Involvement of the cysteine-rich head domain in activation and desensitization of the P2X1 receptor. - Wikidata - awgldk - TriplyDB

Involvement of the cysteine-rich head domain in activation and desensitization of the P2X1 receptor.

Involvement of the cysteine-rich head domain in activation and desensitization of the P2X1 receptor.

http://www.wikidata.org/entity/Q36094216

about

Insights into the channel gating of P2X receptors from structures, dynamics and small molecules Exploring the ATP-binding site of P2X receptors Solution structure of the rat P2X4 receptor head domain involved in inhibitory metal binding.Imaging P2X4 receptor subcellular distribution, trafficking, and regulation using P2X4-pHluorin Neuromodulation by extracellular ATP and P2X receptors in the CNS.Regulation of ATP-gated P2X channels: from redox signaling to interactions with other proteins Identification of functionally important residues of the rat P2X4 receptor by alanine scanning mutagenesis of the dorsal fin and left flipper domains.Inherent dynamics of head domain correlates with ATP-recognition of P2X4 receptors: insights gained from molecular simulations.Role of domain calcium in purinergic P2X2 receptor channel desensitization Photo-switchable tweezers illuminate pore-opening motions of an ATP-gated P2X ion channel A Highly Conserved Salt Bridge Stabilizes the Kinked Conformation of β2,3-Sheet Essential for Channel Function of P2X4 Receptors The α2δ-1 subunit remodels CaV1.2 voltage sensors and allows Ca2+ influx at physiological membrane potentials Inter- and intrasubunit interactions between transmembrane helices in the open state of P2X receptor channels.P2X receptors as drug targets.Novel approaches to drug design for the treatment of schizophrenia.Desensitization properties of P2X3 receptors shaping pain signaling.Heteromeric assembly of P2X subunits.Key sites for P2X receptor function and multimerization: overview of mutagenesis studies on a structural basis.P2X Receptor Activation.A rare P2X7 variant Arg307Gln with absent pore formation function protects against neuroinflammation in multiple sclerosis.Inter-subunit disulfide locking of the human P2X3 receptor elucidates ectodomain movements associated with channel gating Mechanistic insights from resolving ligand-dependent kinetics of conformational changes at ATP-gated P2X1R ion channels.Conformational flexibility of the agonist binding jaw of the human P2X3 receptor is a prerequisite for channel opening.Mass spectrometry analysis of human P2X1 receptors; insight into phosphorylation, modelling and conformational changes.Intermediate closed channel state(s) precede(s) activation in the ATP-gated P2X2 receptor.Structural insights into the competitive inhibition of the ATP-gated P2X receptor channel The Dynamic Behavior of the P2X4 Ion Channel in the Closed Conformation.Intersubunit physical couplings fostered by the left flipper domain facilitate channel opening of P2X4 receptors.Druggable negative allosteric site of P2X3 receptors.Opposing Roles of Calcium and Intracellular ATP on Gating of the Purinergic P2X2 Receptor Channel.

P2860

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P2860

Involvement of the cysteine-rich head domain in activation and desensitization of the P2X1 receptor.

http://www.wikidata.org/entity/Q36094216

description

2012 nî lūn-bûn

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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2012年论文

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2012年论文

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name

Involvement of the cysteine-ri ...... tization of the P2X1 receptor.

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Involvement of the cysteine-ri ...... tization of the P2X1 receptor.

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type

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Involvement of the cysteine-ri ...... tization of the P2X1 receptor.

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Involvement of the cysteine-ri ...... tization of the P2X1 receptor.

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Involvement of the cysteine-ri ...... tization of the P2X1 receptor.

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Involvement of the cysteine-ri ...... tization of the P2X1 receptor.

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PNAS.1118759109

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Proceedings of the National Academy of Sciences of the United States of America

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Involvement of the cysteine-ri ...... itization of the P2X1 receptor

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Alonso Barrantes-Freer

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Annette Nicke

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Jürgen Rettinger

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Karina Kaczmarek-Hájek

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Stephen F Marino

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Thomas Grutter

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Éva Lörinczi

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P2860

P2X1 and P2X3 receptors form stable trimers: a novel structural motif of ligand-gated ion channels.

Crystal structure of the ATP-gated P2X(4) ion channel in the closed state

Molecular mechanism of ATP binding and ion channel activation in P2X receptors

AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading

Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

Comparative protein modelling by satisfaction of spatial restraints

Signaling at purinergic P2X receptors

Identification of an intersubunit cross-link between substituted cysteine residues located in the putative ATP binding site of the P2X1 receptor

Tightening of the ATP-binding sites induces the opening of P2X receptor channels

Conserved cysteine residues in the extracellular loop of the human P2X(1) receptor form disulfide bonds and are involved in receptor trafficking to the cell surface.

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11396-11401

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10.1073/PNAS.1118759109

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28

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109

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Sébastien Dutertre

Yogesh Bhargava

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2012-06-27T00:00:00Z

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