S100A1 and Calmodulin Compete for the Same Binding Site on Ryanodine Receptor - Wikidata - wikimedia - TriplyDB

S100A1 and Calmodulin Compete for the Same Binding Site on Ryanodine Receptor

S100A1 and Calmodulin Compete for the Same Binding Site on Ryanodine Receptor

http://www.wikidata.org/entity/Q27651297

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Transcriptional adaptations following exercise in thoroughbred horse skeletal muscle highlights molecular mechanisms that lead to muscle hypertrophy The structure of Ca2+-loaded S100A2 at 1.3-Å resolution Critical Role of Intracellular RyR1 Calcium Release Channels in Skeletal Muscle Function and Disease FK506-binding protein 1b/12.6: a key to aging-related hippocampal Ca2+ dysregulation?Refinement of the solution structure and dynamic properties of Ca2+-bound rat S100B Crystal structure of the S100A4-nonmuscle myosin IIA tail fragment complex reveals an asymmetric target binding mechanism Asymmetric Mode of Ca2+-S100A4 Interaction with Nonmuscle Myosin IIA Generates Nanomolar Affinity Required for Filament Remodeling Solution structure and small angle scattering analysis of TraI (381-569)S100A1 and calmodulin regulation of ryanodine receptor in striated muscle S100A1 in cardiovascular health and disease: closing the gap between basic science and clinical therapy Calmodulin and S100A1 protein interact with N terminus of TRPM3 channel S100A1: Structure, Function, and Therapeutic Potential Minding the calcium store: Ryanodine receptor activation as a convergent mechanism of PCB toxicity Augmentation of Cav1 channel current and action potential duration after uptake of S100A1 in sympathetic ganglion neurons.Complex formation between S100B protein and the p90 ribosomal S6 kinase (RSK) in malignant melanoma is calcium-dependent and inhibits extracellular signal-regulated kinase (ERK)-mediated phosphorylation of RSK Myoplasmic resting Ca2+ regulation by ryanodine receptors is under the control of a novel Ca2+-binding region of the receptor.The Activation of Protein Kinase A by the Calcium-Binding Protein S100A1 Is Independent of Cyclic AMP.S100A1: a regulator of striated muscle sarcoplasmic reticulum Ca2+ handling, sarcomeric, and mitochondrial function The calcium-dependent interaction between S100B and the mitochondrial AAA ATPase ATAD3A and the role of this complex in the cytoplasmic processing of ATAD3A.Ryanodine receptors: structure, expression, molecular details, and function in calcium release.S100A1 promotes action potential-initiated calcium release flux and force production in skeletal muscle Characterization of the S100A1 protein binding site on TRPC6 C-terminus Modulation of sarcoplasmic reticulum Ca2+ release in skeletal muscle expressing ryanodine receptor impaired in regulation by calmodulin and S100A1.Two functional S100A4 monomers are necessary for regulating nonmuscle myosin-IIA and HCT116 cell invasion S100A1 (S100 calcium binding protein A1)S100 calcium binding proteins and ion channels Target binding to S100B reduces dynamic properties and increases Ca(2+)-binding affinity for wild type and EF-hand mutant proteins.Bioactive nanoparticles improve calcium handling in failing cardiac myocytes.Molecular Basis of S100A1 Activation at Saturating and Subsaturating Calcium Concentrations.Functions of S100 proteins.S100A1 Protein Does Not Compete with Calmodulin for Ryanodine Receptor Binding but Structurally Alters the Ryanodine Receptor·Calmodulin Complex.Solution structure of S100A1 bound to the CapZ peptide (TRTK12).The structural biology of ryanodine receptors.Reciprocal dihydropyridine and ryanodine receptor interactions in skeletal muscle activation.Ryanodine receptors: structure and function.Ryanodine receptor calcium release channels: lessons from structure-function studies.Ca2+/S100 proteins inhibit the interaction of FKBP38 with Bcl-2 and Hsp90.The S100A10-annexin A2 complex provides a novel asymmetric platform for membrane repair.Activation of IP3 receptors requires an endogenous 1-8-14 calmodulin-binding motif.Functional interaction between Smad3 and S100A4 (metastatin-1) for TGF-beta-mediated cancer cell invasiveness.

P2860

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P2860

S100A1 and Calmodulin Compete for the Same Binding Site on Ryanodine Receptor

http://www.wikidata.org/entity/Q27651297

description

2008 nî lūn-bûn

@nan

2008 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2008年の論文

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2008年論文

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2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

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2008年論文

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2008年论文

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name

S100A1 and Calmodulin Compete for the Same Binding Site on Ryanodine Receptor

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S100A1 and Calmodulin Compete for the Same Binding Site on Ryanodine Receptor

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S100A1 and Calmodulin Compete for the Same Binding Site on Ryanodine Receptor

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type

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S100A1 and Calmodulin Compete for the Same Binding Site on Ryanodine Receptor

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S100A1 and Calmodulin Compete for the Same Binding Site on Ryanodine Receptor

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S100A1 and Calmodulin Compete for the Same Binding Site on Ryanodine Receptor

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prefLabel

S100A1 and Calmodulin Compete for the Same Binding Site on Ryanodine Receptor

@ast

S100A1 and Calmodulin Compete for the Same Binding Site on Ryanodine Receptor

@en

S100A1 and Calmodulin Compete for the Same Binding Site on Ryanodine Receptor

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P1433

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P1433

Journal of Biological Chemistry

P1476

S100A1 and Calmodulin Compete for the Same Binding Site on Ryanodine Receptor

@en

P2093

Benjamin L Prosser

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

Danna B Zimmer

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

David J Weber

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

Kristen M Varney

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

Martin F Schneider

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

Nathan T Wright

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

P2860

Structure of the Ca2+/S100B/NDR kinase peptide complex: insights into S100 target specificity and activation of the kinase

The use of dipolar couplings for determining the solution structure of rat apo-S100B(ββ)

Structure of the negative regulatory domain of p53 bound to S100B(betabeta)

Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as determined by NMR

Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12

A novel S100 target conformation is revealed by the solution structure of the Ca2+-S100B-TRTK-12 complex

Solution structure of the DNA-binding domain of Drosophila heat shock transcription factor

Use of dipolar 1H-15N and 1H-13C couplings in the structure determination of magnetically oriented macromolecules in solution

Solution structure of calcium-bound rat S100B(betabeta) as determined by nuclear magnetic resonance spectroscopy,

Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra

P304

26676-83

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P31

scholarly article

P356

10.1074/JBC.M804432200

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P407

P433

39

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P478

283

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P577

2008-09-26T00:00:00Z

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18650434

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P921

P932

2546546

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