Mechanosensation and the DEG/ENaC ion channels

Science

Volumn 273, Issue 5273, 1996, Pages 323-324

  Corey, David P ^a   García Añoveros, Jaime ^a  

^a MASSACHUSETTS GENERAL HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ION CHANNEL;

CELL FUNCTION; CHEMOSENSITIVITY; ION TRANSPORT; MECHANICAL STIMULATION; PRIORITY JOURNAL; SHORT SURVEY;

AMINO ACID SEQUENCE; ANIMALS; CAENORHABDITIS ELEGANS; GENES, HELMINTH; HELMINTH PROTEINS; MOLECULAR SEQUENCE DATA; MUSCLE CONTRACTION; MUTATION; PHENOTYPE; SENSATION; SODIUM CHANNELS; TOUCH;

EID: 0029904202     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.273.5273.323     Document Type: Short Survey

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39. The conserved regions of all members (174 amino acids, including the transmembrane domains) were aligned with CLUSTALW and relationships calculated with PAUP version 3.1 with 2000 iterations. GenBank accession numbers for representative sequences are as follows: MEC-4 (U53669), MEC-10 (P34886), DEG-1 (L34414), E02H4.1 (Z68003), R13A1.4 (U40798), UNC-105 (Z48045), F02D10.5 (Z67990), C27C12.5 (Z67883), C18B2.6 (U40413), T28D9.7 (U28738), BNaC1 (U57352), FaNaC (X92113), αENaC (X70497), βENaC (X77932), γENaC (X77933), δENaC (U38254).
40. Supported by the Howard Hughes Medical Institute and the Ramón Areces Foundation. We appreciate help from B. Chang with the PAUP program.