(Q37661766)

21 August 2017

Elucidating the mechanism of substrate recognition by the bacterial Hsp90 molecular chaperone (English)

1 reference

21 August 2017

0 references

5

Andrej Sali

0 references

Timothy O Street

1

object named as

Timothy O Street

1 reference

21 August 2017

Xiaohui Zeng

2

1 reference

21 August 2017

Riccardo Pellarin

3

1 reference

21 August 2017

Massimiliano Bonomi

4

1 reference

21 August 2017

Mark J S Kelly

6

1 reference

21 August 2017

Feixia Chu

7

1 reference

21 August 2017

David A Agard

8

1 reference

21 August 2017

language of work or name

English

0 references

publication date

12 April 2014

1 reference

Journal of Molecular Biology

21 August 2017

1 reference

21 August 2017

426

1 reference

21 August 2017

12

1 reference

21 August 2017

2393-2404

1 reference

describes a project that uses

21 August 2017

ImageJ

1 reference

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC5322795/fullTextXML

inferred from PubMed Central ID database lookup

cites work

Structural Asymmetry in the Closed State of Mitochondrial Hsp90 (TRAP1) Supports a Two-Step ATP Hydrolysis Mechanism

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

The molecular chaperone gp96/GRP94 interacts with Toll-like receptors and integrins via its C-terminal hydrophobic domain

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activity

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

The client protein p53 adopts a molten globule-like state in the presence of Hsp90.

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

Xlink-identifier: an automated data analysis platform for confident identifications of chemically cross-linked peptides using tandem mass spectrometry

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

xComb: a cross-linked peptide database approach to protein-protein interaction analysis

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

Protein refolding by pH-triggered chaperone binding and release

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

Finding chimeras: a bioinformatics strategy for identification of cross-linked peptides

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

Bleach activates a redox-regulated chaperone by oxidative protein unfolding

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

Identification of cross-linked peptides from large sequence databases

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

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

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

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

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

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

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

Some like it hot: the structure and function of small heat-shock proteins.

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

Unraveling the interface of signal recognition particle and its receptor by using chemical cross-linking and tandem mass spectrometry

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

A model of the changes in denatured state structure underlying m value effects in staphylococcal nuclease

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

Isolation of Hsp90 mutants by screening for decreased steroid receptor function

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

Hydrogen exchange in unligated and ligated staphylococcal nuclease

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: a heteronuclear NMR study

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

Electrophoretic characterization of the denatured states of staphylococcal nuclease

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

Truncated staphylococcal nuclease is compact but disordered

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

Hsp90 and client protein maturation

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

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

25 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

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

25 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

Conserved conformational changes in the ATPase cycle of human Hsp90.

25 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

The foldon substructure of staphylococcal nuclease

25 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

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

25 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5322795

Protein conformational stabilities can be determined from hydrogen exchange rates

1 September 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/24726919

12 December 2020

inferred from PubMed ID database lookup

Backbone dynamics of a highly disordered 131 residue fragment of staphylococcal nuclease

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/24726919

12 December 2020

inferred from PubMed ID database lookup

The equilibrium folding pathway of staphylococcal nuclease: identification of the most stable chain-chain interactions by NMR and CD spectroscopy

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/24726919

12 December 2020

inferred from PubMed ID database lookup

Identifiers

DOI

10.1016/J.JMB.2014.04.001

1 reference

21 August 2017

1 reference

21 August 2017

PubMed publication ID

24726919

1 reference