Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum
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Role of Junctin protein interactions in cellular dynamics of calsequestrin polymer upon calcium perturbationCalsequestrin 2 and arrhythmiasHigh-capacity Ca2+ binding of human skeletal calsequestrinCrystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix proteinBioinspired design of a polymer gel sensor for the realization of extracellular Ca(2+) imagingCrystal structure and functional analysis of Drosophila Wind, a protein-disulfide isomerase-related proteinComparing skeletal and cardiac calsequestrin structures and their calcium binding: a proposed mechanism for coupled calcium binding and protein polymerizationGlycosylation of Skeletal Calsequestrin: IMPLICATIONS FOR ITS FUNCTIONCrystal structure of class III chitinase from pomegranate provides the insight into its metal storage capacityA missense mutation in a highly conserved region of CASQ2 is associated with autosomal recessive catecholamine-induced polymorphic ventricular tachycardia in Bedouin families from IsraelCalsequestrin mutations and catecholaminergic polymorphic ventricular tachycardiaCalsequestrin is an inhibitor of skeletal muscle ryanodine receptor calcium release channelsThe catecholaminergic polymorphic ventricular tachycardia mutation R33Q disrupts the N-terminal structural motif that regulates reversible calsequestrin polymerizationA retrograde signal from calsequestrin for the regulation of store-operated Ca2+ entry in skeletal muscleThe calsequestrin mutation CASQ2D307H does not affect protein stability and targeting to the junctional sarcoplasmic reticulum but compromises its dynamic regulation of calcium bufferingStructure of frozen-hydrated triad junctions: a case study in motif searching inside tomogramsIdentification of calcium binding sites on calsequestrin 1 and their implications for polymerization.Polymerization of calsequestrin. Implications for Ca2+ regulation.A missense mutation in CASQ2 is associated with autosomal recessive catecholamine-induced polymorphic ventricular tachycardia in Bedouin families from Israel.The protein disulphide-isomerase family: unravelling a string of folds.Identification and analysis of muscle-related protein isoforms expressed in the white muscle of the mandarin fish (Siniperca chuatsi).Dysregulated sarcoplasmic reticulum calcium release: potential pharmacological target in cardiac disease.Molecular and phylogenetic characterization of the sieve element occlusion gene family in Fabaceae and non-Fabaceae plantsLocalization and characterization of the calsequestrin-binding domain of triadin 1. Evidence for a charged beta-strand in mediating the protein-protein interaction.Potential role of cardiac calsequestrin in the lethal arrhythmic effects of cocaineThe asp-rich region at the carboxyl-terminus of calsequestrin binds to Ca(2+) and interacts with triadin.A minimal model for the mitochondrial rapid mode of Ca²+ uptake mechanism.Regulation of ryanodine receptors by calsequestrin: effect of high luminal Ca2+ and phosphorylation.A mutation in the CASQ1 gene causes a vacuolar myopathy with accumulation of sarcoplasmic reticulum protein aggregates.Negatively charged amino acids within the intraluminal loop of ryanodine receptor are involved in the interaction with triadin.Triadin/Junctin double null mouse reveals a differential role for Triadin and Junctin in anchoring CASQ to the jSR and regulating Ca(2+) homeostasis.High-resolution NMR studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibilityCalcium powered phloem protein of SEO gene family "Forisome" functions in wound sealing and act as biomimetic smart materialsHistidine-rich calcium binding protein: the new regulator of sarcoplasmic reticulum calcium cycling.Functional and structural characterization of a eurytolerant calsequestrin from the intertidal teleost Fundulus heteroclitus.Structure-function analysis of the endoplasmic reticulum oxidoreductase TMX3 reveals interdomain stabilization of the N-terminal redox-active domain.The conformation of calsequestrin determines its ability to regulate skeletal ryanodine receptors.Biphasic modulation of ryanodine receptors by sulfhydryl oxidation in rat ventricular myocytesCalcium and arrhythmogenesis.C-terminal residues of skeletal muscle calsequestrin are essential for calcium binding and for skeletal ryanodine receptor inhibition
P2860
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P2860
Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum
description
1998 nî lūn-bûn
@nan
1998 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum
@ast
Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum
@en
Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum
@nl
type
label
Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum
@ast
Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum
@en
Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum
@nl
prefLabel
Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum
@ast
Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum
@en
Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum
@nl
P2093
P2860
P3181
P356
P1476
Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum
@en
P2093
P2860
P304
P3181
P356
10.1038/NSB0698-476
P407
P577
1998-06-01T00:00:00Z