Negatively charged amino acids within the intraluminal loop of ryanodine receptor are involved in the interaction with triadin. - Wikidata - wikimedia - TriplyDB

Negatively charged amino acids within the intraluminal loop of ryanodine receptor are involved in the interaction with triadin.

Negatively charged amino acids within the intraluminal loop of ryanodine receptor are involved in the interaction with triadin.

http://www.wikidata.org/entity/Q34279088

about

Absence of triadin, a protein of the calcium release complex, is responsible for cardiac arrhythmia with sudden death in human Junctin - the quiet achiever Review of RyR1 pathway and associated pathomechanisms AAV-mediated knock-down of HRC exacerbates transverse aorta constriction-induced heart failure Triadin (Trisk 95) overexpression blocks excitation-contraction coupling in rat skeletal myotubes A structural model of the pore-forming region of the skeletal muscle ryanodine receptor (RyR1)A model of the putative pore region of the cardiac ryanodine receptor channel Probing the role of negatively charged amino acid residues in ion permeation of skeletal muscle ryanodine receptor A skeletal muscle ryanodine receptor interaction domain in triadin On the footsteps of Triadin and its role in skeletal muscle Retrograde regulation of STIM1-Orai1 interaction and store-operated Ca2+ entry by calsequestrin.Triadin binding to the C-terminal luminal loop of the ryanodine receptor is important for skeletal muscle excitation contraction coupling.Exon skipping as a therapeutic strategy applied to an RYR1 mutation with pseudo-exon inclusion causing a severe core myopathy.Altered stored calcium release in skeletal myotubes deficient of triadin and junctin.Junctin and triadin each activate skeletal ryanodine receptors but junctin alone mediates functional interactions with calsequestrin.Triadin: what possible function 20 years later?Functional Characterization of a Central Core Disease RyR1 Mutation (p.Y4864H) Associated with Quantitative Defect in RyR1 Protein.A chemical chaperone improves muscle function in mice with a RyR1 mutation.Proteins within the intracellular calcium store determine cardiac RyR channel activity and cardiac output.Characterization of Ca(2+)-Dependent Protein-Protein Interactions within the Ca(2+) Release Units of Cardiac Sarcoplasmic Reticulum.Calsequestrin interacts directly with the cardiac ryanodine receptor luminal domain.A guide to the 3D structure of the ryanodine receptor type 1 by cryoEM.Core skeletal muscle ryanodine receptor calcium release complex.Silencing genes of sarcoplasmic reticulum proteins clarifies their roles in excitation-contraction coupling.Knocking down type 2 but not type 1 calsequestrin reduces calcium sequestration and release in C2C12 skeletal muscle myotubes.Triadins are not triad-specific proteins: two new skeletal muscle triadins possibly involved in the architecture of sarcoplasmic reticulum Distinct regions of triadin are required for targeting and retention at the junctional domain of the sarcoplasmic reticulum.Inefficient glycosylation leads to high steady-state levels of actively degrading cardiac triadin-1.Null mutations causing depletion of the type 1 ryanodine receptor (RYR1) are commonly associated with recessive structural congenital myopathies with cores.The structural basis of ryanodine receptor ion channel function.Three residues in the luminal domain of triadin impact on Trisk 95 activation of skeletal muscle ryanodine receptors.Correlation of phenotype with genotype and protein structure in RYR1-related disorders With the greatest care, stromal interaction molecule (STIM) proteins verify what skeletal muscle is doing

P2860

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P2860

Negatively charged amino acids within the intraluminal loop of ryanodine receptor are involved in the interaction with triadin.

http://www.wikidata.org/entity/Q34279088

description

2003 nî lūn-bûn

@nan

2003 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

Negatively charged amino acids ...... the interaction with triadin.

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Negatively charged amino acids ...... the interaction with triadin.

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Negatively charged amino acids ...... the interaction with triadin.

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type

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Negatively charged amino acids ...... the interaction with triadin.

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Negatively charged amino acids ...... the interaction with triadin.

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Negatively charged amino acids ...... the interaction with triadin.

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Negatively charged amino acids ...... the interaction with triadin.

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Negatively charged amino acids ...... the interaction with triadin.

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Negatively charged amino acids ...... the interaction with triadin.

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P1433

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P2860

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P698

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P1433

Journal of Biological Chemistry

P1476

Negatively charged amino acids ...... the interaction with triadin.

@en

P2093

Chunghee Cho

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

Do Han Kim

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

Dong Wook Shin

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

Jae Man Lee

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

Jianjie Ma

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

Seong-Hwan Rho

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

Soo Hyun Eom

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

Woo Jin Park

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

P2860

The Structure of the Potassium Channel: Molecular Basis of K+ Conduction and Selectivity

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

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum

FKBP12 binding modulates ryanodine receptor channel gating

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

Regulation of Ca2+ signaling in transgenic mouse cardiac myocytes overexpressing calsequestrin

Molecular identification of the ryanodine receptor pore-forming segment

Luminal loop of the ryanodine receptor: a pore-forming segment?

Functional interaction of the cytoplasmic domain of triadin with the skeletal ryanodine receptor.

P304

6994-7000

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scholarly article

P356

10.1074/JBC.M312446200

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P433

8

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P478

279

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P577

2003-11-24T00:00:00Z

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P698

14638677

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