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The Journal of Biological Chemistry|July 7, 2001
Coordinated ATP hydrolysis by the Hsp90 dimerK Richter, P Muschler, O Hainzl, et al.Science (New York, N.Y.)|December 6, 1996
Chaperone function of Hsp90-associated proteinsS Bose, T Weikl, H Bügl, et al.The Journal of Biological Chemistry|June 6, 1998
The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone networkL Veinger, S Diamant, J Buchner, et al.The EMBO Journal|January 15, 1997
Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivationM Ehrnsperger, S Gräber, M Gaestel, et al.The Journal of Biological Chemistry|January 25, 1993
Small heat shock proteins are molecular chaperonesU Jakob, M Gaestel, K Engel, et al.The Journal of Biological Chemistry|October 15, 1992
GroE dependence of refolding and holoenzyme formation of 6-hydroxy-D-nicotine oxidaseR Brandsch, V Bichler, M Schmidt, et al.The Journal of Biological Chemistry|November 11, 1994
Correlation between the stability of the GroEL-protein ligand complex and the release mechanismM Schmidt, U Bücheler, B Kaluza, et al.FEBS Letters|July 6, 1992
Glycosylation inhibits the interaction of invertase with the chaperone GroELG Kern, M Schmidt, J Buchner, et al.The Journal of Biological Chemistry|July 27, 2001
Localization of the chaperone domain of FKBP52F Pirkl, E Fischer, S Modrow, et al.Nature|July 9, 1992
Hsp90 chaperones protein folding in vitroH Wiech, J Buchner, R Zimmermann, et al.Pageof 12