Glycosylation of asparagines 136 and 184 is necessary for the α2δ subunit-mediated regulation of voltage-gated Ca 2+ channels

FEBS Letters

Volumn 576, Issue 1-2, 2004, Pages 21-26

  Sandoval, Alejandro ^a   Oviedo, Norma ^a   Andrade, Arturo ^a   Felix, Ricardo ^a  

^a DEPARTAMENTO DE FÍSICA   (Mexico)

Author keywords

2 subunit; Ca V2.2 channel; Ca2+ channel; HEK 293 cell; N glycosylation

Indexed keywords

AMINO ACID; ASPARAGINE DERIVATIVE; BARIUM ION; GLUTAMINE; PROTEIN SUBUNIT; VOLTAGE GATED CALCIUM CHANNEL;

AMINO ACID SUBSTITUTION; ARTICLE; CELL MEMBRANE; EMBRYO; GLYCOSYLATION; HUMAN; HUMAN CELL; KINETICS; NUCLEOTIDE SEQUENCE; PATCH CLAMP; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; SITE DIRECTED MUTAGENESIS;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ASPARAGINE; BARIUM; CALCIUM CHANNELS; CELL LINE; CONSENSUS SEQUENCE; GENES, REPORTER; GLYCOSYLATION; HUMANS; ION CHANNEL GATING; PATCH-CLAMP TECHNIQUES; PEPTIDE FRAGMENTS; POINT MUTATION; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; UP-REGULATION;

EID: 4944265229     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2004.08.054     Document Type: Article

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