(Q41281023)

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Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites (English)

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

object named as

Klaus Richter

6

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author name string

Julia M Eckl

1

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

Daniel A Rutz

2

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

Veronika Haslbeck

3

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

Bettina K Zierer

4

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

Jochen Reinstein

5

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

language of work or name

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publication date

8 April 2013

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

288

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

22

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

16032-16042

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

Hsp90 in non-mammalian metazoan model systems

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

Cdc37-Hsp90 complexes are responsive to nucleotide-induced conformational changes and binding of further cofactors

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

Biological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

The human Cdc37.Hsp90 complex studied by heteronuclear NMR spectroscopy

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

The Hsp90 chaperone machinery

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

Structure of an Hsp90-Cdc37-Cdk4 complex.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

Hsp90 and Cdc37 -- a chaperone cancer conspiracy.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

Hsp90 isoforms: functions, expression and clinical importance

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

Cdc37 goes beyond Hsp90 and kinases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

Structure and functional relationships of Hsp90.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

Hsp90: chaperoning signal transduction

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

p50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

The induction of gene activity in drosophila by heat shock

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

1 October 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

14 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

14 June 2018

Conserved conformational changes in the ATPase cycle of human Hsp90.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

14 June 2018

The heat-shock response in cultured cells exposed to ethanol and its metabolites

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

14 June 2018

Reduced levels of hsp90 compromise steroid receptor action in vivo

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

14 June 2018

Characterization of the interaction of Aha1 with components of the Hsp90 chaperone machine and client proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

19 August 2018

The non-canonical Hop protein from Caenorhabditis elegans exerts essential functions and forms binary complexes with either Hsc70 or Hsp90.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

19 August 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

19 August 2018

Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

19 August 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

19 August 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

19 August 2018

A positive feedback loop between protein kinase CKII and Cdc37 promotes the activity of multiple protein kinases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

19 August 2018

Binding of hsp90-associated immunophilins to cytoplasmic dynein: direct binding and in vivo evidence that the peptidylprolyl isomerase domain is a dynein interaction domain

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

19 August 2018

Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3668759

19 August 2018

A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains

1 reference

https://pubmed.ncbi.nlm.nih.gov/23569206

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Asymmetric Activation of the Hsp90 Dimer by Its Cochaperone Aha1

1 reference

https://pubmed.ncbi.nlm.nih.gov/23569206

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle

1 reference

https://pubmed.ncbi.nlm.nih.gov/23569206

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1074/JBC.M112.439257

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

ResearchGate publication ID

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