Localization and characterization of the calsequestrin-binding domain of triadin 1. Evidence for a charged beta-strand in mediating the protein-protein interaction.
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Interaction of HRC (histidine-rich Ca(2+)-binding protein) and triadin in the lumen of sarcoplasmic reticulumOn the role of junctin in cardiac Ca2+ handling, contractility, and heart failureAbsence of triadin, a protein of the calcium release complex, is responsible for cardiac arrhythmia with sudden death in humanJunctin - the quiet achieverProtein protein interactions between triadin and calsequestrin are involved in modulation of sarcoplasmic reticulum calcium release in cardiac myocytesThe role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium.Junctin and the histidine-rich Ca2+ binding protein: potential roles in heart failure and arrhythmogenesisTriadin regulation of the ryanodine receptor complexCardiac hypertrophy and impaired relaxation in transgenic mice overexpressing triadin 1Calsequestrin is an inhibitor of skeletal muscle ryanodine receptor calcium release channelsAblation of triadin causes loss of cardiac Ca2+ release units, impaired excitation-contraction coupling, and cardiac arrhythmiasAAV-mediated knock-down of HRC exacerbates transverse aorta constriction-induced heart failureTriadin (Trisk 95) overexpression blocks excitation-contraction coupling in rat skeletal myotubesAltered expression of triadin 95 causes parallel changes in localized Ca2+ release events and global Ca2+ signals in skeletal muscle cells in cultureDysregulated sarcoplasmic reticulum calcium release: potential pharmacological target in cardiac disease.The asp-rich region at the carboxyl-terminus of calsequestrin binds to Ca(2+) and interacts with triadin.Regulation of ryanodine receptors by calsequestrin: effect of high luminal Ca2+ and phosphorylation.Negatively charged amino acids within the intraluminal loop of ryanodine receptor are involved in the interaction with triadin.A skeletal muscle ryanodine receptor interaction domain in triadinThe fungal pathogen Moniliophthora perniciosa has genes similar to plant PR-1 that are highly expressed during its interaction with cacaoA new cytoplasmic interaction between junctin and ryanodine receptor Ca2+ release channels.On the footsteps of Triadin and its role in skeletal muscleC-terminal residues of skeletal muscle calsequestrin are essential for calcium binding and for skeletal ryanodine receptor inhibitionTransitions of protein traffic from cardiac ER to junctional SRCommon Variants in TRDN and CALM1 Are Associated with Risk of Sudden Cardiac Death in Chronic Heart Failure Patients in Chinese Han PopulationRetrograde regulation of STIM1-Orai1 interaction and store-operated Ca2+ entry by calsequestrin.Luminal Ca2+ regulation of single cardiac ryanodine receptors: insights provided by calsequestrin and its mutantsAltered stored calcium release in skeletal myotubes deficient of triadin and junctin.A mutation in calsequestrin, CASQ2D307H, impairs Sarcoplasmic Reticulum Ca2+ handling and causes complex ventricular arrhythmias in mice.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.Triadin deletion induces impaired skeletal muscle functionProteins within the intracellular calcium store determine cardiac RyR channel activity and cardiac output.Functional interaction between calsequestrin and ryanodine receptor in the heart.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.Calsequestrin interacts directly with the cardiac ryanodine receptor luminal domain.Core skeletal muscle ryanodine receptor calcium release complex.Modeling CICR in rat ventricular myocytes: voltage clamp studies.Calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers.
P2860
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P2860
Localization and characterization of the calsequestrin-binding domain of triadin 1. Evidence for a charged beta-strand in mediating the protein-protein interaction.
description
2000 nî lūn-bûn
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2000 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունիսին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Localization and characterizat ...... e protein-protein interaction.
@ast
Localization and characterizat ...... e protein-protein interaction.
@en
type
label
Localization and characterizat ...... e protein-protein interaction.
@ast
Localization and characterizat ...... e protein-protein interaction.
@en
prefLabel
Localization and characterizat ...... e protein-protein interaction.
@ast
Localization and characterizat ...... e protein-protein interaction.
@en
P2093
P2860
P356
P1476
Localization and characterizat ...... e protein-protein interaction.
@en
P2093
Alseikhan BA
Kobayashi YM
P2860
P304
17639-17646
P356
10.1074/JBC.M002091200
P407
P577
2000-06-01T00:00:00Z