Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface. - Wikidata - wikimedia - TriplyDB

Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface.

Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface.

http://www.wikidata.org/entity/Q35571420

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Structure and function of human DnaJ homologue subfamily a member 1 (DNAJA1) and its relationship to pancreatic cancer Direct and Propagated Effects of Small Molecules on Protein-Protein Interaction Networks Fine-tuning multiprotein complexes using small molecules BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions Features of protein-protein interactions that translate into potent inhibitors: topology, surface area and affinity Chaperone machines for protein folding, unfolding and disaggregation Molecular mechanism of allosteric communication in Hsp70 revealed by molecular dynamics simulations Combining crystallography and EPR: crystal and solution structures of the multidomain cochaperone DnaJ Crystal structure of the nucleotide-binding domain of mortalin, the mitochondrial Hsp70 chaperone The human HSP70 family of chaperones: where do we stand?Allostery in the Hsp70 chaperone proteins Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro Signaling through dynamic linkers as revealed by PKA HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.Structural insights into the chaperone activity of the 40-kDa heat shock protein DnaJ: binding and remodeling of a native substrate Inhibitors of difficult protein-protein interactions identified by high-throughput screening of multiprotein complexes.Modeling Hsp70/Hsp40 interaction by multi-scale molecular simulations and coevolutionary sequence analysis Nucleotide-dependent interactions within a specialized Hsp70/Hsp40 complex involved in Fe-S cluster biogenesis.The anti-cancer IgM monoclonal antibody PAT-SM6 binds with high avidity to the unfolded protein response regulator GRP78.A bacteriophage-encoded J-domain protein interacts with the DnaK/Hsp70 chaperone and stabilizes the heat-shock factor σ32 of Escherichia coli Genetic interaction of hnRNPA2B1 and DNAJB6 in a Drosophila model of multisystem proteinopathy.ATPase subdomain IA is a mediator of interdomain allostery in Hsp70 molecular chaperones.Dancing through Life: Molecular Dynamics Simulations and Network-Centric Modeling of Allosteric Mechanisms in Hsp70 and Hsp110 Chaperone Proteins.Simulation of the opening and closing of Hsp70 chaperones by coarse-grained molecular dynamics Computational Analysis of Residue Interaction Networks and Coevolutionary Relationships in the Hsp70 Chaperones: A Community-Hopping Model of Allosteric Regulation and Communication Activation of UbcH5c~Ub is the result of a shift in interdomain motions of the conjugate bound to U-box E3 ligase E4B.Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.ArHsp40, a type 1 J-domain protein, is developmentally regulated and stress inducible in post-diapause Artemia franciscana.Allosteric linkers in cAMP signalling.Reconstitution of a Mycobacterium tuberculosis proteostasis network highlights essential cofactor interactions with chaperone DnaK.Hsp70 protein complexes as drug targets.ATP-driven molecular chaperone machines.Structural mechanisms of chaperone mediated protein disaggregation.A cytosolic chaperone complexes with dynamic membrane J-proteins and mobilizes a nonenveloped virus out of the endoplasmic reticulum.Structural and Biological Interaction of hsc-70 Protein with Phosphatidylserine in Endosomal Microautophagy.Therapeutic Strategies for Restoring Tau Homeostasis.The remarkable multivalency of the Hsp70 chaperones.Molecular analysis of Hsp70 mechanisms in plants and their function in response to stress.Tyrosine 601 of Bacillus subtilis DnaK Undergoes Phosphorylation and Is Crucial for Chaperone Activity and Heat Shock Survival.

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P2860

Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface.

http://www.wikidata.org/entity/Q35571420

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2011 nî lūn-bûn

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Heat shock protein 70 kDa chap ...... an unusual dynamic interface.

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Heat shock protein 70 kDa chap ...... an unusual dynamic interface.

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Heat shock protein 70 kDa chap ...... an unusual dynamic interface.

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Heat shock protein 70 kDa chap ...... an unusual dynamic interface.

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Heat shock protein 70 kDa chap ...... an unusual dynamic interface.

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Heat shock protein 70 kDa chap ...... s an unusual dynamic interface

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P2093

Akash Bhattacharya

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

Benjamin Ellington

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

Eric B Bertelsen

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

Erik R P Zuiderweg

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

Melissa Cordes

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

Ramsay A McDonald

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P2860

The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate

Insights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1

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

Structural analysis of substrate binding by the molecular chaperone DnaK

NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone

The Amber biomolecular simulation programs

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

The J-protein family: modulating protein assembly, disassembly and translocation.

The HSP70 chaperone machinery: J proteins as drivers of functional specificity

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22065753

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molecular chaperones

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3223468

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