Allostery in Hsp70 chaperones is transduced by subdomain rotations - Test2 - elhamkhani - TriplyDB

Allostery in Hsp70 chaperones is transduced by subdomain rotations

Allostery in Hsp70 chaperones is transduced by subdomain rotations

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NMR insights into protein allostery Features of protein-protein interactions that translate into potent inhibitors: topology, surface area and affinity Molecular mechanism of allosteric communication in Hsp70 revealed by molecular dynamics simulations Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP 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 Substrate-specific reorganization of the conformational ensemble of CSK implicates novel modes of kinase function Protein structure validation and identification from unassigned residual dipolar coupling data using 2D-PDPA.HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.Pathways of allosteric regulation in Hsp70 chaperones.Role of Hsp70 ATPase domain intrinsic dynamics and sequence evolution in enabling its functional interactions with NEFs.Measurement and interpretation of 15N-1H residual dipolar couplings in larger proteins.Role of the loop L4,5 in allosteric regulation in mtHsp70s: in vivo significance of domain communication and its implications in protein translocation Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (Hsp70/DnaK)Expression profile in rice panicle: insights into heat response mechanism at reproductive stage.The specialized Hsp70 (HscA) interdomain linker binds to its nucleotide-binding domain and stimulates ATP hydrolysis in both cis and trans configurations.C-terminal amino acids are essential for human heat shock protein 70 dimerization Chemical screens against a reconstituted multiprotein complex: myricetin blocks DnaJ regulation of DnaK through an allosteric mechanism Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones 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.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 Gene Expression Profile in the Long-Living Lotus: Insights into the Heat Stress Response Mechanism.Simulation of the opening and closing of Hsp70 chaperones by coarse-grained molecular dynamics Intrinsic negative feedback governs activation surge in two-component regulatory systems.Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.Inducible hsp70 in the regulation of cancer cell survival: analysis of chaperone induction, expression and activity Structural mechanisms of chaperone mediated protein disaggregation.Heat shock protein 70 inhibitors. 1. 2,5'-thiodipyrimidine and 5-(phenylthio)pyrimidine acrylamides as irreversible binders to an allosteric site on heat shock protein 70 Identification of an allosteric pocket on human hsp70 reveals a mode of inhibition of this therapeutically important protein.The remarkable multivalency of the Hsp70 chaperones.An atomistic view of Hsp70 allosteric crosstalk: from the nucleotide to the substrate binding domain and back Allosteric drugs: the interaction of antitumor compound MKT-077 with human Hsp70 chaperones.An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones.An interdomain sector mediating allostery in Hsp70 molecular chaperones.Millisecond dynamics in the allosteric enzyme imidazole glycerol phosphate synthase (IGPS) from Thermotoga maritima.Toward understanding allosteric signaling mechanisms in the ATPase domain of molecular chaperones.

P2860

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P2860

Allostery in Hsp70 chaperones is transduced by subdomain rotations

http://www.wikidata.org/entity/Q28752577

description

2009 nî lūn-bûn

@nan

2009 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Allostery in Hsp70 chaperones is transduced by subdomain rotations

@ast

Allostery in Hsp70 chaperones is transduced by subdomain rotations

@en

Allostery in Hsp70 chaperones is transduced by subdomain rotations

@nl

type

label

Allostery in Hsp70 chaperones is transduced by subdomain rotations

@ast

Allostery in Hsp70 chaperones is transduced by subdomain rotations

@en

Allostery in Hsp70 chaperones is transduced by subdomain rotations

@nl

prefLabel

Allostery in Hsp70 chaperones is transduced by subdomain rotations

@ast

Allostery in Hsp70 chaperones is transduced by subdomain rotations

@en

Allostery in Hsp70 chaperones is transduced by subdomain rotations

@nl

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J.JMB.2009.01.062

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Journal of Molecular Biology

P1476

Allostery in Hsp70 chaperones is transduced by subdomain rotations

@en

P2093

Akash Bhattacharya

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

Alexander V Kurochkin

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

Grover N B Yip

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

Yongbo Zhang

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

P2860

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

Structural insights into substrate binding by the molecular chaperone DnaK

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

The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG

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

Structure of the Hsp110:Hsc70 nucleotide exchange machine.

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

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

Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

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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475-490

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5008484

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10.1016/J.JMB.2009.01.062

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3

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388

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2009-02-04T00:00:00Z

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24272854

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19361428

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molecular chaperones

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2693909

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