The conformation of calsequestrin determines its ability to regulate skeletal ryanodine receptors.
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Role of Junctin protein interactions in cellular dynamics of calsequestrin polymer upon calcium perturbationReview of RyR1 pathway and associated pathomechanismsAnesthetic- and heat-induced sudden death in calsequestrin-1-knockout miceThe catecholaminergic polymorphic ventricular tachycardia mutation R33Q disrupts the N-terminal structural motif that regulates reversible calsequestrin polymerizationAltered expression of triadin 95 causes parallel changes in localized Ca2+ release events and global Ca2+ signals in skeletal muscle cells in cultureThe excitation-contraction coupling mechanism in skeletal muscle.Cardiac ryanodine receptor activation by a high Ca²⁺ store load is reversed in a reducing cytoplasmic redox environment.A skeletal muscle ryanodine receptor interaction domain in triadinFunctional and structural characterization of a eurytolerant calsequestrin from the intertidal teleost Fundulus heteroclitus.Cyclization of the intrinsically disordered α1S dihydropyridine receptor II-III loop enhances secondary structure and in vitro function.The elusive role of the SPRY2 domain in RyR1.A new cytoplasmic interaction between junctin and ryanodine receptor Ca2+ release channels.C-terminal residues of skeletal muscle calsequestrin are essential for calcium binding and for skeletal ryanodine receptor inhibitionTriadin binding to the C-terminal luminal loop of the ryanodine receptor is important for skeletal muscle excitation contraction coupling.Calcium-dependent inactivation terminates calcium release in skeletal muscle of amphibians.Ryanodine receptor luminal Ca2+ regulation: swapping calsequestrin and channel isoforms.Junctin and triadin each activate skeletal ryanodine receptors but junctin alone mediates functional interactions with calsequestrin.Proteins within the intracellular calcium store determine cardiac RyR channel activity and cardiac output.Functional interaction between calsequestrin and ryanodine receptor in the heart.Regulation of RYR2 by sarcoplasmic reticulum Ca(2+).Organization of junctional sarcoplasmic reticulum proteins in skeletal muscle fibers.Association of FK506 binding proteins with RyR channels - effect of CLIC2 binding on sub-conductance opening and FKBP binding.
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P2860
The conformation of calsequestrin determines its ability to regulate skeletal ryanodine receptors.
description
2006 nî lūn-bûn
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2006 թուականի Մայիսին հրատարակուած գիտական յօդուած
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2006 թվականի մայիսին հրատարակված գիտական հոդված
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2006年の論文
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2006年論文
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2006年論文
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2006年論文
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2006年論文
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2006年論文
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2006年论文
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name
The conformation of calsequest ...... skeletal ryanodine receptors.
@ast
The conformation of calsequest ...... skeletal ryanodine receptors.
@en
The conformation of calsequest ...... skeletal ryanodine receptors.
@nl
type
label
The conformation of calsequest ...... skeletal ryanodine receptors.
@ast
The conformation of calsequest ...... skeletal ryanodine receptors.
@en
The conformation of calsequest ...... skeletal ryanodine receptors.
@nl
prefLabel
The conformation of calsequest ...... skeletal ryanodine receptors.
@ast
The conformation of calsequest ...... skeletal ryanodine receptors.
@en
The conformation of calsequest ...... skeletal ryanodine receptors.
@nl
P2093
P2860
P1433
P1476
The conformation of calsequest ...... skeletal ryanodine receptors.
@en
P2093
Angela F Dulhunty
Magdolna Varsányi
Nicole A Beard
P2860
P304
P356
10.1529/BIOPHYSJ.106.082610
P407
P577
2006-05-12T00:00:00Z