Cysteine substitution mutants give structural insight and identify ATP binding and activation sites at P2X receptors.
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Exploring the ATP-binding site of P2X receptorsPrinciples and properties of ion flow in P2X receptorsMolecular mechanism of ATP binding and ion channel activation in P2X receptorsRole of the domain encompassing Arg304-Ile328 in rat P2X2 receptor conformation revealed by alterations in complex glycosylation at Asn298A histidine scan to probe the flexibility of the rat P2X2 receptor zinc-binding siteA mechanism of intracellular P2X receptor activation.P2X receptors: dawn of the post-structure era.A putative extracellular salt bridge at the subunit interface contributes to the ion channel function of the ATP-gated P2X2 receptorRegulation of ATP-gated P2X channels: from redox signaling to interactions with other proteinsExpression, purification, electron microscopy, N-glycosylation mutagenesis and molecular modeling of human P2X4 and Dictyostelium discoideum P2XA.Covalent modification of mutant rat P2X2 receptors with a thiol-reactive fluorophore allows channel activation by zinc or acidic pH without ATP.Identification of functionally important residues of the rat P2X4 receptor by alanine scanning mutagenesis of the dorsal fin and left flipper domains.Multiple roles of the extracellular vestibule amino acid residues in the function of the rat P2X4 receptor.Agonist trapped in ATP-binding sites of the P2X2 receptor.Activation and regulation of purinergic P2X receptor channelsAgonist binding evokes extensive conformational changes in the extracellular domain of the ATP-gated human P2X1 receptor ion channel.Involvement of the cysteine-rich head domain in activation and desensitization of the P2X1 receptor.Cysteine substitution mutagenesis and the effects of methanethiosulfonate reagents at P2X2 and P2X4 receptors support a core common mode of ATP action at P2X receptors.Allosteric modulation of ATP-gated P2X receptor channelsThe P2X1 ion channel in platelet function.New structure enlivens interest in P2X receptors.Structural interpretation of P2X receptor mutagenesis studies on drug actionKey sites for P2X receptor function and multimerization: overview of mutagenesis studies on a structural basis.Cysteine scanning mutagenesis (residues Glu52-Gly96) of the human P2X1 receptor for ATP: mapping agonist binding and channel gatingP2X Receptor Activation.Ectodomain lysines and suramin block of P2X1 receptors.Characterisation of ATP analogues to cross-link and label P2X receptorsContribution of the region Glu181 to Val200 of the extracellular loop of the human P2X1 receptor to agonist binding and gating revealed using cysteine scanning mutagenesis.Mass spectrometry analysis of human P2X1 receptors; insight into phosphorylation, modelling and conformational changes.Characterisation of the R276A gain-of-function mutation in the ectodomain of murine P2X7Regions of the amino terminus of the P2X receptor required for modification by phorbol ester and mGluR1alpha receptors.Functional and structural identification of amino acid residues of the P2X2 receptor channel critical for the voltage- and [ATP]-dependent gating.
P2860
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P2860
Cysteine substitution mutants give structural insight and identify ATP binding and activation sites at P2X receptors.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh
2007年學術文章
@zh-hant
name
Cysteine substitution mutants ...... vation sites at P2X receptors.
@ast
Cysteine substitution mutants ...... vation sites at P2X receptors.
@en
type
label
Cysteine substitution mutants ...... vation sites at P2X receptors.
@ast
Cysteine substitution mutants ...... vation sites at P2X receptors.
@en
prefLabel
Cysteine substitution mutants ...... vation sites at P2X receptors.
@ast
Cysteine substitution mutants ...... vation sites at P2X receptors.
@en
P2860
P1476
Cysteine substitution mutants ...... vation sites at P2X receptors.
@en
P2093
Jonathan A Roberts
Richard J Evans
P2860
P304
P356
10.1523/JNEUROSCI.2310-06.2007
P407
P577
2007-04-01T00:00:00Z