Residues 155 and 348 contribute to the determination of P2X7 receptor function via distinct mechanisms revealed by single-nucleotide polymorphisms.
about
Molecular and functional properties of P2X receptors--recent progress and persisting challengesInsights into the Molecular Mechanisms Underlying Mammalian P2X7 Receptor Functions and Contributions in Diseases, Revealed by Structural Modeling and Single Nucleotide PolymorphismsGenetically dissecting P2rx7 expression within the central nervous system using conditional humanized mice.Gain and loss of function of P2X7 receptors: mechanisms, pharmacology and relevance to diabetic neuropathic pain.Non-synonymous single nucleotide polymorphisms in the P2X receptor genes: association with diseases, impact on receptor functions and potential use as diagnosis biomarkersThe second transmembrane domain of P2X7 contributes to dilated pore formationHaplotypes of P2RX7 gene polymorphisms are associated with both cold pain sensitivity and analgesic effect of fentanyl.Genetically determined P2X7 receptor pore formation regulates variability in chronic pain sensitivity.Structure-based identification and characterisation of structurally novel human P2X7 receptor antagonistsPurinergic signalling: Its unpopular beginning, its acceptance and its exciting future.Key sites for P2X receptor function and multimerization: overview of mutagenesis studies on a structural basis.Pharmacological properties of the rhesus macaque monkey P2X7 receptor.Safety and Efficacy of an Oral Inhibitor of the Purinergic Receptor P2X7 in Adult Patients with Moderately to Severely Active Crohn's Disease: A Randomized Placebo-controlled, Double-blind, Phase IIa Study.Searching Novel Therapeutic Targets for Scleroderma: P2X7-Receptor Is Up-regulated and Promotes a Fibrogenic Phenotype in Systemic Sclerosis Fibroblasts.ATP-induced P2X Receptor-Dependent Large Pore Formation: How Much Do We Know?Conformational changes during human P2X7 receptor activation examined by structural modelling and cysteine-based cross-linking studies.Zinc inactivates melastatin transient receptor potential 2 channels via the outer pore.The P2X7 receptor as a route for non-exocytotic glutamate release: dependence on the carboxyl tail.The P2X7 Receptor.MED1101: a new dialdehydic compound regulating P2×7 receptor cell surface expression in U937 cells.Purinergic Receptors in Neurological Diseases With Motor Symptoms: Targets for Therapy.The purinergic P2×7 receptor is expressed on monocytes in Behçet's disease and is modulated by TNF-α
P2860
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P2860
Residues 155 and 348 contribute to the determination of P2X7 receptor function via distinct mechanisms revealed by single-nucleotide polymorphisms.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年学术文章
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2011年学术文章
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2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
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2011年學術文章
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2011年學術文章
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name
Residues 155 and 348 contribut ...... ngle-nucleotide polymorphisms.
@en
Residues 155 and 348 contribut ...... ngle-nucleotide polymorphisms.
@en-gb
Residues 155 and 348 contribut ...... ngle-nucleotide polymorphisms.
@nl
type
label
Residues 155 and 348 contribut ...... ngle-nucleotide polymorphisms.
@en
Residues 155 and 348 contribut ...... ngle-nucleotide polymorphisms.
@en-gb
Residues 155 and 348 contribut ...... ngle-nucleotide polymorphisms.
@nl
prefLabel
Residues 155 and 348 contribut ...... ngle-nucleotide polymorphisms.
@en
Residues 155 and 348 contribut ...... ngle-nucleotide polymorphisms.
@en-gb
Residues 155 and 348 contribut ...... ngle-nucleotide polymorphisms.
@nl
P2093
P2860
P50
P356
P1476
Residues 155 and 348 contribut ...... ngle-nucleotide polymorphisms.
@en
P2093
Brian Johnson
G Ranjan Goli
Helen J Bradley
Jocelyn M Baldwin
P2860
P304
P356
10.1074/JBC.M110.211284
P407
P577
2011-01-04T00:00:00Z