A skeletal muscle ryanodine receptor interaction domain in triadin - Wikidata - wikimedia - TriplyDB

A skeletal muscle ryanodine receptor interaction domain in triadin

A skeletal muscle ryanodine receptor interaction domain in triadin

http://www.wikidata.org/entity/Q34399431

about

The excitation-contraction coupling mechanism in skeletal muscle.A new cytoplasmic interaction between junctin and ryanodine receptor Ca2+ release channels.β1a490-508, a 19-residue peptide from C-terminal tail of Cav1.1 β1a subunit, potentiates voltage-dependent calcium release in adult skeletal muscle fibers.Characterization of Ca(2+)-Dependent Protein-Protein Interactions within the Ca(2+) Release Units of Cardiac Sarcoplasmic Reticulum.Organization of junctional sarcoplasmic reticulum proteins in skeletal muscle fibers.Core skeletal muscle ryanodine receptor calcium release complex.Distinct regions of triadin are required for targeting and retention at the junctional domain of the sarcoplasmic reticulum.Association of FK506 binding proteins with RyR channels - effect of CLIC2 binding on sub-conductance opening and FKBP binding.

P2860

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P2860

A skeletal muscle ryanodine receptor interaction domain in triadin

http://www.wikidata.org/entity/Q34399431

description

2012 nî lūn-bûn

@nan

2012 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

A skeletal muscle ryanodine receptor interaction domain in triadin

@ast

A skeletal muscle ryanodine receptor interaction domain in triadin

@en

A skeletal muscle ryanodine receptor interaction domain in triadin

@nl

type

label

A skeletal muscle ryanodine receptor interaction domain in triadin

@ast

A skeletal muscle ryanodine receptor interaction domain in triadin

@en

A skeletal muscle ryanodine receptor interaction domain in triadin

@nl

prefLabel

A skeletal muscle ryanodine receptor interaction domain in triadin

@ast

A skeletal muscle ryanodine receptor interaction domain in triadin

@en

A skeletal muscle ryanodine receptor interaction domain in triadin

@nl

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P356

JOURNAL.PONE.0043817

P1433

P1476

A skeletal muscle ryanodine receptor interaction domain in triadin

@en

P2093

Elize Wium

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

Nicole A Beard

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

P2860

Interaction of HRC (histidine-rich Ca(2+)-binding protein) and triadin in the lumen of sarcoplasmic reticulum

The role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium.

Complex formation between junctin, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane

Calsequestrin is an inhibitor of skeletal muscle ryanodine receptor calcium release channels

Ablation of triadin causes loss of cardiac Ca2+ release units, impaired excitation-contraction coupling, and cardiac arrhythmias

Junctin is a prominent regulator of contractility in cardiomyocytes

Identification of triadin 1 as the predominant triadin isoform expressed in mammalian myocardium.

Localization and characterization of the calsequestrin-binding domain of triadin 1. Evidence for a charged beta-strand in mediating the protein-protein interaction.

The asp-rich region at the carboxyl-terminus of calsequestrin binds to Ca(2+) and interacts with triadin.

Regulation of the cardiac ryanodine receptor channel by luminal Ca2+ involves luminal Ca2+ sensing sites.

P304

e43817

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scholarly article

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10.1371/JOURNAL.PONE.0043817

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8

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7

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Angela F Dulhunty

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2012-08-24T00:00:00Z

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230769833

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22937102

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3427183

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