Literature DB >> 27434765

Chaperones: Speedy motion for function.

Hagen Hofmann1.   

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Year:  2016        PMID： 27434765     DOI： 10.1038/nchembio.2130

Source DB:  PubMed          Journal:  Nat Chem Biol        ISSN： 1552-4450            Impact factor:   15.040


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  7 in total

Review 1.  HSP90 at the hub of protein homeostasis: emerging mechanistic insights.

Authors:  Mikko Taipale; Daniel F Jarosz; Susan Lindquist
Journal:  Nat Rev Mol Cell Biol       Date:  2010-06-09       Impact factor: 94.444

Review 2.  HSP90 and the chaperoning of cancer.

Authors:  Luke Whitesell; Susan L Lindquist
Journal:  Nat Rev Cancer       Date:  2005-10       Impact factor: 60.716

3.  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

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

Authors:  Martin Hessling; Klaus Richter; Johannes Buchner
Journal:  Nat Struct Mol Biol       Date:  2009-02-22       Impact factor: 15.369

5.  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

Review 6.  Hsp90 molecular chaperone inhibitors: are we there yet?

Authors:  Len Neckers; Paul Workman
Journal:  Clin Cancer Res       Date:  2012-01-01       Impact factor: 12.531

7.  Cooperation of local motions in the Hsp90 molecular chaperone ATPase mechanism.

Authors:  Andrea Schulze; Gerti Beliu; Dominic A Helmerich; Jonathan Schubert; Laurence H Pearl; Chrisostomos Prodromou; Hannes Neuweiler
Journal:  Nat Chem Biol       Date:  2016-06-20       Impact factor: 15.040
  7 in total

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