Structural interpretation of P2X receptor mutagenesis studies on drug action
about
Molecular and functional properties of P2X receptors--recent progress and persisting challengesManipulation of P2X Receptor Activities by Light StimulationInsights into the channel gating of P2X receptors from structures, dynamics and small moleculesExploring the ATP-binding site of P2X receptorsSize matters in activation/inhibition of ligand-gated ion channelsInsights into the Molecular Mechanisms Underlying Mammalian P2X7 Receptor Functions and Contributions in Diseases, Revealed by Structural Modeling and Single Nucleotide PolymorphismsTightening of the ATP-binding sites induces the opening of P2X receptor channelsExpression, purification, electron microscopy, N-glycosylation mutagenesis and molecular modeling of human P2X4 and Dictyostelium discoideum P2XA.Non-synonymous single nucleotide polymorphisms in the P2X receptor genes: association with diseases, impact on receptor functions and potential use as diagnosis biomarkersFunctional identification of close proximity amino acid side chains within the transmembrane-spanning helixes of the P2X2 receptorAgonist trapped in ATP-binding sites of the P2X2 receptor.Activation and regulation of purinergic P2X receptor channelsGating mechanism of a P2X4 receptor developed from normal mode analysis and molecular dynamics simulationsAgonist binding evokes extensive conformational changes in the extracellular domain of the ATP-gated human P2X1 receptor ion channel.ATP binding site mutagenesis reveals different subunit stoichiometry of functional P2X2/3 and P2X2/6 receptors.Effects of genetic variation in the P2RX7 gene on pharmacodynamics of a P2X(7) receptor antagonist: a prospective genotyping approachFunctional properties of five Dictyostelium discoideum P2X receptorsHeteromeric assembly of P2X subunits.Key sites for P2X receptor function and multimerization: overview of mutagenesis studies on a structural basis.The P2X1 receptor and platelet function.Pharmacological properties of the rhesus macaque monkey P2X7 receptor.Cysteine scanning mutagenesis (residues Glu52-Gly96) of the human P2X1 receptor for ATP: mapping agonist binding and channel gatingP2X receptorsPreparation and characterization of a monoclonal antibody against the refolded and functional extracellular domain of rat P2X4 receptor.2',3'-O-Substituted ATP derivatives as potent antagonists of purinergic P2X3 receptors and potential analgesic agentsThe intracellular amino terminus plays a dominant role in desensitization of ATP-gated P2X receptor ion channels.Molecular basis of selective antagonism of the P2X1 receptor for ATP by NF449 and suramin: contribution of basic amino acids in the cysteine-rich loop.Use of chimeras, point mutants, and molecular modeling to map the antagonist-binding site of 4,4',4″,4‴-(carbonylbis-(imino-5,1,3-benzenetriylbis(carbonylimino)))tetrakisbenzene-1,3-disulfonic acid (NF449) at P2X1 receptors for ATP.P2X receptor chimeras highlight roles of the amino terminus to partial agonist efficacy, the carboxyl terminus to recovery from desensitization, and independent regulation of channel transitionsMass spectrometry analysis of human P2X1 receptors; insight into phosphorylation, modelling and conformational changes.P2X receptor intermediate activation states have altered nucleotide selectivity.
P2860
Q24617046-5A56D043-8E74-4B31-8F19-47145C94B95BQ26765370-6FE4F161-5973-467E-BFC2-BC453F3EE357Q26771359-E9FBFBF2-1E56-491D-8AE3-5D456DC18127Q26852221-44C5D8ED-BC65-4512-80AA-AD7A2144D670Q27008299-5EDC74E4-A974-4CF5-AB78-29F5A72305A9Q27500422-857F3D54-F0FE-4A3B-828F-6F972701AD66Q30513952-C285BAC1-1AA5-4180-A4F5-1B93C87B8140Q34010439-F8A5F57C-C898-4F28-8F8A-56F8B94BF8BAQ34158330-D4E8DD8E-2D69-4319-9033-0963FB3B0621Q34926081-6E8034B2-C9A9-4D39-9D3D-6ED645D5DDFDQ35021846-0FB3197C-DEAE-43DB-A74A-B85CFE7043D0Q35122793-CE55D0ED-EE2E-46A3-B4BA-D83F1F17406CQ35837037-5AD25D7F-C90B-4A1F-986E-08C86BC6BF34Q35849755-F5B29470-40D2-42C5-A587-3913F628B228Q35922295-7FB92805-D8B8-4432-9EBF-F6730C40C6D9Q36779163-89792027-37EF-43B2-8935-D49453C0591DQ37175111-19CE4D86-533D-4C2D-8735-5BA37A8502A2Q38175966-4A98A216-3E55-44F2-909A-4934140B8906Q38273638-69A6FE2C-C2DD-4707-B8A1-E60B0D659BE5Q38306728-D3FF6042-14DB-4DCD-B166-6DAE4D53E5C3Q38650165-EB79A2DF-BB8A-4A43-9587-6B87F7B7E7ECQ38673214-F373FFAE-2C80-4C35-8FB8-E1AC830B3646Q38885828-23418925-51BC-40FC-933E-6DFA726E4344Q39230694-696B30E9-F26D-4FBB-A261-9819EEC29DB5Q39273167-6225F5F6-3A13-40C4-866A-C8ECF6B993F9Q40040884-7D9062A0-632D-4D79-B8C5-2F7B8A56482BQ40725974-1F00F3D6-4496-4EA0-8141-927D3D71AB42Q41893172-F5A2F6E5-988F-4B89-9606-C4834B246B6DQ42005371-86720FC2-EEBC-4B10-9FE3-E39C52D1922BQ42095503-193C2E7A-EB27-4F70-9E95-94D0DF1A3982Q42604461-1A3D0E12-F92B-401B-BB3B-1D0AD2ED150A
P2860
Structural interpretation of P2X receptor mutagenesis studies on drug action
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年学术文章
@wuu
2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
@yue
2010年學術文章
@zh
2010年學術文章
@zh-hant
name
Structural interpretation of P2X receptor mutagenesis studies on drug action
@en
Structural interpretation of P2X receptor mutagenesis studies on drug action.
@nl
type
label
Structural interpretation of P2X receptor mutagenesis studies on drug action
@en
Structural interpretation of P2X receptor mutagenesis studies on drug action.
@nl
prefLabel
Structural interpretation of P2X receptor mutagenesis studies on drug action
@en
Structural interpretation of P2X receptor mutagenesis studies on drug action.
@nl
P2860
P921
P1476
Structural interpretation of P2X receptor mutagenesis studies on drug action
@en
P2093
Richard J Evans
P2860
P304
P356
10.1111/J.1476-5381.2010.00728.X
P407
P577
2010-11-01T00:00:00Z