Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP. - Wikidata - awgldk - TriplyDB

Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.

Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.

http://www.wikidata.org/entity/Q34171452

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Regulation of the cardiac muscle ryanodine receptor by glutathione transferases Characterization of the molecular architecture of human caveolin-3 and interaction with the skeletal muscle ryanodine receptor Single-Particle Cryo-EM of the Ryanodine Receptor Channel in an Aqueous Environment Coordinated movement of cytoplasmic and transmembrane domains of RyR1 upon gating Disease mutations in the ryanodine receptor N-terminal region couple to a mobile intersubunit interface Structural Basis for Gating and Activation of RyR1.Dynamic, inter-subunit interactions between the N-terminal and central mutation regions of cardiac ryanodine receptor Subnanometer-resolution electron cryomicroscopy-based domain models for the cytoplasmic region of skeletal muscle RyR channel Catecholaminergic polymorphic ventricular tachycardia is caused by mutation-linked defective conformational regulation of the ryanodine receptor.Structure of glutaraldehyde cross-linked ryanodine receptor Imaging single cardiac ryanodine receptor Ca2+ fluxes in lipid bilayers.Interdomain interactions within ryanodine receptors regulate Ca2+ spark frequency in skeletal muscle.Localization of an NH(2)-terminal disease-causing mutation hot spot to the "clamp" region in the three-dimensional structure of the cardiac ryanodine receptor.Calcium transport across the sarcoplasmic reticulum: structure and function of Ca2+-ATPase and the ryanodine receptor.Ryanodine receptors: structure, expression, molecular details, and function in calcium release.Structure of the voltage-gated L-type Ca2+ channel by electron cryomicroscopy Three-dimensional structure of the type 1 inositol 1,4,5-trisphosphate receptor at 24 A resolution.Structural mapping of divergent regions in the type 1 ryanodine receptor using fluorescence resonance energy transfer.The skeletal muscle Ca2+ release channel has an oxidoreductase-like domain Structure of Ca2+ release channel at 14 A resolution.The pore structure of the closed RyR1 channel.Modulation of the oligomerization of isolated ryanodine receptors by their functional states Three-dimensional visualization of FKBP12.6 binding to an open conformation of cardiac ryanodine receptor Calcium and arrhythmogenesis.Single-particle cryo-EM of the ryanodine receptor channel in an aqueous environment.Three-dimensional reconstruction of the recombinant type 3 ryanodine receptor and localization of its amino terminus Evolution of skeletal type e-c coupling: a novel means of controlling calcium delivery.Identification of ATP-binding regions in the RyR1 Ca²⁺ release channel.Ligand-dependent conformational changes in the clamp region of the cardiac ryanodine receptor.CLIC2-RyR1 interaction and structural characterization by cryo-electron microscopy.Ryanodine receptor-mediated arrhythmias and sudden cardiac death.Structural insights into Ca(2+)-activated long-range allosteric channel gating of RyR1.Ryanodine receptor structure: progress and challenges.Sarcoplasmic reticulum function in smooth muscle.The structural biology of ryanodine receptors.Calcium signaling in cardiac myocytes.ARVC-related mutations in divergent region 3 alter functional properties of the cardiac ryanodine receptor.All three ryanodine receptor isoforms generate rapid cooling responses in muscle cells.Three-dimensional localization of divergent region 3 of the ryanodine receptor to the clamp-shaped structures adjacent to the FKBP binding sites.The N-Terminal Region of the Ryanodine Receptor Affects Channel Activation.

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P2860

Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.

http://www.wikidata.org/entity/Q34171452

description

1999 nî lūn-bûn

@nan

1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1999 թվականի հոտեմբերին հրատարակված գիտական հոդված

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年论文

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name

Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.

@ast

Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.

@en

Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.

@nl

type

label

Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.

@ast

Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.

@en

Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.

@nl

prefLabel

Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.

@ast

Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.

@en

Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.

@nl

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P1476

Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.

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P2093

I I Serysheva

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

M Schatz

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M van Heel

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S L Hamilton

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W Chiu

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P2860

FK506 binding protein associated with the calcium release channel (ryanodine receptor)

Molecular cloning of cDNA encoding human and rabbit forms of the Ca2+ release channel (ryanodine receptor) of skeletal muscle sarcoplasmic reticulum

A new generation of the IMAGIC image processing system

Heterogeneity of Ca2+ gating of skeletal muscle and cardiac ryanodine receptors.

Electrophysiological effects of ryanodine derivatives on the sheep cardiac sarcoplasmic reticulum calcium-release channel

Desensitization of the skeletal muscle ryanodine receptor: evidence for heterogeneity of calcium release channels

Primary structure and expression from complementary DNA of skeletal muscle ryanodine receptor.

Ryanodine as a functional probe of the skeletal muscle sarcoplasmic reticulum Ca2+ release channel.

Densely packed beta-structure at the protein-lipid interface of porin is revealed by high-resolution cryo-electron microscopy.

Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle.

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