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Nature|July 9, 1992
Hsp90 chaperones protein folding in vitroH Wiech, J Buchner, R Zimmermann, et al.
The Journal of Biological Chemistry|April 5, 1993
Hsc70, immunoglobulin heavy chain binding protein, and Hsp90 differ in their ability to stimulate transport of precursor proteins into mammalian microsomesH Wiech, J Buchner, M Zimmermann, et al.
Trends in Biochemical Sciences|May 1, 1994
Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperonesU Jakob, J Buchner
Seminars in Cell Biology|February 1, 1990
Role of cytosolic factors in the transport of proteins across membranesH Wiech, R Stuart, R Zimmermann
The Journal of Biological Chemistry|March 31, 1995
Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivoU Jakob, H Lilie, I Meyer, et al.
Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences|March 29, 1993
The role of molecular chaperones in protein transport into the endoplasmic reticulumT Dierks, P Klappa, H Wiech, et al.
The EMBO Journal|April 1, 1987
The ATP requiring step in assembly of M13 procoat protein into microsomes is related to preservation of transport competence of the precursor proteinH Wiech, M Sagstetter, G Müller, 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|April 26, 1996
Assessment of the ATP binding properties of Hsp90U Jakob, T Scheibel, S Bose, et al.
The EMBO Journal|January 1, 1994
Stress- and mitogen-induced phosphorylation of the small heat shock protein Hsp25 by MAPKAP kinase 2 is not essential for chaperone properties and cellular thermoresistanceU Knauf, U Jakob, K Engel, et al.
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