Conserved cysteine residues in the extracellular loop of the human P2X1 receptor form disulfide bonds and are involved in receptor trafficking to the cell surface

Molecular Pharmacology

Volumn 61, Issue 2, 2002, Pages 303-311

  Ennion, Steven J ^a   Evans, Richard J ^a  

^a UNIVERSITY OF LEICESTER   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BIOTIN; CYSTEINE; ION CHANNEL; PURINE P2X RECEPTOR; SULFONIC ACID DERIVATIVE;

ANIMAL TISSUE; ARTICLE; BIOTINYLATION; CELL TRANSPORT; CONTROLLED STUDY; DISULFIDE BOND; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; XENOPUS LAEVIS;

ADENOSINE TRIPHOSPHATE; ALANINE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BIOLOGICAL TRANSPORT; BIOTIN; BIOTINYLATION; CONSERVED SEQUENCE; CYSTEINE; DISULFIDES; DITHIOTHREITOL; ELECTROPHYSIOLOGY; HUMANS; MEMBRANE PROTEINS; MERCAPTOETHANOL; MOLECULAR SEQUENCE DATA; MUTATION; OOCYTES; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, PURINERGIC P2; REDUCING AGENTS; SEQUENCE HOMOLOGY, AMINO ACID; XENOPUS LAEVIS;

EID: 0036154216     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: 10.1124/mol.61.2.303     Document Type: Article

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