(Q27676637)

5

0 references

Marc B Cox

object named as

Marc B Cox

7

0 references

Klaus Richter

object named as

Klaus Richter

9

0 references

author name string

Andreas B Schmid

1

0 references

Stephan Lagleder

2

0 references

Melissa Ann Gräwert

3

0 references

Alina Röhl

4

0 references

Sebastian K Wandinger

6

0 references

Oliver Demmer

8

0 references

Horst Kessler

11

0 references

Johannes Buchner

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

12

0 references

language of work or name

English

0 references

publication date

21 March 2012

0 references

published in

The EMBO Journal

0 references

volume

31

0 references

issue

6

0 references

page(s)

1506-17

0 references

cites work

1 reference

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

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

20 March 2017

1 reference

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

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

20 March 2017

1 reference

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

The CCP4 suite: programs for protein crystallography

20 March 2017

1 reference

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

The Xplor-NIH NMR molecular structure determination package

20 March 2017

1 reference

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

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

20 March 2017

1 reference

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

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

20 March 2017

1 reference

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

Sti1 Is a Novel Activator of the Ssa Proteins

20 March 2017

1 reference

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

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

20 March 2017

1 reference

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

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

20 March 2017

1 reference

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

In vivo analysis of the Hsp90 cochaperone Sti1 (p60)

20 March 2017

1 reference

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

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

20 March 2017

1 reference

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

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

20 March 2017

1 reference

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

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

20 March 2017

1 reference

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

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

20 March 2017

1 reference

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

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

20 March 2017

1 reference

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

Hop modulates Hsp70/Hsp90 interactions in protein folding

20 March 2017

1 reference

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

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

20 March 2017

1 reference

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

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

20 March 2017

1 reference

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

HSP90 at the hub of protein homeostasis: emerging mechanistic insights

20 March 2017

1 reference

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

The HADDOCK web server for data-driven biomolecular docking

7 April 2017

1 reference

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

Pathways of chaperone-mediated protein folding in the cytosol

7 April 2017

1 reference

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

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

7 April 2017

1 reference

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

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

7 April 2017

1 reference

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

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

29 September 2017

1 reference

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

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

29 September 2017

1 reference

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

The Hsp90 chaperone machinery

29 September 2017

1 reference

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

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

29 September 2017

1 reference

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

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

29 September 2017

1 reference

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

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

29 September 2017

1 reference

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

Hsp90 at the crossroads of genetics and epigenetics

29 September 2017

1 reference

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

Chaperoning steroid hormone action

29 September 2017

1 reference

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

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

29 September 2017

1 reference

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

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

29 September 2017

1 reference

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

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

29 September 2017

1 reference

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

Hop: more than an Hsp70/Hsp90 adaptor protein

29 September 2017

1 reference

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

Hsp90 chaperones wild-type p53 tumor suppressor protein

29 September 2017

1 reference

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

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

29 September 2017

1 reference

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

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

29 September 2017

1 reference

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

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

29 September 2017

1 reference

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

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

29 September 2017

1 reference

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

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

29 September 2017

1 reference

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

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

2 June 2018

1 reference

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

Reconstitution of progesterone receptor with heat shock proteins

2 June 2018

1 reference

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

An efficient strategy for assignment of cross-peaks in 3D heteronuclear NOESY experiments

2 June 2018

1 reference

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

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

27 November 2018

1 reference

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

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

27 November 2018

1 reference

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

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

27 November 2018

1 reference

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

Substrate transfer from the chaperone Hsp70 to Hsp90.

27 November 2018

1 reference

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

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

27 November 2018

1 reference

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

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

27 November 2018

1 reference

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

Automated backbone assignment of labeled proteins using the threshold accepting algorithm

27 November 2018

1 reference

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

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

27 November 2018

1 reference

PubMed

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

12 December 2020

inferred from PubMed ID database lookup

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

1 reference

PubMed

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

12 December 2020

inferred from PubMed ID database lookup

Chaperone function of Hsp90-associated proteins

1 reference

PubMed

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

12 December 2020

inferred from PubMed ID database lookup

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

1 reference

Crossref

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

7 January 2021

inferred from DOI database lookup

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

1 reference

Crossref

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

7 January 2021

inferred from DOI database lookup

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

1 reference

Crossref

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

7 January 2021

inferred from DOI database lookup

Identifiers

DOI

10.1038/EMBOJ.2011.472

1 reference

1 reference

1 reference

PubMed publication ID

22227520

1 reference