Literature DB >> 17055424

hsp90: twist and fold.

Klaus Richter1, Johannes Buchner.   

Abstract

Molecular chaperones are cellular machines that facilitate protein folding. The crystal structures of HtpG, the Escherichia coli homolog of hsp90, reported in this issue (Shiau et al., 2006) together with the recently published structures of an hsp90-cochaperone complex (Ali et al., 2006) and an hsp90-client protein complex (Vaughan et al., 2006), reveal exciting insights into the hsp90 reaction cycle.

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Year:  2006        PMID: 17055424     DOI: 10.1016/j.cell.2006.10.004

Source DB:  PubMed          Journal:  Cell        ISSN: 0092-8674            Impact factor:   41.582


  19 in total

Review 1.  GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum.

Authors:  Michal Marzec; Davide Eletto; Yair Argon
Journal:  Biochim Biophys Acta       Date:  2011-11-03

2.  Hsp90 cochaperone Aha1 is a negative regulator of the Saccharomyces MAL activator and acts early in the chaperone activation pathway.

Authors:  Fulai Ran; Nidhi Gadura; Corinne A Michels
Journal:  J Biol Chem       Date:  2010-02-22       Impact factor: 5.157

3.  N-terminal domain of human Hsp90 triggers binding to the cochaperone p23.

Authors:  G Elif Karagöz; Afonso M S Duarte; Hans Ippel; Charlotte Uetrecht; Tessa Sinnige; Martijn van Rosmalen; Jens Hausmann; Albert J R Heck; Rolf Boelens; Stefan G D Rüdiger
Journal:  Proc Natl Acad Sci U S A       Date:  2010-12-23       Impact factor: 11.205

Review 4.  The protective and destructive roles played by molecular chaperones during ERAD (endoplasmic-reticulum-associated degradation).

Authors:  Jeffrey L Brodsky
Journal:  Biochem J       Date:  2007-06-15       Impact factor: 3.857

5.  Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms.

Authors:  Jill L Johnson; Celeste Brown
Journal:  Cell Stress Chaperones       Date:  2008-07-18       Impact factor: 3.667

Review 6.  Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin.

Authors:  Gabriel M Altschuler; Keith R Willison
Journal:  J R Soc Interface       Date:  2008-12-06       Impact factor: 4.118

7.  Exploiting conformational dynamics in drug discovery: design of C-terminal inhibitors of Hsp90 with improved activities.

Authors:  Elisabetta Moroni; Huiping Zhao; Brian S J Blagg; Giorgio Colombo
Journal:  J Chem Inf Model       Date:  2014-01-15       Impact factor: 4.956

8.  Chemical Perturbation of Oncogenic Protein Folding: from the Prediction of Locally Unstable Structures to the Design of Disruptors of Hsp90-Client Interactions.

Authors:  Antonella Paladino; Mark R Woodford; Sarah J Backe; Rebecca A Sager; Priyanka Kancherla; Michael A Daneshvar; Victor Z Chen; Dimitra Bourboulia; Elham F Ahanin; Chrisostomos Prodromou; Greta Bergamaschi; Alessandro Strada; Marina Cretich; Alessandro Gori; Marina Veronesi; Tiziano Bandiera; Renzo Vanna; Gennady Bratslavsky; Stefano A Serapian; Mehdi Mollapour; Giorgio Colombo
Journal:  Chemistry       Date:  2020-07-08       Impact factor: 5.236

9.  Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle.

Authors:  C Ratzke; M Mickler; B Hellenkamp; J Buchner; T Hugel
Journal:  Proc Natl Acad Sci U S A       Date:  2010-08-24       Impact factor: 11.205

10.  The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis.

Authors:  Moritz Mickler; Martin Hessling; Christoph Ratzke; Johannes Buchner; Thorsten Hugel
Journal:  Nat Struct Mol Biol       Date:  2009-02-22       Impact factor: 15.369

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