Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones - Wikidata - awgldk - TriplyDB

Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones

Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones

http://www.wikidata.org/entity/Q34880691

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NMR Methods to Study Dynamic Allostery Mechanisms of amyloid formation revealed by solution NMR Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions NMR insights into protein allostery Molecular mechanism of allosteric communication in Hsp70 revealed by molecular dynamics simulations Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP Modulation of Global Low-Frequency Motions Underlies Allosteric Regulation: Demonstration in CRP/FNR Family Transcription Factors Substrate-binding domain conformational dynamics mediate Hsp70 allostery Allostery in the Hsp70 chaperone proteins Identification of key hinge residues important for nucleotide-dependent allostery in E. coli Hsp70/DnaK Signaling through dynamic linkers as revealed by PKA HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.Nucleotides regulate the mechanical hierarchy between subdomains of the nucleotide binding domain of the Hsp70 chaperone DnaK.Inhibitors of difficult protein-protein interactions identified by high-throughput screening of multiprotein complexes.Pathways of allosteric regulation in Hsp70 chaperones.Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular Machines Using ¹⁵N-ammonium to characterise and map potassium binding sites in proteins by NMR spectroscopy.NMR mapping of protein conformational landscapes using coordinated behavior of chemical shifts upon ligand binding.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.Conditional disorder in chaperone action.The specialized Hsp70 (HscA) interdomain linker binds to its nucleotide-binding domain and stimulates ATP hydrolysis in both cis and trans configurations.Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain.Interplay between E. coli DnaK, ClpB and GrpE during protein disaggregation.Common functionally important motions of the nucleotide-binding domain of Hsp70 Decipher the mechanisms of protein conformational changes induced by nucleotide binding through free-energy landscape analysis: ATP binding to Hsp70.ATPase subdomain IA is a mediator of interdomain allostery in Hsp70 molecular chaperones.Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface.DOMMINO: a database of macromolecular interactions.Dancing through Life: Molecular Dynamics Simulations and Network-Centric Modeling of Allosteric Mechanisms in Hsp70 and Hsp110 Chaperone Proteins.Isoform-selective Genetic Inhibition of Constitutive Cytosolic Hsp70 Activity Promotes Client Tau Degradation Using an Altered Co-chaperone Complement Computational Analysis of Residue Interaction Networks and Coevolutionary Relationships in the Hsp70 Chaperones: A Community-Hopping Model of Allosteric Regulation and Communication Proteasome allostery as a population shift between interchanging conformers Glutathionylation of the Bacterial Hsp70 Chaperone DnaK Provides a Link between Oxidative Stress and the Heat Shock Response.The glucocorticoid receptor dimer interface allosterically transmits sequence-specific DNA signals.Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.The allosteric communication pathways in KIX domain of CBP Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates.Sequences flanking the core-binding site modulate glucocorticoid receptor structure and activity.

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P2860

Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones

http://www.wikidata.org/entity/Q34880691

description

2011 nî lūn-bûn

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2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի ապրիլին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Allosteric signal transmission ...... n (Hsp70) molecular chaperones

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Allosteric signal transmission ...... n (Hsp70) molecular chaperones

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Allosteric signal transmission ...... n of 70-kDa heat shock protein

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type

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Allosteric signal transmission ...... n (Hsp70) molecular chaperones

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Allosteric signal transmission ...... n (Hsp70) molecular chaperones

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Allosteric signal transmission ...... n of 70-kDa heat shock protein

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Allosteric signal transmission ...... n (Hsp70) molecular chaperones

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Allosteric signal transmission ...... n (Hsp70) molecular chaperones

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Allosteric signal transmission ...... n of 70-kDa heat shock protein

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PNAS.1014448108

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

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Allosteric signal transmission ...... n (Hsp70) molecular chaperones

@en

P2093

Lila M Gierasch

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P2860

Consistent blind protein structure generation from NMR chemical shift data

Allosteric communication occurs via networks of tertiary and quaternary motions in proteins

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

Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors

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

Structural Basis of J Cochaperone Binding and Regulation of Hsp70

Structure of the Hsp110:Hsc70 nucleotide exchange machine.

Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding

The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange

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

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6987-6992

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10.1073/PNAS.1014448108

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17

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108

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Anastasia Zhuravleva

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2011-04-11T00:00:00Z

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51041591

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21482798

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molecular chaperones

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3084084

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