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Molecular Microbiology|November 24, 1999
Contribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiaeT Scheibel, T Weikl, R Rimerman, et al.Journal of Molecular Biology|October 31, 2000
C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycleT Weikl, P Muschler, K Richter, et al.Biochemistry|July 29, 2000
The N-terminal fragment of human parathyroid hormone receptor 1 constitutes a hormone binding domain and reveals a distinct disulfide patternU Grauschopf, H Lilie, K Honold, et al.The Journal of Biological Chemistry|June 16, 1995
Structural organization of procaryotic and eucaryotic Hsp90. Influence of divalent cations on structure and functionU Jakob, I Meyer, H Bügl, et al.The Journal of Biological Chemistry|April 8, 1994
On the role of groES in the chaperonin-assisted folding reaction. Three case studiesM Schmidt, J Buchner, M J Todd, et al.Structure (London, England : 1993)|May 30, 2001
Activation of the redox-regulated molecular chaperone Hsp33--a two-step mechanismJ Graumann, H Lilie, X Tang, et al.Sleep & Breathing = Schlaf & Atmung|January 8, 2011
Treatment of obstructive sleep apnea reduces arterial stiffnessNikolaus J Buchner, Ivo Quack, Johannes Stegbauer, et al.The Journal of Biological Chemistry|October 19, 2000
The crystal structure of the fab fragment of the monoclonal antibody MAK33. Implications for folding and interaction with the chaperone bipJ G Augustine, A de La Calle, G Knarr, et al.International Journal of Biological Macromolecules|July 3, 1998
The effect of the intersubunit disulfide bond on the structural and functional properties of the small heat shock protein Hsp25A Zavialov, R Benndorf, M Ehrnsperger, et al.Journal of Molecular Biology|July 2, 1999
Novel molecular architecture of the multimeric archaeal PEP-synthase homologue (MAPS) from Staphylothermus marinusC Cicicopol, J Peters, A Lupas, et al.Pageof 12