Structural Basis of J Cochaperone Binding and Regulation of Hsp70 - Test2 - elhamkhani - TriplyDB

Structural Basis of J Cochaperone Binding and Regulation of Hsp70

Structural Basis of J Cochaperone Binding and Regulation of Hsp70

http://www.wikidata.org/entity/Q27649002

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Crystal structure of the stress-inducible human heat shock protein 70 substrate-binding domain in complex with peptide substrate Structure and mechanistic insights into novel iron-mediated moonlighting functions of human J-protein cochaperone, Dph4 Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3 Structure and function of human DnaJ homologue subfamily a member 1 (DNAJA1) and its relationship to pancreatic cancer DNAJs: more than substrate delivery to HSPA Fine-tuning multiprotein complexes using small molecules BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions NMR insights into protein allostery Features of protein-protein interactions that translate into potent inhibitors: topology, surface area and affinity Chaperone machines for protein folding, unfolding and disaggregation Structure of the Hsp110:Hsc70 nucleotide exchange machine.Biochemical and structural studies on the high affinity of Hsp70 for ADP Structural analysis of the Sil1-Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factor The Crystal Structure of the Human Co-Chaperone P58IPK Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP Combining crystallography and EPR: crystal and solution structures of the multidomain cochaperone DnaJ Cwc23, an essential J protein critical for pre-mRNA splicing with a dispensable J domain Cytosolic Hsp70 and co-chaperones constitute a novel system for tRNA import into the nucleus Prion-impairing mutations in Hsp70 chaperone Ssa1: effects on ATPase and chaperone activities.Plasmodium falciparum Hsp70-x: a heat shock protein at the host-parasite interface The C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activation Allostery in the Hsp70 chaperone proteins Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro The HSP70 chaperone machinery: J proteins as drivers of functional specificity 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.ATP-induced conformational changes in Hsp70: molecular dynamics and experimental validation of an in silico predicted conformation.DnaJ homolog Hdj2 facilitates Japanese encephalitis virus replication Binding of a small molecule at a protein-protein interface regulates the chaperone activity of hsp70-hsp40.Structure of clathrin coat with bound Hsc70 and auxilin: mechanism of Hsc70-facilitated disassembly.Role of Hsp70 ATPase domain intrinsic dynamics and sequence evolution in enabling its functional interactions with NEFs.Modeling Hsp70/Hsp40 interaction by multi-scale molecular simulations and coevolutionary sequence analysis Heat shock protein 70 (hsp70) as an emerging drug target.Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (Hsp70/DnaK)J domain co-chaperone specificity defines the role of BiP during protein translocation Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.Nucleotide-dependent interactions within a specialized Hsp70/Hsp40 complex involved in Fe-S cluster biogenesis.The lid domain of Caenorhabditis elegans Hsc70 influences ATP turnover, cofactor binding and protein folding activity.Rapid isolation of extracellular vesicles from cell culture and biological fluids using a synthetic peptide with specific affinity for heat shock proteins.DNAJC6 Mutations Associated With Early-Onset Parkinson's Disease.

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Structural Basis of J Cochaperone Binding and Regulation of Hsp70

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2007 nî lūn-bûn

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Structural Basis of J Cochaperone Binding and Regulation of Hsp70

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Structural basis of J cochaperone binding and regulation of Hsp70

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Alexander B Taylor

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Andrew P Hinck

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E Guy Maes

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Jianwen Jiang

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Liping Wang

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Rui Sousa

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P2860

Mechanisms for regulation of Hsp70 function by Hsp40

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

Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

Improved methods for building protein models in electron density maps and the location of errors in these models

Mapping the role of active site residues for transducing an ATP-induced conformational change in the bovine 70-kDa heat shock cognate protein

Structure-function analysis of the auxilin J-domain reveals an extended Hsc70 interaction interface

Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment

Structure of DNA polymerase I Klenow fragment bound to duplex DNA

Structural analysis of substrate binding by the molecular chaperone DnaK

Structural replacement of active site monovalent cations by the epsilon-amino group of lysine in the ATPase fragment of bovine Hsc70

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