Differences in conformational dynamics within the Hsp90 chaperone family reveal mechanistic insights (Q40568581)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25988145%20AND%20SRC:MED&resulttype=core&format=json

8 March 2020

title

Differences in conformational dynamics within the Hsp90 chaperone family reveal mechanistic insights (English)

1 reference

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8 March 2020

0 references

5

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8 March 2020

author name string

Christian Graf

1

1 reference

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8 March 2020

Chung-Tien Lee

2

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8 March 2020

L Eva Meier-Andrejszki

3

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8 March 2020

Minh T N Nguyen

4

1 reference

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8 March 2020

language of work or name

1 reference

10 June 2014

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25988145%20AND%20SRC:MED&resulttype=core&format=json

Frontiers in molecular biosciences

8 March 2020

published in

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8 March 2020

volume

1

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8 March 2020

page(s)

4

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The ‘active life’ of Hsp90 complexes

8 March 2020

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22 September 2017

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The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site

22 September 2017

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22 September 2017

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Hsp70 and Hsp90--a relay team for protein folding

22 September 2017

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Global analysis of protein expression in yeast

22 September 2017

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The Hsp90 Cochaperone p23 Is the Limiting Component of the Multiprotein Hsp90/Hsp70-based Chaperone System in Vivo Where It Acts to Stabilize the Client Protein·Hsp90 Complex

22 September 2017

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Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions

22 September 2017

1 reference

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Protein analysis by hydrogen exchange mass spectrometry

22 September 2017

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Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1

22 September 2017

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Hsp90: a specialized but essential protein-folding tool

22 September 2017

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Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23.

22 September 2017

1 reference

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Modulation of Akt kinase activity by binding to Hsp90

22 September 2017

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The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains

22 September 2017

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Structure and in vivo function of Hsp90.

22 September 2017

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An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function

22 September 2017

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SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins

22 September 2017

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Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

22 September 2017

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22 September 2017

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22 September 2017

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22 September 2017

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22 September 2017

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22 September 2017

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Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle

25 September 2017

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Dynamics of the regulation of Hsp90 by the co-chaperone Sti1.

17 June 2018

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pH-dependent conformational changes in bacterial Hsp90 reveal a Grp94-like conformation at pH 6 that is highly active in suppression of citrate synthase aggregation

17 June 2018

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Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle

17 June 2018

1 reference

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The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis

17 June 2018

1 reference

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Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90.

20 August 2018

1 reference

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Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine

20 August 2018

1 reference

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Hsp110 is a nucleotide-activated exchange factor for Hsp70.

20 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4428384

Conformational dynamics of the molecular chaperone Hsp90 in complexes with a co-chaperone and anticancer drugs

20 August 2018

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

20 August 2018

1 reference

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The co-chaperone p23 arrests the Hsp90 ATPase cycle to trap client proteins

20 August 2018

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Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle

20 August 2018

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The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle

20 August 2018

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Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery.

20 August 2018

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Mapping temperature-induced conformational changes in the Escherichia coli heat shock transcription factor sigma 32 by amide hydrogen exchange.

20 August 2018

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NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol

20 August 2018

1 reference

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Coordinated ATP hydrolysis by the Hsp90 dimer

20 August 2018

1 reference

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The 43-kilodalton N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs.

20 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4428384

The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes

20 August 2018

1 reference

Crossref

https://api.crossref.org/works/10.3389%2FFMOLB.2014.00004

Nucleotides and two functional states of hsp90

21 January 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/25988145

12 December 2020

inferred from PubMed ID database lookup

Binding of p23 and hsp90 during assembly with the progesterone receptor

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/25988145

12 December 2020

inferred from PubMed ID database lookup

From a ratchet mechanism to random fluctuations evolution of Hsp90's mechanochemical cycle

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/25988145

12 December 2020

inferred from PubMed ID database lookup

Identifiers

DOI

10.3389/FMOLB.2014.00004

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25988145%20AND%20SRC:MED&resulttype=core&format=json

release_u2f722cxjrajflsxmovsxgflbi

8 March 2020

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/u2f722cxjrajflsxmovsxgflbi

24 November 2022

mapped directly with Wikidata item

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25988145%20AND%20SRC:MED&resulttype=core&format=json

8 March 2020

PubMed publication ID

25988145

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25988145%20AND%20SRC:MED&resulttype=core&format=json