The co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922 (Q28485166)

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English	The co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922	scientific article

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scholarly article

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The co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922 (English)

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molecular chaperones

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Heather Armstrong

object named as

Heather Armstrong

1

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ORCID Public Data File 2021

author name string

Annemarie Wolmarans

2

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Rebecca Mercier

3

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BaoChan Mai

4

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Paul LaPointe

5

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language of work or name

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publication date

2012

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7

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11

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e49322

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copyright license

Creative Commons Attribution 4.0 International

14 November 2012

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April 2022 Public Data File from Crossref

copyright status

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The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones

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19 March 2017

The ‘active life’ of Hsp90 complexes

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19 March 2017

Threonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activity

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Targeting the dynamic HSP90 complex in cancer

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19 March 2017

NVP-AUY922: a small molecule HSP90 inhibitor with potent antitumor activity in preclinical breast cancer models

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19 March 2017

NVP-AUY922: a novel heat shock protein 90 inhibitor active against xenograft tumor growth, angiogenesis, and metastasis

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19 March 2017

Chaperone ligand-discrimination by the TPR-domain protein Tah1.

1 reference

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19 March 2017

Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis

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19 March 2017

The molecular chaperone Hsp90 is required for high osmotic stress response in Saccharomyces cerevisiae

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19 March 2017

Cooperation of heat shock protein 90 and p23 in aryl hydrocarbon receptor signaling

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19 March 2017

Global analysis of protein expression in yeast

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

19 March 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=3498168

19 March 2017

Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

19 March 2017

Phosphorylation and hsp90 binding mediate heat shock stabilization of p53

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

19 March 2017

Hsp90: a specialized but essential protein-folding tool

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

19 March 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=3498168

19 March 2017

Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

19 March 2017

The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

19 March 2017

Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

19 March 2017

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

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

19 March 2017

In vivo analysis of the Hsp90 cochaperone Sti1 (p60)

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

19 March 2017

Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

19 March 2017

Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds

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19 March 2017

A positive selection for mutants lacking orotidine-5'-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

19 March 2017

Transformation of intact yeast cells treated with alkali cations

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

19 March 2017

Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product

1 reference

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19 March 2017

hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

19 March 2017

HSP90 at the hub of protein homeostasis: emerging mechanistic insights

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

7 April 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

7 April 2017

Heat shock protein 90's mechanochemical cycle is dominated by thermal fluctuations

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

29 September 2017

A compound that inhibits the HOP-Hsp90 complex formation and has unique killing effects in breast cancer cell lines

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

29 September 2017

Conformational dynamics of the molecular chaperone Hsp90

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29 September 2017

Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function

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29 September 2017

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

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29 September 2017

Update on Hsp90 inhibitors in clinical trial.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

29 September 2017

Signalling profile and antitumour activity of the novel Hsp90 inhibitor NVP-AUY922 in multiple myeloma.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

29 September 2017

An acetylation site in the middle domain of Hsp90 regulates chaperone function

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

29 September 2017

Nucleotide-dependent interaction of Saccharomyces cerevisiae Hsp90 with the cochaperone proteins Sti1, Cpr6, and Sba1.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

29 September 2017

The middle domain of Hsp90 acts as a discriminator between different types of client proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

29 September 2017

Effect of mutation of the tetratricopeptide repeat and asparatate-proline 2 domains of Sti1 on Hsp90 signaling and interaction in Saccharomyces cerevisiae

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

29 September 2017

Hsp90 restrains ErbB-2/HER2 signalling by limiting heterodimer formation

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

29 September 2017

Roles of molecular chaperones in protein misfolding diseases

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

29 September 2017

The achilles heel of ErbB-2/HER2: regulation by the Hsp90 chaperone machine and potential for pharmacological intervention.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

29 September 2017

Sensitivity to Hsp90-targeting drugs can arise with mutation to the Hsp90 chaperone, cochaperones and plasma membrane ATP binding cassette transporters of yeast

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

29 September 2017

Heat shock protein 90-antagonist destabilizes Bcr-Abl/HSP90 chaperone complex

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

29 September 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=3498168

29 September 2017

Heat-shock protein hsp90 governs the activity of pp60v-src kinase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

29 September 2017

Ancient heat shock gene is dispensable

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

29 September 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=3498168

2 June 2018

A non-toxic Hsp90 inhibitor protects neurons from Abeta-induced toxicity

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https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0049322

21 January 2018

Substrate transfer from the chaperone Hsp70 to Hsp90.

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https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0049322

21 January 2018

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

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https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0049322

21 January 2018

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

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https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0049322

21 January 2018

System of centromeric, episomal, and integrative vectors based on drug resistance markers for Saccharomyces cerevisiae.

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https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0049322

21 January 2018

The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle

1 reference

https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0049322

21 January 2018

Yeast is selectively hypersensitised to heat shock protein 90 (Hsp90)-targetting drugs with heterologous expression of the human Hsp90beta, a property that can be exploited in screens for new Hsp90 chaperone inhibitors

1 reference

https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0049322

21 January 2018

Histone deacetylase inhibitor LAQ824 both lowers expression and promotes proteasomal degradation of Bcr-Abl and induces apoptosis of imatinib mesylate-sensitive or -refractory chronic myelogenous leukemia-blast crisis cells.

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3498168

27 November 2018

Modulation of p53, ErbB1, ErbB2, and Raf-1 expression in lung cancer cells by depsipeptide FR901228

1 reference

https://pubmed.ncbi.nlm.nih.gov/23166640

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Binding of p23 and hsp90 during assembly with the progesterone receptor

1 reference

https://pubmed.ncbi.nlm.nih.gov/23166640

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/23166640

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1371/JOURNAL.PONE.0049322

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2012PLoSO...749322A

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OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PMC publication ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

ResearchGate publication ID

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