An Aspartic Acid Residue Near the Second Transmembrane Segment of ATP Receptor/ Channel Regulates Agonist Sensitivity
- 17 March 1998
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 244 (2) , 599-603
- https://doi.org/10.1006/bbrc.1998.8312
Abstract
No abstract availableKeywords
Funding Information
- Ministry of Education, Culture, Sports, Science and Technology
- Ministry of Health, Labour and Welfare
This publication has 17 references indexed in Scilit:
- P2x receptors bring new structure to ligand-gated ion channelsPublished by Elsevier ,1999
- Identification of amino acid residues contributing to the pore of a P2X receptorThe EMBO Journal, 1997
- Effects of neuroamines and divalent cations on cloned and mutated ATP-gated channelsEuropean Journal of Pharmacology, 1997
- Domains of P2X receptors involved in desensitizationProceedings of the National Academy of Sciences, 1996
- Purinergic receptors: their role in nociception and primary afferent neurotransmissionCurrent Opinion in Neurobiology, 1996
- The Cytolytic P 2Z Receptor for Extracellular ATP Identified as a P 2X Receptor (P2X 7 )Science, 1996
- Cloning OF P2X5 and P2X6 receptors and the distribution and properties of an extended family of ATP-gated ion channelsJournal of Neuroscience, 1996
- Block by apomorphine of acetylcholine receptor channels expressed in Xenopus oocytesEuropean Journal of Pharmacology: Molecular Pharmacology, 1994
- New structural motif for ligand-gated ion channels defined by an ionotropic ATP receptorNature, 1994
- A new class of ligand-gated ion channel defined by P2X receptor for extracellular ATPNature, 1994