(Q35764464)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22063096%20AND%20SRC:MED&resulttype=core&format=json

16 January 2020

title

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

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22063096%20AND%20SRC:MED&resulttype=core&format=json

16 January 2020

0 references

2

1 reference

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16 January 2020

Matthias P. Mayer

5

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22063096%20AND%20SRC:MED&resulttype=core&format=json

16 January 2020

1

Timothy O Street

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22063096%20AND%20SRC:MED&resulttype=core&format=json

16 January 2020

author name string

Kliment A Verba

3

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22063096%20AND%20SRC:MED&resulttype=core&format=json

16 January 2020

Chung-Tien Lee

4

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22063096%20AND%20SRC:MED&resulttype=core&format=json

16 January 2020

David A Agard

6

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22063096%20AND%20SRC:MED&resulttype=core&format=json

16 January 2020

language of work or name

English

0 references

publication date

31 October 2011

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22063096%20AND%20SRC:MED&resulttype=core&format=json

Journal of Molecular Biology

16 January 2020

published in

1 reference

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16 January 2020

volume

415

1 reference

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16 January 2020

issue

1

1 reference

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16 January 2020

page(s)

3-15

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22063096%20AND%20SRC:MED&resulttype=core&format=json

Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex

16 January 2020

cites work

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

Charge-rich regions modulate the anti-aggregation activity of Hsp90.

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

DANGLE: A Bayesian inferential method for predicting protein backbone dihedral angles and secondary structure.

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

Structure of an Hsp90-Cdc37-Cdk4 complex.

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

Structure and mechanism of the Hsp90 molecular chaperone machinery

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

Combinatorial attack on multistep oncogenesis by inhibiting the Hsp90 molecular chaperone

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

ARIA: automated NOE assignment and NMR structure calculation

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

Hsp90: a specialized but essential protein-folding tool

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

Osmolyte-induced conformational changes in the Hsp90 molecular chaperone

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

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

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

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

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

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

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

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

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

Conserved conformational changes in the ATPase cycle of human Hsp90.

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

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

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

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

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

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

25 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

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

25 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

A common conformationally coupled ATPase mechanism for yeast and human cytoplasmic HSP90s

25 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

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

25 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

Intrinsic inhibition of the Hsp90 ATPase activity

25 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

Fast mapping of protein-protein interfaces by NMR spectroscopy

25 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

Coordinated ATP hydrolysis by the Hsp90 dimer

25 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3282117

Asymmetric Activation of the Hsp90 Dimer by Its Cochaperone Aha1

25 September 2018

1 reference

12 December 2020

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

1 reference

12 December 2020

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

1 reference

12 December 2020

In vitro evidence that hsp90 contains two independent chaperone sites

1 reference

12 December 2020

10.1016/J.JMB.2011.10.038

Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22063096%20AND%20SRC:MED&resulttype=core&format=json

16 January 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22063096%20AND%20SRC:MED&resulttype=core&format=json

16 January 2020

1 reference