Structural and Electrostatic Properties of the 5-HT3Receptor Pore Revealed by Substituted Cysteine Accessibility Mutagenesis
Open Access
- 1 November 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (45), 42035-42042
- https://doi.org/10.1074/jbc.m106066200
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- Conversion of the Ion Selectivity of the 5-HT3AReceptor from Cationic to Anionic Reveals a Conserved Feature of the Ligand-gated Ion Channel SuperfamilyPublished by Elsevier ,2001
- Diltiazem causes open channel block of recombinant 5‐HT3 receptorsThe Journal of Physiology, 1999
- Spatial structure of the M2 transmembrane segment of the nicotinic acetylcholine receptor α-subunitFEBS Letters, 1999
- Contribution of the β Subunit M2 Segment to the Ion-Conducting Pathway of the Acetylcholine ReceptorBiochemistry, 1998
- Volatile general anaesthetic actions on recombinant nAChα7, 5‐HT3 and chimeric nAChα7‐5‐HT3 receptors expressed in Xenopus oocytesBritish Journal of Pharmacology, 1997
- Histidine 225, a Residue of the NhaA-Na+/H+ Antiporter of Escherichia coli Is Exposed and Faces the Cell ExteriorPublished by Elsevier ,1997
- Identification of channel-lining residues in the M2 membrane-spanning segment of the GABA(A) receptor alpha1 subunit.The Journal of general physiology, 1996
- Channel gating governed symmetrically by conserved leucine residues in the M2 domain of nicotinic receptorsNature, 1995
- Mapping the binding-site crevice of the dopamine D2 receptor by the substituted-cysteine accessibility methodNeuron, 1995
- Nicotinic Acetylcholine Receptor an 9 Å ResolutionJournal of Molecular Biology, 1993