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Journal of Cellular Physiology|July 27, 2001
Hsp90: chaperoning signal transductionK Richter, J BuchnerThe Journal of Biological Chemistry|July 7, 2001
Coordinated ATP hydrolysis by the Hsp90 dimerK Richter, P Muschler, O Hainzl, et al.The Journal of Biological Chemistry|August 16, 2000
Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional propertiesC Mayr, K Richter, H Lilie, et al.Journal of Molecular Biology|June 12, 2001
The alternatively folded state of the antibody C(H)3 domainM J Thies, R Kammermeier, K Richter, 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.FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology|January 1, 1996
Supervising the fold: functional principles of molecular chaperonesJ BuchnerJournal of Structural Biology|October 3, 2001
Review: a structural view of the GroE chaperone cycleH Grallert, J BuchnerThe Journal of Biological Chemistry|July 10, 1999
Analysis of GroE-assisted folding under nonpermissive conditionsH Grallert, J BuchnerHandbook of Experimental Pharmacology|April 14, 2006
Protein aggregation as a cause for diseaseT Scheibel, J BuchnerPageof 54