Allostery in the Hsp70 chaperone proteins - Wikidata - awgldk - TriplyDB

Allostery in the Hsp70 chaperone proteins

Allostery in the Hsp70 chaperone proteins

http://www.wikidata.org/entity/Q28266387

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Protein Folding and Mechanisms of Proteostasis BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions The ensemble nature of allostery Chaperone machines for protein folding, unfolding and disaggregation Diversification, evolution and sub-functionalization of 70kDa heat-shock proteins in two sister species of antarctic krill: differences in thermal habitats, responses and implications under climate change Molecular mechanism of allosteric communication in Hsp70 revealed by molecular dynamics simulations Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP Functional analysis of Hsp70 inhibitors Crystal structure of the nucleotide-binding domain of mortalin, the mitochondrial Hsp70 chaperone Redox signaling via the molecular chaperone BiP protects cells against endoplasmic reticulum-derived oxidative stress Selective targeting of the stress chaperome as a therapeutic strategy Substrate-binding domain conformational dynamics mediate Hsp70 allostery EZ-ASSIGN, a program for exhaustive NMR chemical shift assignments of large proteins from complete or incomplete triple-resonance data Large-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 Chaperones ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro Heterogeneous binding of the SH3 client protein to the DnaK molecular chaperone.Inhibitors of difficult protein-protein interactions identified by high-throughput screening of multiprotein complexes.Pathways of allosteric regulation in Hsp70 chaperones.Hsp70 chaperones are non-equilibrium machines that achieve ultra-affinity by energy consumption Modeling Hsp70/Hsp40 interaction by multi-scale molecular simulations and coevolutionary sequence analysis Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.Conditional disorder in chaperone action.Heat shock protein 70 in Alzheimer's disease The specialized Hsp70 (HscA) interdomain linker binds to its nucleotide-binding domain and stimulates ATP hydrolysis in both cis and trans configurations.Interplay between E. coli DnaK, ClpB and GrpE during protein disaggregation.Quantifying the role of chaperones in protein translocation by computational modeling.Insertion of a xylanase in xylose binding protein results in a xylose-stimulated xylanase.Dancing through Life: Molecular Dynamics Simulations and Network-Centric Modeling of Allosteric Mechanisms in Hsp70 and Hsp110 Chaperone Proteins.Mutations in the Yeast Hsp70, Ssa1, at P417 Alter ATP Cycling, Interdomain Coupling, and Specific Chaperone Functions.Computational Analysis of Residue Interaction Networks and Coevolutionary Relationships in the Hsp70 Chaperones: A Community-Hopping Model of Allosteric Regulation and Communication Glutathionylation of the Bacterial Hsp70 Chaperone DnaK Provides a Link between Oxidative Stress and the Heat Shock Response.Substrate protein folds while it is bound to the ATP-independent chaperone Spy The HSP70 family and cancer Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.Clathrin-coat disassembly illuminates the mechanisms of Hsp70 force generation Emerging role of high-mobility group box 1 (HMGB1) in liver diseases.Reconstitution of a Mycobacterium tuberculosis proteostasis network highlights essential cofactor interactions with chaperone DnaK.The molecular chaperone Hsp70 activates protein phosphatase 5 (PP5) by binding the tetratricopeptide repeat (TPR) domain.Potential synergy between tau aggregation inhibitors and tau chaperone modulators.

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P2860

Allostery in the Hsp70 chaperone proteins

http://www.wikidata.org/entity/Q28266387

description

2013 nî lūn-bûn

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2013 թուականին հրատարակուած գիտական յօդուած

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2013 թվականին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

Allostery in the Hsp70 chaperone proteins

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Allostery in the Hsp70 chaperone proteins

@en

Allostery in the Hsp70 chaperone proteins

@nl

type

label

Allostery in the Hsp70 chaperone proteins

@ast

Allostery in the Hsp70 chaperone proteins

@en

Allostery in the Hsp70 chaperone proteins

@nl

prefLabel

Allostery in the Hsp70 chaperone proteins

@ast

Allostery in the Hsp70 chaperone proteins

@en

Allostery in the Hsp70 chaperone proteins

@nl

P1433

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P932

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P3181

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P1433

Topics in Current Chemistry

P1476

Allostery in the Hsp70 chaperone proteins

@en

P2093

Aikaterini Rousaki

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

Atta Ahmad

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

Jason E Gestwicki

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

Matthias P Mayer

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

P2860

The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins

Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53.

Protein phylogenies and signature sequences: A reappraisal of evolutionary relationships among archaebacteria, eubacteria, and eukaryotes

Hsp70 chaperones: cellular functions and molecular mechanism

Akt and CHIP coregulate tau degradation through coordinated interactions

The influence of C-terminal extension on the structure of the “J-domain” in E. coli DnaJ

Structure of a new crystal form of human Hsp70 ATPase domain

High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70

Site-site communication in the EF-hand Ca2+-binding protein calbindin D9k

Structural insights into substrate binding by the molecular chaperone DnaK

P2888

P304

99-153

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P31

scholarly article

P3181

3121833

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P356

10.1007/128_2012_323

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P407

P478

328

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P577

2013-01-01T00:00:00Z

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P698

22576356

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P921

molecular chaperones

P932

3623542

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