(Q35018042)

5 August 2017

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

1 reference

5 August 2017

0 references

1

Timothy O Street

1 reference

5 August 2017

Laura A Lavery

2

1 reference

PubMed ID

21474071

5 August 2017

David A Agard

series ordinal

3

1 reference

5 August 2017

1 April 2011

1 reference

5 August 2017

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5 August 2017

42

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5 August 2017

1

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5 August 2017

96-105

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PubMed ID

21474071

describes a project that uses

5 August 2017

ImageQuant

1 reference

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC3105473/fullTextXML

inferred from PubMed Central ID database lookup

cites work

HSP90 at the hub of protein homeostasis: emerging mechanistic insights

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

Osmolyte-induced conformational changes in the Hsp90 molecular chaperone

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

The molecular chaperone Hsp90 modulates intermediate steps of amyloid assembly of the Parkinson-related protein alpha-synuclein.

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

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

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

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

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

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

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

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

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

Structural studies on the co-chaperone Hop and its complexes with Hsp90.

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

Apo-Hsp90 coexists in two open conformational states in solution.

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

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

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

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

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

Structure of an Hsp90-Cdc37-Cdk4 complex.

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

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

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

The expanded denatured state: an ensemble of conformations trapped in a locally encoded topological space

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

CRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90.

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

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

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

Hsp90: a specialized but essential protein-folding tool

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

Stable association of hsp90 and p23, but Not hsp70, with active human telomerase

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

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

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

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

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

Initial studies of the equilibrium folding pathway of staphylococcal nuclease

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

Residual structure in large fragments of staphylococcal nuclease: effects of amino acid substitutions.

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

Hsp90 chaperones protein folding in vitro.

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

Ribosomal protein L2 associates with E. coli HtpG and activates its ATPase activity

8 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

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

25 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

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

25 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

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

25 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

Biochemical and structural studies of the interaction of Cdc37 with Hsp90.

25 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

Effects of denaturants and substitutions of hydrophobic residues on backbone dynamics of denatured staphylococcal nuclease

25 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3105473

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

25 October 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/21474071

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/21474071

12 December 2020

inferred from PubMed ID database lookup

Forcing thermodynamically unfolded proteins to fold

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/21474071

12 December 2020

inferred from PubMed ID database lookup

Identifiers

DOI

10.1016/J.MOLCEL.2011.01.029

1 reference

5 August 2017

1 reference

5 August 2017

1 reference

PubMed ID

21474071