRATE SPECIFICITY; SUPPRESSION, GENETIC; TOUCH; XENOPUS LAEVIS;

EID: 0037069699     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01205     Document Type: Article

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