The metal-ion-dependent adhesion site in the Von Willebrand factor-A domain of α2δ subunits is key to trafficking voltage-gated Ca2+ channels

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

Volumn 102, Issue 32, 2005, Pages 11230-11235

  Canti, C ^a   Nieto Rostro, M ^a   Foucault, I ^a   Heblich, F ^a   Wratten, J ^a   Richards, M W ^a   Hendrich, J ^a   Douglas, L ^a   Page, K M ^a   Davies, A ^a   Dolphin, A C ^a  

^a UNIVERSITY COLLEGE LONDON   (United Kingdom)

Author keywords

Expression; Integrin; Motif; Neuron

Indexed keywords

BARIUM; DIVALENT CATION; GREEN FLUORESCENT PROTEIN; INTEGRIN; METAL ION; SODIUM; VOLTAGE GATED CALCIUM CHANNEL; VON WILLEBRAND FACTOR;

ANIMAL CELL; ARTICLE; CALCIUM CURRENT; CELL STRAIN COS7; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENDOPLASMIC RETICULUM; HETEROLOGOUS EXPRESSION; IMMUNOCYTOCHEMISTRY; INTRACELLULAR TRANSPORT; MUTATION; NONHUMAN; OOCYTE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN GLYCOSYLATION; PURKINJE CELL; XENOPUS;

BINDING SITES; CALCIUM CHANNELS; CATIONS, DIVALENT; DNA, COMPLEMENTARY; ELECTROPHYSIOLOGY; IMMUNOBLOTTING; IMMUNOHISTOCHEMISTRY; IMMUNOPRECIPITATION; METALS; MICROSCOPY, CONFOCAL; MODELS, MOLECULAR; MUTATION; PROTEIN CONFORMATION; VON WILLEBRAND FACTOR;

EID: 23844500323     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0504183102     Document Type: Article

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