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Journal of Molecular Biology|May 15, 2001
Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40F Pirkl, J BuchnerCurrent Opinion in Biotechnology|August 1, 1991
Routes to active proteins from transformed microorganismsJ Buchner, R RudolphTrends in Biochemical Sciences|May 1, 1994
Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperonesU Jakob, J BuchnerBiochemical Pharmacology|September 29, 1998
The Hsp90 complex--a super-chaperone machine as a novel drug targetT Scheibel, J BuchnerThe Journal of Biological Chemistry|August 25, 1992
Interaction of GroE with an all-beta-proteinM Schmidt, J BuchnerBio/Technology (Nature Publishing Company)|February 1, 1991
Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coliJ Buchner, R RudolphAnalytical Biochemistry|September 1, 1992
A method for increasing the yield of properly folded recombinant fusion proteins: single-chain immunotoxins from renaturation of bacterial inclusion bodiesJ Buchner, I Pastan, U BrinkmannJournal 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 BuchnerProceedings of the National Academy of Sciences of the United States of America|February 18, 1997
Catalysis of protein folding by symmetric chaperone complexesH Sparrer, K Rutkat, J BuchnerPageof 127