(Q42540989)

English

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

scientific article published on 7 May 2009

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

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 (English)

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

Timothy O Street

3

object named as

Timothy O Street

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

author name string

Kristin A Krukenberg

1

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

Daniel R Southworth

2

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

David A Agard

4

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

language of work or name

0 references

publication date

7 May 2009

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

Journal of Molecular Biology

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

390

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

2

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

278-291

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

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

1 reference

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28 May 2018

Phase II trial of 17-allylamino-17-demethoxygeldanamycin in patients with metastatic melanoma.

1 reference

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28 May 2018

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

1 reference

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28 May 2018

Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90.

1 reference

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28 May 2018

Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90.

1 reference

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28 May 2018

X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution

1 reference

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28 May 2018

Illuminating the mechanistic roles of enzyme conformational dynamics

1 reference

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28 May 2018

Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones

1 reference

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28 May 2018

Heat shock protein 90: the cancer chaperone

1 reference

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28 May 2018

Molecular chaperones and protein kinase quality control.

1 reference

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28 May 2018

Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements

1 reference

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28 May 2018

Chaperoning steroid hormone action

1 reference

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28 May 2018

Structure and mechanism of the Hsp90 molecular chaperone machinery

1 reference

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28 May 2018

Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex

1 reference

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28 May 2018

Effect of hsp70 chaperone on the folding and misfolding of polypeptides modeling an elongating protein chain

1 reference

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28 May 2018

Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone

1 reference

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28 May 2018

Pathways of chaperone-mediated protein folding in the cytosol

1 reference

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28 May 2018

Use of non-crystallographic symmetry in protein structure refinement

1 reference

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28 May 2018

Negative staining and image classification — powerful tools in modern electron microscopy

1 reference

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28 May 2018

Combinatorial attack on multistep oncogenesis by inhibiting the Hsp90 molecular chaperone

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2735500

28 May 2018

Heat shock protein 90.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2735500

28 May 2018

Development of Purine-Scaffold Small Molecule Inhibitors of Hsp90

1 reference

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28 May 2018

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

1 reference

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28 May 2018

Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery

1 reference

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28 May 2018

Heat-shock protein 90, a chaperone for folding and regulation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2735500

28 May 2018

Disassembly of transcriptional regulatory complexes by molecular chaperones

1 reference

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28 May 2018

Stimulation of the weak ATPase activity of human hsp90 by a client protein

1 reference

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28 May 2018

Hsp90: chaperoning signal transduction

1 reference

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28 May 2018

Hsp90: a specialized but essential protein-folding tool

1 reference

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Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing

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28 May 2018

The Hsp70 and Hsp60 chaperone machines

1 reference

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Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence

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1 reference

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28 May 2018

ATP induces a conformational change of the 90-kDa heat shock protein (hsp90).

1 reference

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28 May 2018

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1 reference

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

1 reference

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

1 reference

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1 reference

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1 reference

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Analysis of chaperone function using citrate synthase as nonnative substrate protein

1 reference

https://pubmed.ncbi.nlm.nih.gov/19427321

12 December 2020

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Identifiers

10.1016/J.JMB.2009.04.080

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

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