Activation of the DnaK-ClpB Complex is Regulated by the Properties of the Bound Substrate. (Q52324439)

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23 March 2020

title

Activation of the DnaK-ClpB Complex is Regulated by the Properties of the Bound Substrate (English)

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José Ángel Fernández-Higuero

23 March 2020

author

1

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23 March 2020

author name string

Alejandra Aguado

2

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23 March 2020

Judit Perales-Calvo

3

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23 March 2020

Fernando Moro

4

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23 March 2020

Arturo Muga

5

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23 March 2020

language of work or name

English

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publication date

11 April 2018

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23 March 2020

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volume

8

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issue

1

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page(s)

5796

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Creative Commons Attribution 4.0 International

23 March 2020

copyright license

start time

11 April 2018

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April 2022 Public Data File from Crossref

copyright status

copyrighted

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cites work

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22 June 2018

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22 June 2018

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Disruption of ionic interactions between the nucleotide binding domain 1 (NBD1) and middle (M) domain in Hsp100 disaggregase unleashes toxic hyperactivity and partial independence from Hsp70.

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Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation

13 August 2018

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Mechanics of Hsp70 chaperones enables differential interaction with client proteins.

13 August 2018

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Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions.

13 August 2018

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The conformational dynamics of the mitochondrial Hsp70 chaperone

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Nucleotide utilization requirements that render ClpB active as a chaperone

13 August 2018

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Coupling and dynamics of subunits in the hexameric AAA chaperone ClpB.

13 August 2018

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DnaJ recruits DnaK to protein aggregates

13 August 2018

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M domains couple the ClpB threading motor with the DnaK chaperone activity

13 August 2018

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Amide hydrogen exchange reveals conformational changes in hsp70 chaperones important for allosteric regulation.

13 August 2018

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Characterization of a trap mutant of the AAA chaperone ClpB.

13 August 2018

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Roles of individual domains and conserved motifs of the AAA chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity

13 August 2018

1 reference

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Interdomain interaction through helices A and B of DnaK peptide binding domain

13 August 2018

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Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery.

13 August 2018

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ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli

13 August 2018

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7 January 2021

DnaK-mediated association of ClpB to protein aggregates. A bichaperone network at the aggregate surface

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7 January 2021

A quantitative analysis of the effect of nucleotides and the M domain on the association equilibrium of ClpB

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7 January 2021

Solution structure of native proteins with irregular folds from Raman optical activity

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7 January 2021

Multistep mechanism of substrate binding determines chaperone activity of Hsp70

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Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:29643454 AND SRC:MED&resulttype=core&format=json

23 March 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:29643454 AND SRC:MED&resulttype=core&format=json

23 March 2020

PubMed publication ID

29643454

1 reference