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The Journal of Cell Biology|July 27, 2001
Hsp90: a specialized but essential protein-folding toolJ C Young, I Moarefi, F U HartlCell|December 7, 2000
Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteinsR Siegert, M R Leroux, C Scheufler, et al.Science (New York, N.Y.)|February 27, 2001
Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factorsH Sondermann, C Scheufler, C Schneider, et al.The EMBO Journal|November 4, 2000
Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23J C Young, F U HartlFEBS Letters|December 31, 1997
In vitro evidence that hsp90 contains two independent chaperone sitesJ C Young, C Schneider, F U HartlCell|April 29, 2000
Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machineC Scheufler, A Brinker, G Bourenkov, et al.The Journal of Biological Chemistry|July 11, 1998
Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90J C Young, W M Obermann, F U HartlPhilosophical Transactions of the Royal Society of London. Series B, Biological Sciences|April 29, 1995
Principles of chaperone-mediated protein foldingF U HartlSeminars in Immunology|January 1, 1991
Heat shock proteins in protein folding and membrane translocationF U HartlPageof 26