The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop (Q27676637)

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Language	Label	Description	Also known as
English	The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop	scientific article

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scholarly article

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

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molecular chaperones

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10

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object named as

Franz Hagn

5

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object named as

Marc B Cox

7

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object named as

Klaus Richter

9

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author name string

Andreas B Schmid

1

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Stephan Lagleder

2

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Melissa Ann Gräwert

3

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Alina Röhl

4

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Sebastian K Wandinger

6

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Oliver Demmer

8

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Horst Kessler

11

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Johannes Buchner

12

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language of work or name

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publication date

21 March 2012

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The EMBO Journal

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31

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6

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1506-17

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Electrostatic Interactions of Hsp-organizing Protein Tetratricopeptide Domains with Hsp70 and Hsp90: COMPUTATIONAL ANALYSIS AND PROTEIN ENGINEERING

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20 March 2017

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

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

20 March 2017

The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies

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20 March 2017

The CCP4 suite: programs for protein crystallography

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20 March 2017

The Xplor-NIH NMR molecular structure determination package

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

20 March 2017

Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

20 March 2017

Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

20 March 2017

Sti1 Is a Novel Activator of the Ssa Proteins

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

20 March 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=3321170

20 March 2017

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=3321170

20 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=3321170

20 March 2017

HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

20 March 2017

The Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

20 March 2017

The tetratricopeptide repeat: a structural motif mediating protein-protein interactions

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

20 March 2017

An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

20 March 2017

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=3321170

20 March 2017

Hop modulates Hsp70/Hsp90 interactions in protein folding

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

20 March 2017

The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

20 March 2017

Hsp90 regulates the activity of wild type p53 under physiological and elevated temperatures

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

20 March 2017

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=3321170

7 April 2017

The HADDOCK web server for data-driven biomolecular docking

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

7 April 2017

Pathways of chaperone-mediated protein folding in the cytosol

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

7 April 2017

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=3321170

7 April 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

29 September 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=3321170

29 September 2017

HOP is a monomer: investigation of the oligomeric state of the co-chaperone HOP.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

29 September 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=3321170

29 September 2017

The Hsp90 molecular chaperone: an open and shut case for treatment

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

29 September 2017

Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

29 September 2017

p53--a natural cancer killer: structural insights and therapeutic concepts

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

29 September 2017

Hsp90 at the crossroads of genetics and epigenetics

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

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Chaperoning steroid hormone action

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

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=3321170

29 September 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=3321170

29 September 2017

Functional specificity of co-chaperone interactions with Hsp90 client proteins.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

29 September 2017

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=3321170

29 September 2017

Hsp90 chaperones wild-type p53 tumor suppressor protein

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

29 September 2017

Comparison of the carboxy-terminal DP-repeat region in the co-chaperones Hop and Hip.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

29 September 2017

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=3321170

29 September 2017

Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

29 September 2017

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1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

29 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

2 June 2018

Definition of the minimal fragments of Sti1 required for dimerization, interaction with Hsp70 and Hsp90 and in vivo functions

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

2 June 2018

Reconstitution of progesterone receptor with heat shock proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

2 June 2018

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1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

27 November 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=3321170

27 November 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=3321170

27 November 2018

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

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

27 November 2018

Substrate transfer from the chaperone Hsp70 to Hsp90.

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3321170

27 November 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=3321170

27 November 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=3321170

27 November 2018

Automated backbone assignment of labeled proteins using the threshold accepting algorithm

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27 November 2018

Molecular chaperone machines: chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23

1 reference

https://pubmed.ncbi.nlm.nih.gov/22227520

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb

1 reference

https://pubmed.ncbi.nlm.nih.gov/22227520

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Chaperone function of Hsp90-associated proteins

1 reference

https://pubmed.ncbi.nlm.nih.gov/22227520

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The tetratricopeptide repeat: a structural motif mediating protein-protein interactions

1 reference

https://api.crossref.org/works/10.1038%2FEMBOJ.2011.472

7 January 2021

based on heuristic

inferred from DOI database lookup

The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes

1 reference

https://api.crossref.org/works/10.1038%2FEMBOJ.2011.472

7 January 2021

based on heuristic

inferred from DOI database lookup

Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants

1 reference

https://api.crossref.org/works/10.1038%2FEMBOJ.2011.472

7 January 2021

based on heuristic

inferred from DOI database lookup

Identifiers

10.1038/EMBOJ.2011.472

1 reference

Consolidated OpenCitations Corpus – April 2017

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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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