Contribution of conserved glycine residues to ATP action at human P2X 1 receptors: Mutagenesis indicates that the glycine at position 250 is important for channel function

Journal of Neurochemistry

Volumn 95, Issue 6, 2005, Pages 1746-1754

  Digby, Helen R ^a   Roberts, Jonathan A ^a   Sutcliffe, Michael J ^a   Evans, Richard J ^a  

^a UNIVERSITY OF LEICESTER   (United Kingdom)

Author keywords

ATP; Glycine; Mutagenesis; P2X receptor

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALANINE; ASPARAGINE; ASPARTIC ACID; CYSTEINE; GLYCINE; ISOLEUCINE; LYSINE; MUTANT PROTEIN; PHENYLALANINE; PROLINE; PURINE P2X RECEPTOR; PURINE P2X1 RECEPTOR;

AMINO ACID SUBSTITUTION; AMPLITUDE MODULATION; ARTICLE; CONTROLLED STUDY; DOSE TIME EFFECT RELATION; GENE MUTATION; HUMAN; HUMAN CELL; MUTAGENESIS; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN MOTIF; PROTEIN SECONDARY STRUCTURE; XENOPUS;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BLOTTING, WESTERN; ELECTROPHYSIOLOGY; EXTRACELLULAR SPACE; GLYCINE; HUMANS; ION CHANNELS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OOCYTES; PATCH-CLAMP TECHNIQUES; RECEPTORS, PURINERGIC P2; SERINE; XENOPUS;

EID: 29144521525     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2005.03494.x     Document Type: Article

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