Atomic force microscopy imaging demonstrates that P2X2 receptors are trimers but that P2X6 receptor subunits do not oligomerize - Wikidata - awgldk - TriplyDB

Atomic force microscopy imaging demonstrates that P2X2 receptors are trimers but that P2X6 receptor subunits do not oligomerize

Atomic force microscopy imaging demonstrates that P2X2 receptors are trimers but that P2X6 receptor subunits do not oligomerize

http://www.wikidata.org/entity/Q28303030

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Atomic force microscopy (AFM) imaging suggests that stromal interaction molecule 1 (STIM1) binds to Orai1 with sixfold symmetry Molecular and functional properties of P2X receptors--recent progress and persisting challenges Analysis of assembly and trafficking of native P2X4 and P2X7 receptor complexes in rodent immune cells Crystal structure of the ATP-gated P2X(4) ion channel in the closed state The role of purinergic receptors in stem cell differentiation Insights into the channel gating of P2X receptors from structures, dynamics and small molecules Principles and properties of ion flow in P2X receptors Filming biomolecular processes by high-speed atomic force microscopy Age-related nuclear translocation of P2X6 subunit modifies splicing activity interacting with splicing factor 3A1 Direct observation of ATP-induced conformational changes in single P2X(4) receptors P2X6 Knockout Mice Exhibit Normal Electrolyte Homeostasis Atomic force microscopy reveals the architecture of the epithelial sodium channel (ENaC)Identification of P2X2/P2X4/P2X6 heterotrimeric receptors using atomic force microscopy (AFM) imaging The stoichiometry of P2X2/6 receptor heteromers depends on relative subunit expression levels Sp1/3 and NF-1 mediate basal transcription of the human P2X1 gene in megakaryoblastic MEG-01 cells.P2X receptors: dawn of the post-structure era.Gated access to the pore of a P2X receptor: structural implications for closed-open transitions.Neuromodulation by extracellular ATP and P2X receptors in the CNS.Atomic force microscopy reveals the stoichiometry and subunit arrangement of 5-HT3 receptors.Regulation of ATP-gated P2X channels: from redox signaling to interactions with other proteins Expression, purification, electron microscopy, N-glycosylation mutagenesis and molecular modeling of human P2X4 and Dictyostelium discoideum P2XA.Atomic force microscopy reveals the alternating subunit arrangement of the TRPP2-TRPV4 heterotetramer.Distinct annular oligomers captured along the assembly and disassembly pathways of transthyretin amyloid protofibrils Covalent modification of mutant rat P2X2 receptors with a thiol-reactive fluorophore allows channel activation by zinc or acidic pH without ATP.A C-terminal lysine that controls human P2X4 receptor desensitization.The penultimate arginine of the carboxyl terminus determines slow desensitization in a P2X receptor from the cattle tick Boophilus microplus Activation and regulation of purinergic P2X receptor channels A truncation variant of the cation channel P2RX5 is upregulated during T cell activation.Association of the endosomal sorting complex ESCRT-II with the Vps20 subunit of ESCRT-III generates a curvature-sensitive complex capable of nucleating ESCRT-III filaments ATP binding site mutagenesis reveals different subunit stoichiometry of functional P2X2/3 and P2X2/6 receptors.Acidic amino acids impart enhanced Ca2+ permeability and flux in two members of the ATP-gated P2X receptor family.Allosteric nature of P2X receptor activation probed by photoaffinity labelling.Comparative study of the P2X gene family in animals and plants.Voltage- and [ATP]-dependent gating of the P2X(2) ATP receptor channel.Gating the pore of P2X receptor channels Assembly and trafficking of P2X purinergic receptors (Review).The trafficking and targeting of P2X receptors.P2X1 and P2X5 subunits form the functional P2X receptor in mouse cortical astrocytes.Dynamic aspects of functional regulation of the ATP receptor channel P2X2.New structure enlivens interest in P2X receptors.

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P2860

Atomic force microscopy imaging demonstrates that P2X2 receptors are trimers but that P2X6 receptor subunits do not oligomerize

http://www.wikidata.org/entity/Q28303030

description

2005 nî lūn-bûn

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2005 թուականի Մարտին հրատարակուած գիտական յօդուած

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2005 թվականի մարտին հրատարակված գիտական հոդված

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2005年の論文

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年學術文章

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name

Atomic force microscopy imagin ...... or subunits do not oligomerize

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Atomic force microscopy imagin ...... or subunits do not oligomerize

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Atomic force microscopy imagin ...... or subunits do not oligomerize

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type

label

Atomic force microscopy imagin ...... or subunits do not oligomerize

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Atomic force microscopy imagin ...... or subunits do not oligomerize

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Atomic force microscopy imagin ...... or subunits do not oligomerize

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prefLabel

Atomic force microscopy imagin ...... or subunits do not oligomerize

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Atomic force microscopy imagin ...... or subunits do not oligomerize

@en

Atomic force microscopy imagin ...... or subunits do not oligomerize

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P1433

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P2860

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P1433

Journal of Biological Chemistry

P1476

Atomic force microscopy imagin ...... or subunits do not oligomerize

@en

P2093

J Michael Edwardson

http://www.w3.org/2001/XMLSchema#string

Nelson P Barrera

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Robert M Henderson

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Ruth D Murrell-Lagnado

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Susan J Ormond

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P2860

Trimeric architecture of homomeric P2X2 and heteromeric P2X1+2 receptor subtypes

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

Single channel properties of P2X2 purinoceptors

Hetero-oligomeric assembly of P2X receptor subunits. Specificities exist with regard to possible partners

Molecular physiology of P2X receptors

Identification of a trafficking motif involved in the stabilization and polarization of P2X receptors

Stoichiometry of a ligand-gated ion channel determined by fluorescence energy transfer.

Translocation-independent dimerization of the EcoKI endonuclease visualized by atomic force microscopy.

Which GABAA-receptor subtypes really occur in the brain?

Topological analysis of the ATP-gated ionotropic [correction of ionotrophic] P2X2 receptor subunit.

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10759-65

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scholarly article

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1079534

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P356

10.1074/JBC.M412265200

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P407

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11

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280

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15657042

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