Effect of mutation of the tetratricopeptide repeat and asparatate-proline 2 domains of Sti1 on Hsp90 signaling and interaction in Saccharomyces cerevisiae (Q34587324)

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Language	Label	Description	Also known as
English	Effect of mutation of the tetratricopeptide repeat and asparatate-proline 2 domains of Sti1 on Hsp90 signaling and interaction in Saccharomyces cerevisiae	scientific article

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

3 August 2017

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

1 reference

Europe PubMed Central

PubMed publication ID

3 August 2017

Saccharomyces cerevisiae

1 reference

based on heuristic

inferred from title

author name string

Gary Flom

1

1 reference

Europe PubMed Central

PubMed publication ID

3 August 2017

Janae Weekes

2

1 reference

Europe PubMed Central

PubMed publication ID

3 August 2017

Julia J Williams

3

1 reference

Europe PubMed Central

PubMed publication ID

3 August 2017

Jill L Johnson

4

1 reference

Europe PubMed Central

PubMed publication ID

3 August 2017

language of work or name

0 references

publication date

11 October 2005

1 reference

Europe PubMed Central

PubMed publication ID

3 August 2017

1 reference

Europe PubMed Central

PubMed publication ID

3 August 2017

172

1 reference

Europe PubMed Central

PubMed publication ID

3 August 2017

1

1 reference

Europe PubMed Central

PubMed publication ID

3 August 2017

41-51

1 reference

Europe PubMed Central

PubMed publication ID

3 August 2017

Independent regulation of Hsp70 and Hsp90 chaperones by Hsp70/Hsp90-organizing protein Sti1 (Hop1).

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

Novel interaction of the Hsp90 chaperone machine with Ssl2, an essential DNA helicase in Saccharomyces cerevisiae

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

Tetratricopeptide repeat cochaperones in steroid receptor complexes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

Hop: more than an Hsp70/Hsp90 adaptor protein

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

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=1456168

7 July 2018

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=1456168

7 July 2018

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=1456168

7 July 2018

Overview: Translating Hsp90 Biology into Hsp90 Drugs

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

Sti1 Is a Novel Activator of the Ssa Proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

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=1456168

7 July 2018

Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

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=1456168

7 July 2018

Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

Hsp104 interacts with Hsp90 cochaperones in respiring yeast

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

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=1456168

7 July 2018

A role for the Hsp40 Ydj1 in repression of basal steroid receptor activity in yeast

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

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=1456168

7 July 2018

Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

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=1456168

7 July 2018

Two eukaryote-specific regions of Hsp82 are dispensable for its viability and signal transduction functions in yeast

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

The Ydj1 molecular chaperone facilitates formation of active p60v-src in yeast

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

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=1456168

7 July 2018

Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

7 July 2018

Functional comparison of human and Drosophila Hop reveals novel role in steroid receptor maturation.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

27 October 2018

Multiple domains of the co-chaperone Hop are important for Hsp70 binding.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456168

27 October 2018

Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways

1 reference

https://pubmed.ncbi.nlm.nih.gov/16219779

12 December 2020

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10.1534/GENETICS.105.045815

1 reference

Europe PubMed Central

PubMed publication ID

3 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

3 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

3 August 2017

ResearchGate publication ID

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