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| Small heat shock proteins are molecular chaperones. U Jakob, M Gaestel, K Engel, J Buchner Journal of Biological Chemistry 268 (3), 1517-1520, 1993 | 1709 | 1993 |
| The HSP90 chaperone machinery FH Schopf, MM Biebl, J Buchner Nature reviews Molecular cell biology 18 (6), 345-360, 2017 | 1372 | 2017 |
| Some like it hot: the structure and function of small heat-shock proteins M Haslbeck, T Franzmann, D Weinfurtner, J Buchner Nature structural & molecular biology 12 (10), 842-846, 2005 | 1046 | 2005 |
| Binding of non‐native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation M Ehrnsperger, S Gräber, M Gaestel, J Buchner The EMBO journal, 1997 | 997 | 1997 |
| Hsp90 & Co.–a holding for folding J Buchner Trends in biochemical sciences 24 (4), 136-141, 1999 | 974 | 1999 |
| Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor α by phosphorylation T Rogalla, M Ehrnsperger, X Preville, A Kotlyarov, G Lutsch, C Ducasse, ... Journal of Biological Chemistry 274 (27), 18947-18956, 1999 | 919 | 1999 |
| Hsp70 and Hsp90—a relay team for protein folding H Wegele, L Müller, J Buchner Reviews of physiology, biochemistry and pharmacology, 1-44, 2004 | 854 | 2004 |
| Hsp90: chaperoning signal transduction K Richter, J Buchner Journal of cellular physiology 188 (3), 281-290, 2001 | 768 | 2001 |
| The Hsp90 chaperone machinery SK Wandinger, K Richter, J Buchner Journal of Biological Chemistry 283 (27), 18473-18477, 2008 | 711 | 2008 |
| Hsp90 chaperones protein folding in vitro H Wiech, J Buchner, R Zimmermann, U Jakob Nature 358 (6382), 169-170, 1992 | 685 | 1992 |
| Protein Aggregation in vitro and in vivo: A Quantitative Model of the Kinetic Competition between Folding and Aggregation T Kiefhaber, R Rudolph, HH Kohler, J Buchner Bio/technology 9 (9), 825-829, 1991 | 668 | 1991 |
| Molecular chaperones—cellular machines for protein folding S Walter, J Buchner Angewandte Chemie International Edition 41 (7), 1098-1113, 2002 | 628 | 2002 |
| The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones J Li, J Soroka, J Buchner Biochimica et Biophysica Acta (BBA)-Molecular Cell Research 1823 (3), 624-635, 2012 | 615 | 2012 |
| GroE facilitates refolding of citrate synthase by suppressing aggregation J Buchner, M Schmidt, M Fuchs, R Jaenicke, R Rudolph, FX Schmid, ... Biochemistry 30 (6), 1586-1591, 1991 | 613 | 1991 |
| Renaturation, Purification and Characterization of Recombinant Fab-Fragments Produced in Escherichia coli J Buchner, R Rudolph Bio/technology 9 (2), 157-162, 1991 | 613 | 1991 |
| Supervising the fold: functional principles of molecular chaperones J Buchner The FASEB journal 10 (1), 10-19, 1996 | 604 | 1996 |
| A method for increasing the yield of properly folded recombinant fusion proteins: single-chain immunotoxins from renaturation of bacterial inclusion bodies J Buchner, I Pastan, U Brinkmann Analytical biochemistry 205 (2), 263-270, 1992 | 599 | 1992 |
| Hsp26: a temperature-regulated chaperone M Haslbeck, S Walke, T Stromer, M Ehrnsperger, HE White, S Chen, ... The EMBO journal 18 (23), 6744-6751, 1999 | 590 | 1999 |
| Reduction of disulphide bonds unmasks potent antimicrobial activity of human β-defensin 1 BO Schroeder, Z Wu, S Nuding, S Groscurth, M Marcinowski, J Beisner, ... Nature 469 (7330), 419-423, 2011 | 554 | 2011 |
