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Cold Spring Harbor Perspectives in Biology|February 13, 2019
Structure, Function, and Regulation of the Hsp90 MachineryMaximilian M Biebl, Johannes BuchnerSub-Cellular Biochemistry|December 15, 2022
p23 and Aha1: Distinct Functions Promote Client MaturationMaximilian M Biebl, Johannes BuchnerCell Reports|August 27, 2020
Hsp90 Co-chaperones Form Plastic Genetic Networks Adapted to Client MaturationMaximilian M Biebl, Maximilian Riedl, Johannes BuchnerNature Reviews. Molecular Cell Biology|April 22, 2017
The HSP90 chaperone machineryFlorian H Schopf, Maximilian M Biebl, Johannes BuchnerNature Communications|February 6, 2021
Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycleMaximilian M Biebl, Abraham Lopez, Alexandra Rehn, et al.The Journal of Biological Chemistry|January 11, 2019
Molecular chaperones and protein quality control: an introduction to the JBC Reviews thematic seriesJohannes BuchnerMolecular Cell|March 17, 2019
The Co-chaperone Cns1 and the Recruiter Protein Hgh1 Link Hsp90 to Translation Elongation via Chaperoning Elongation Factor 2Florian H Schopf, Eva M Huber, Christopher Dodt, et al.Methods in Molecular Medicine|February 13, 2004
Refolding of inclusion body proteinsMarcus Mayer, Johannes BuchnerMethods in Molecular Biology (Clifton, N.J.)|March 26, 2015
Assays to characterize molecular chaperone function in vitroMartin Haslbeck, Johannes BuchnerPageof 22