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Proceedings of the National Academy of Sciences of the United States of America|February 17, 1999
The charged region of Hsp90 modulates the function of the N-terminal domainT Scheibel, H I Siegmund, R Jaenicke, et al.Nature Structural Biology|October 31, 2001
The role of conformational flexibility in prion propagation and maintenance for Sup35pT Scheibel, S L LindquistFASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology|January 1, 1996
Supervising the fold: functional principles of molecular chaperonesJ BuchnerFASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology|September 1, 1997
S. cerevisiae and sulfur: a unique way to deal with the environmentT Scheibel, S Bell, S WalkeJournal of Cellular Physiology|July 27, 2001
Hsp90: chaperoning signal transductionK Richter, J 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 BuchnerThe Journal of Biological Chemistry|May 30, 1997
How GroES regulates binding of nonnative protein to GroELH Sparrer, J BuchnerFEBS Letters|March 27, 1995
Domain interactions stabilize the alternatively folded state of an antibody Fab fragmentH Lilie, J BuchnerPageof 10