Identification of Amino Acid Residues Contributing to the ATP-binding Site of a Purinergic P2X Receptor

This publication has 24 references indexed in Scilit:

• A Protein Kinase C Site Highly Conserved in P2X Subunits Controls the Desensitization Kinetics of P2X2 ATP-gated Channels
  Published by Elsevier ,2000
• Single Channel Properties of P2X2 Purinoceptors
  The Journal of general physiology, 1999
• Binding, gating, affinity and efficacy: The interpretation of structure‐activity relationships for agonists and of the effects of mutating receptors
  British Journal of Pharmacology, 1998
• Topological analysis of the ATP-gated ionotrophic P2X₂receptor subunit
  FEBS Letters, 1998
• Identification of amino acid residues contributing to the pore of a P2X receptor
  The EMBO Journal, 1997
• Nucleotide receptors
  Current Opinion in Neurobiology, 1997
• Domains of P2X receptors involved in desensitization
  Proceedings of the National Academy of Sciences, 1996
• The functions and consensus motifs of nine types of peptide segments that form different types of nucleotide‐binding sites
  European Journal of Biochemistry, 1994
• Ion channels: molecular basis of ion selectivity
  FEBS Letters, 1993
• The P-loop — a common motif in ATP- and GTP-binding proteins
  Trends in Biochemical Sciences, 1990