Nanomechanics of the substrate binding domain of Hsp70 determine its allosteric ATP-induced conformational change.

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The β6/β7 region of the Hsp70 substrate-binding domain mediates heat-shock response and prion propagation.

P2860

Q47417959-F5F699CB-4C78-4FEC-B3CD-60877D477946

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Nanomechanics of the substrate binding domain of Hsp70 determine its allosteric ATP-induced conformational change.

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http://www.wikidata.org/entity/Q36378270

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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Nanomechanics of the substrate ...... induced conformational change.

@ast

Nanomechanics of the substrate ...... induced conformational change.

@en

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Item

label

Nanomechanics of the substrate ...... induced conformational change.

@ast

Nanomechanics of the substrate ...... induced conformational change.

@en

prefLabel

Nanomechanics of the substrate ...... induced conformational change.

@ast

Nanomechanics of the substrate ...... induced conformational change.

@en

P1476

Nanomechanics of the substrate ...... induced conformational change.

@en

P2093

Matthias Rief

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

Maximilian Buchsteiner

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

Ruxandra I Dima

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

Soumit Sankar Mandal

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

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Structural insights into substrate binding by the molecular chaperone DnaK

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

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

Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones

Structural studies on the forward and reverse binding modes of peptides to the chaperone DnaK

Structural analysis of substrate binding by the molecular chaperone DnaK

NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction

Structural basis for the inhibition of HSP70 and DnaK chaperones by small-molecule targeting of a C-terminal allosteric pocket

Substrate-binding domain conformational dynamics mediate Hsp70 allostery

P304

6040-6045

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

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scholarly article

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10.1073/PNAS.1619843114

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

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English

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

P478

114

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

P50

Gabriel Zoldak

Dale R Merz

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2017-05-22T00:00:00Z

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

P698

28533394

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

P932

5468673

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

Nanomechanics of the substrate binding domain of Hsp70 determine its allosteric ATP-induced conformational change.

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P2860

P2860

Nanomechanics of the substrate binding domain of Hsp70 determine its allosteric ATP-induced conformational change.

description

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type

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prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932