An Arg307 to Gln Polymorphism within the ATP-binding Site Causes Loss of Function of the Human P2X7 Receptor
Open Access
- 1 July 2004
- journal article
- Published by Elsevier
- Vol. 279 (30), 31287-31295
- https://doi.org/10.1074/jbc.m313902200
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- P2X7 Receptor Cell Surface Expression and Cytolytic Pore Formation Are Regulated by a Distal C-terminal RegionJournal of Biological Chemistry, 2003
- Functional evidence of distinct ATP activation sites at the human P2X7 receptorThe Journal of Physiology, 2001
- Differential Assembly of Rat Purinergic P2X7 Receptor in Immune Cells of the Brain and PeripheryPublished by Elsevier ,2001
- A Glu-496 to Ala Polymorphism Leads to Loss of Function of the Human P2X7 ReceptorJournal of Biological Chemistry, 2001
- Identification of Amino Acid Residues Contributing to the ATP-binding Site of a Purinergic P2X ReceptorJournal of Biological Chemistry, 2000
- The Role of Positively Charged Amino Acids in ATP Recognition by Human P2X1 ReceptorsPublished by Elsevier ,2000
- SAPK/JNK activation and apoptotic induction by the macrophage P2X7 nucleotide receptorJournal of Biological Chemistry, 2000
- Structural Motif and Characteristics of the Extracellular Domain of P2XReceptorsBiochemical and Biophysical Research Communications, 1997
- Extracellular ATP causes loss of L-selectin from human lymphocytes via occupancy of P2Z purinoceptorsJournal of Cellular Physiology, 1996
- ATP-induced pore formation in the plasma membrane of rat peritoneal mast cells.The Journal of general physiology, 1990