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Proceedings of the National Academy of Sciences of the United States of America|March 21, 1998
Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependenceT Scheibel, T Weikl, J BuchnerMolecular Microbiology|November 24, 1999
Contribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiaeT Scheibel, T Weikl, R Rimerman, et al.The Journal of Biological Chemistry|July 25, 1997
ATP-binding properties of human Hsp90T Scheibel, S Neuhofen, T Weikl, et al.Biochemical Pharmacology|September 29, 1998
The Hsp90 complex--a super-chaperone machine as a novel drug targetT Scheibel, J BuchnerHandbook of Experimental Pharmacology|April 14, 2006
Protein aggregation as a cause for diseaseT Scheibel, J BuchnerJournal of Molecular Biology|November 2, 1999
An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone functionT Weikl, K Abelmann, J BuchnerScience (New York, N.Y.)|December 6, 1996
Chaperone function of Hsp90-associated proteinsS Bose, T Weikl, H Bügl, et al.Journal of Molecular Biology|October 31, 2000
C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycleT Weikl, P Muschler, K Richter, et al.The Journal of Biological Chemistry|April 26, 1996
Assessment of the ATP binding properties of Hsp90U Jakob, T Scheibel, S Bose, et al.Journal of Molecular Biology|October 1, 1998
Folding and association of beta-GalactosidaseA Nichtl, J Buchner, R Jaenicke, et al.Pageof 10