Mutagenesis studies of conserved proline residues of human P2X1 receptors for ATP indicate that proline 272 contributes to channel function

Journal of Neurochemistry

Volumn 92, Issue 5, 2005, Pages 1256-1264

  Roberts, Jonathan A ^a   Evans, Richard J ^a  

^a UNIVERSITY OF LEICESTER   (United Kingdom)

Author keywords

ATP; Electrophysiology; Mutagenesis; P2X receptor; Proline

Indexed keywords

2',3' O (2,4,6 TRINITROPHENYL)ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE DERIVATIVE; MUTANT PROTEIN; PROLINE; PURINE P2X1 RECEPTOR; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; BINDING AFFINITY; CELL SURFACE; EXTRACELLULAR SPACE; FEMALE; MUTAGENESIS; MUTANT; NONHUMAN; OOCYTE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; RECEPTOR BINDING; VOLTAGE CLAMP; WILD TYPE; XENOPUS;

ADENOSINE TRIPHOSPHATE; ANIMALS; CONSERVED SEQUENCE; DOSE-RESPONSE RELATIONSHIP, DRUG; DRUG INTERACTIONS; EXTRACELLULAR SPACE; GENE EXPRESSION REGULATION; HUMANS; MEMBRANE POTENTIALS; MUTAGENESIS; OOCYTES; PATCH-CLAMP TECHNIQUES; PROLINE; RECEPTORS, PURINERGIC P2; SEQUENCE ALIGNMENT; XENOPUS LAEVIS;

EID: 14844335685     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2004.02960.x     Document Type: Article

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