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Angewandte Chemie (International Ed. in English)|December 20, 2002
Molecular chaperones--cellular machines for protein foldingStefan Walter, Johannes Buchner
Biological Chemistry|October 7, 2005
Characterization of oligomeric species in the fibrillization pathway of the yeast prion Ure2pSilvia Catharino, Johannes Buchner, Stefan Walter
Journal of Molecular Biology|September 15, 2004
The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycleKlaus Richter, Stefan Walter, Johannes Buchner
Journal of Molecular Biology|October 27, 2004
Folding mechanism of the CH2 antibody domainMatthias J Feige, Stefan Walter, Johannes Buchner
Molecular Cell|February 5, 2008
Activation of the chaperone Hsp26 is controlled by the rearrangement of its thermosensor domainTitus M Franzmann, Petra Menhorn, Stefan Walter, et al.
The Journal of Biological Chemistry|April 22, 2005
Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104Martin Haslbeck, Anita Miess, Thusnelda Stromer, et al.
The Journal of Biological Chemistry|December 12, 2003
The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104Valerie Grimminger, Klaus Richter, Axel Imhof, et al.
Journal of Molecular Biology|June 22, 2005
The activation mechanism of Hsp26 does not require dissociation of the oligomerTitus M Franzmann, Martin Wühr, Klaus Richter, et al.
The Journal of Biological Chemistry|January 11, 2019
Molecular chaperones and protein quality control: an introduction to the JBC Reviews thematic seriesJohannes Buchner
Methods in Molecular Medicine|February 13, 2004
Refolding of inclusion body proteinsMarcus Mayer, Johannes Buchner
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