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55 in total

1. What is a co-chaperone?

Authors: Avrom J Caplan
Journal: Cell Stress Chaperones Date: 2003 Impact factor: 3.667

2. CRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90.

Authors: Stefan Rudiger; Stefan M V Freund; Dmitry B Veprintsev; Alan R Fersht
Journal: Proc Natl Acad Sci U S A Date: 2002-08-05 Impact factor: 11.205

Review 3. Getting a grip on non-native proteins.

Authors: Peter C Stirling; Victor F Lundin; Michel R Leroux
Journal: EMBO Rep Date: 2003-06 Impact factor: 8.807

4. Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery.

Authors: Philippe Meyer; Chrisostomos Prodromou; Chunyan Liao; Bin Hu; S Mark Roe; Cara K Vaughan; Ignacija Vlasic; Barry Panaretou; Peter W Piper; Laurence H Pearl
Journal: EMBO J Date: 2004-01-22 Impact factor: 11.598

5. 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

6. High-throughput assay for the identification of Hsp90 inhibitors based on Hsp90-dependent refolding of firefly luciferase.

Authors: Lakshmi Galam; M Kyle Hadden; Zeqiang Ma; Qi-Zhuang Ye; Bo-Geon Yun; Brian S J Blagg; Robert L Matts
Journal: Bioorg Med Chem Date: 2007-01-04 Impact factor: 3.641

10. Alteration of the protein kinase binding domain enhances function of the Saccharomyces cerevisiae molecular chaperone Cdc37.

Authors: Min Ren; Arti Santhanam; Paul Lee; Avrom Caplan; Stephen Garrett
Journal: Eukaryot Cell Date: 2007-06-15

Structure, function, and mechanism of the Hsp90 molecular chaperone.