ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2001
On the contribution of the first transmembrane domain to whole-cell current through an ATP-gated ionotropic P2X receptor.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 47 citations in OpenAlex.
- Key sites for P2X receptor function and multimerization: overview of mutagenesis studies on a structural basis.Current medicinal chemistry · 2015Review
- Structural and functional properties of the rat P2X4 purinoreceptor extracellular vestibule during gating.Frontiers in cellular neuroscience · 2014Article
- Article
- Ion channels as drug targets in central nervous system disorders.Current medicinal chemistry · 2013Review
- Review
- Allosteric modulation of Ca2+ flux in ligand-gated cation channel (P2X4) by actions on lateral portals.The Journal of biological chemistry · 2012Article
- The intracellular amino terminus plays a dominant role in desensitization of ATP-gated P2X receptor ion channels.The Journal of biological chemistry · 2011Article
- Activation and regulation of purinergic P2X receptor channels.Pharmacological reviews · 2011Review
- Allosteric modulation of ATP-gated P2X receptor channels.Reviews in the neurosciences · 2011Review
- Structural insights into the function of P2X4: an ATP-gated cation channel of neuroendocrine cells.Cellular and molecular neurobiology · 2010Review
- Structural interpretation of P2X receptor mutagenesis studies on drug action.British journal of pharmacology · 2010Review
- New structure enlivens interest in P2X receptors.Trends in pharmacological sciences · 2010Review
- Gated access to the pore of a P2X receptor: structural implications for closed-open transitions.The Journal of biological chemistry · 2010Article
- Functional relevance of aromatic residues in the first transmembrane domain of P2X receptors.Journal of neurochemistry · 2009Article
- Gating the pore of P2X receptor channels.Nature neuroscience · 2008Article
- Identification of P2X(4) receptor transmembrane residues contributing to channel gating and interaction with ivermectin.Pflugers Archiv : European journal of physiology · 2008Article
- Cysteine substitution mutants give structural insight and identify ATP binding and activation sites at P2X receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007Article
- Acidic amino acids impart enhanced Ca2+ permeability and flux in two members of the ATP-gated P2X receptor family.The Journal of general physiology · 2007Article
- Biophysics of P2X receptors.Pflugers Archiv : European journal of physiology · 2006Review
- Secondary structure and gating rearrangements of transmembrane segments in rat P2X4 receptor channels.The Journal of general physiology · 2005Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Scanning cysteine mutagenesis was used to identify potential pore-forming residues in and around the first transmembrane domains of ionotropic P2X(2) receptor subunits. Twenty-eight unique cysteine-substituted mutants (R28C-Y55C) were individually expressed in HEK293 cells by lipofection. Twenty-three of these were functional as assayed by application of ATP to transfected voltage-clamped cells. Individual mutants varied in their sensitivity to ATP; otherwise, currents through functional mutant receptors resembled those of the homomeric wild-type (WT) receptor. In five (H33C, R34C, I50C, K53C, and S54C) of 23 functional mutants, coapplication of 30 microm ATP and 500 nm Ag(+) irreversibly inhibited inward current evoked by subsequent applications of ATP alone. These inhibitions did not result in a lateral shift in the agonist concentration-response curve and are unlikely to involve a modification of the agonist binding site. Two (K53C and S54C) of the five residues modified by Ag(+) applied in the presence of ATP when the channels were gating were also modified by 1 mm (2-aminoethyl)methanethiosulfonate applied in the absence of ATP when the channels were closed. These data suggest that domains near either end of the first transmembrane domain influence ion conduction through the pore of the P2X(2) receptor.
Indexed as
Identifiers
11487611PMC6763184W1499734543What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.