Binding of a small molecule at a protein-protein interface regulates the chaperone activity of hsp70-hsp40. - Wikidata - awgldk - TriplyDB

Binding of a small molecule at a protein-protein interface regulates the chaperone activity of hsp70-hsp40.

Binding of a small molecule at a protein-protein interface regulates the chaperone activity of hsp70-hsp40.

http://www.wikidata.org/entity/Q33580742

about

Model systems of protein-misfolding diseases reveal chaperone modifiers of proteotoxicity Direct and Propagated Effects of Small Molecules on Protein-Protein Interaction Networks Fine-tuning multiprotein complexes using small molecules Features of protein-protein interactions that translate into potent inhibitors: topology, surface area and affinity Protein homeostasis as a therapeutic target for diseases of protein conformation Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis Hsp70 May Be a Molecular Regulator of Schistosome Host Invasion Molecular mechanism of allosteric communication in Hsp70 revealed by molecular dynamics simulations Allostery in the Hsp70 chaperone proteins Contributions of academic laboratories to the discovery and development of chemical biology tools Identification of key hinge residues important for nucleotide-dependent allostery in E. coli Hsp70/DnaK Combined chemical-genetic approach identifies cytosolic HSP70 dependence in rhabdomyosarcoma Plasmodium falciparum encodes a single cytosolic type I Hsp40 that functionally interacts with Hsp70 and is upregulated by heat shock HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.A fragment-based approach applied to a highly flexible target: Insights and challenges towards the inhibition of HSP70 isoforms.Chemical methodology as a source of small-molecule checkpoint inhibitors and heat shock protein 70 (Hsp70) modulators.A chaperone trap contributes to the onset of cystic fibrosis.Receptor agonists of macrophage migration inhibitory factor.Chemical screens against a reconstituted multiprotein complex: myricetin blocks DnaJ regulation of DnaK through an allosteric mechanism Common functionally important motions of the nucleotide-binding domain of Hsp70 Antimyeloma Effects of the Heat Shock Protein 70 Molecular Chaperone Inhibitor MAL3-101 Molecular chaperones and regulation of tau quality control: strategies for drug discovery in tauopathies.Heat shock protein defenses in the neocortex and allocortex of the telencephalon.A functional DnaK dimer is essential for the efficient interaction with Hsp40 heat shock protein HSP70 inhibits stress-induced cardiomyocyte apoptosis by competitively binding to FAF1.Protein-protein interactions as drug targets.Visualization and functional analysis of the oligomeric states of Escherichia coli heat shock protein 70 (Hsp70/DnaK).Chemical induction of Hsp70 reduces α-synuclein aggregation in neuroglioma cells.Mutations in the Yeast Hsp70, Ssa1, at P417 Alter ATP Cycling, Interdomain Coupling, and Specific Chaperone Functions.The Chemical Biology of Molecular Chaperones--Implications for Modulation of Proteostasis Chemical Tools to Investigate Mechanisms Associated with HSP90 and HSP70 in Disease.Engineering therapeutic protein disaggregases.Synthesis and initial evaluation of YM-08, a blood-brain barrier permeable derivative of the heat shock protein 70 (Hsp70) inhibitor MKT-077, which reduces tau levels.Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates.Hsp70 protein complexes as drug targets.Heat shock proteins 27, 40, and 70 as combinational and dual therapeutic cancer targets.Opportunities and challenges for molecular chaperone modulation to treat protein-conformational brain diseases Targeting Allosteric Control Mechanisms in Heat Shock Protein 70 (Hsp70).Modulation of Molecular Chaperones in Huntington's Disease and Other Polyglutamine Disorders.Validation of the Hsp70-Bag3 protein-protein interaction as a potential therapeutic target in cancer.

P2860

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P2860

Binding of a small molecule at a protein-protein interface regulates the chaperone activity of hsp70-hsp40.

http://www.wikidata.org/entity/Q33580742

description

2010 nî lūn-bûn

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2010 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունիսին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年论文

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Binding of a small molecule at ...... erone activity of hsp70-hsp40.

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Binding of a small molecule at ...... erone activity of hsp70-hsp40.

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Binding of a small molecule at ...... erone activity of hsp70-hsp40.

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Binding of a small molecule at ...... erone activity of hsp70-hsp40.

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Binding of a small molecule at ...... erone activity of hsp70-hsp40.

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Binding of a small molecule at ...... erone activity of hsp70-hsp40.

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ACS Chemical Biology

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Binding of a small molecule at ...... erone activity of hsp70-hsp40.

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P2093

Andrea D Thompson

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Christopher G Evans

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Eric B Bertelsen

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Erik R P Zuiderweg

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Gladis M Walter

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Jason E Gestwicki

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Jeffrey L Brodsky

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Lyra Chang

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Srikanth Patury

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Susanne Wisén

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P2860

Allosteric Inhibition of the Protein-Protein Interaction between the Leukemia-Associated Proteins Runx1 and CBFβ

Eukaryotic homologues of Escherichia coli dnaJ: a diverse protein family that functions with hsp70 stress proteins

Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions

Binding of small molecules to an adaptive protein-protein interface

Structural Basis of J Cochaperone Binding and Regulation of Hsp70

Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate

Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

Comparison of multiple Amber force fields and development of improved protein backbone parameters

The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE

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611-622

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10.1021/CB1000422

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6

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5

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Peter Man-Un Ung

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2010-06-01T00:00:00Z

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44610337

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20481474

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molecular chaperones

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2950966

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