The structure of calsequestrin in triads of vertebrate skeletal muscle: a deep-etch study.
about
Molecular cloning, expression, functional characterization, chromosomal localization, and gene structure of junctate, a novel integral calcium binding protein of sarco(endo)plasmic reticulum membraneRole of Junctin protein interactions in cellular dynamics of calsequestrin polymer upon calcium perturbationCalsequestrin 2 and arrhythmiasHigh-capacity Ca2+ binding of human skeletal calsequestrinCalreticulinComparing 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 calsequestrin from rabbit skeletal muscle sarcoplasmic reticulumDifferent subcellular localization of Saccharomyces cerevisiae HMG-CoA reductase isozymes at elevated levels corresponds to distinct endoplasmic reticulum membrane proliferations.Calsequestrin is an inhibitor of skeletal muscle ryanodine receptor calcium release channelsCalsequestrin (CASQ1) rescues function and structure of calcium release units in skeletal muscles of CASQ1-null miceAnesthetic- and heat-induced sudden death in calsequestrin-1-knockout miceVesicle budding from endoplasmic reticulum is involved in calsequestrin routing to sarcoplasmic reticulum of skeletal musclesReorganized stores and impaired calcium handling in skeletal muscle of mice lacking calsequestrin-1Regulation of Ca2+ signaling in transgenic mouse cardiac myocytes overexpressing calsequestrinStructure 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.Dysregulated sarcoplasmic reticulum calcium release: potential pharmacological target in cardiac disease.The endoplasmic reticulum-sarcoplasmic reticulum connection: distribution of endoplasmic reticulum markers in the sarcoplasmic reticulum of skeletal muscle fibers.Cloning, tissue distribution, subcellular localization and overexpression of murine histidine-rich Ca2+ binding protein.Localization and characterization of the calsequestrin-binding domain of triadin 1. Evidence for a charged beta-strand in mediating the protein-protein interaction.The active site structure of tetanus neurotoxin resolved by multiple scattering analysis in X-Ray absorption spectroscopy.Morphology and molecular composition of sarcoplasmic reticulum surface junctions in the absence of DHPR and RyR in mouse skeletal muscleElectron tomography of frozen-hydrated isolated triad junctionsRegulation of ryanodine receptors by calsequestrin: effect of high luminal Ca2+ and phosphorylation.Association of triadin with the ryanodine receptor and calsequestrin in the lumen of the sarcoplasmic reticulum.Triadin/Junctin double null mouse reveals a differential role for Triadin and Junctin in anchoring CASQ to the jSR and regulating Ca(2+) homeostasis.Purification, primary structure, and immunological characterization of the 26-kDa calsequestrin binding protein (junctin) from cardiac junctional sarcoplasmic reticulum.Depletion "skraps" and dynamic buffering inside the cellular calcium store.Functional and structural characterization of a eurytolerant calsequestrin from the intertidal teleost Fundulus heteroclitus.Couplons in rat atria form distinct subgroups defined by their molecular partners.The conformation of calsequestrin determines its ability to regulate skeletal ryanodine receptors.Differential effect of calsequestrin ablation on structure and function of fast and slow skeletal muscle fibers.C-terminal residues of skeletal muscle calsequestrin are essential for calcium binding and for skeletal ryanodine receptor inhibitionEndoplasmic reticulum: a dynamic patchwork of specialized subregionsFunctional consequences of stably expressing a mutant calsequestrin (CASQ2D307H) in the CASQ2 null background.Immunocytochemistry of calciosomes in liver and pancreas.The endoplasmic-sarcoplasmic reticulum of smooth muscle: immunocytochemistry of vas deferens fibers reveals specialized subcompartments differently equipped for the control of Ca2+ homeostasisCharacterization of the sarcoplasmic reticulum proteins in the thermogenic muscles of fish
P2860
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P2860
The structure of calsequestrin in triads of vertebrate skeletal muscle: a deep-etch study.
description
1987 nî lūn-bûn
@nan
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
1987年论文
@zh
1987年论文
@zh-cn
name
The structure of calsequestrin ...... tal muscle: a deep-etch study.
@ast
The structure of calsequestrin ...... tal muscle: a deep-etch study.
@en
type
label
The structure of calsequestrin ...... tal muscle: a deep-etch study.
@ast
The structure of calsequestrin ...... tal muscle: a deep-etch study.
@en
prefLabel
The structure of calsequestrin ...... tal muscle: a deep-etch study.
@ast
The structure of calsequestrin ...... tal muscle: a deep-etch study.
@en
P2093
P2860
P356
P1476
The structure of calsequestrin ...... tal muscle: a deep-etch study.
@en
P2093
C Franzini-Armstrong
E Varriano-Marston
L J Kenney
P2860
P356
10.1083/JCB.105.1.49
P407
P577
1987-07-01T00:00:00Z