Dependence of Purinergic P2X Receptor Activity on Ectodomain Structure
Open Access
- 1 March 2003
- journal article
- Published by Elsevier BV
- Vol. 278 (12), 10182-10188
- https://doi.org/10.1074/jbc.m209094200
Abstract
No abstract availableThis publication has 40 references indexed in Scilit:
- Heteromultimerization Modulates P2X Receptor Functions through Participating Extracellular and C-terminal SubdomainsPublished by Elsevier BV ,2002
- Purinergic P2X2 Receptor Desensitization Depends on Coupling between Ectodomain and C-Terminal DomainMolecular Pharmacology, 2002
- Mechanism of glutamate receptor desensitizationNature, 2002
- Molecular Physiology of P2X ReceptorsPhysiological Reviews, 2002
- Mechanisms for ligand binding to GluR0 ion channels: crystal structures of the glutamate and serine complexes and a closed apo stateJournal of Molecular Biology, 2001
- Identification of Amino Acid Residues Contributing to the ATP-binding Site of a Purinergic P2X ReceptorPublished by Elsevier BV ,2000
- Mechanisms for Activation and Antagonism of an AMPA-Sensitive Glutamate ReceptorNeuron, 2000
- The Role of Positively Charged Amino Acids in ATP Recognition by Human P2X1 ReceptorsPublished by Elsevier BV ,2000
- Nucleotide receptorsCurrent Opinion in Neurobiology, 1997
- A study of the ‘desensitization’ produced by acetylcholine at the motor end‐plateThe Journal of Physiology, 1957