| Molecular chaperones in the cytosol: from nascent chain to folded protein FU Hartl, M Hayer-Hartl Science 295 (5561), 1852-1858, 2002 | 4472 | 2002 |
| Molecular chaperones in protein folding and proteostasis FU Hartl, A Bracher, M Hayer-Hartl Nature 475 (7356), 324-332, 2011 | 3725 | 2011 |
| Molecular chaperone functions in protein folding and proteostasis YE Kim, MS Hipp, A Bracher, M Hayer-Hartl, F Ulrich Hartl Annual review of biochemistry 82, 323-355, 2013 | 1666 | 2013 |
| Converging concepts of protein folding in vitro and in vivo FU Hartl, M Hayer-Hartl Nature structural & molecular biology 16 (6), 574-581, 2009 | 1482 | 2009 |
| In vivo aspects of protein folding and quality control D Balchin, M Hayer-Hartl, FU Hartl Science 353 (6294), aac4354, 2016 | 1335 | 2016 |
| Successive action of DnaK (Hsp70), DnaJ and GroEL (Hsp60) along the pathway of Chaperone-assisted protein folding T Langer, C Lu, H Echols, J Flanagen, MK Hayer, FU Hartl Nature 356, 683-689, 1992 | 1268* | 1992 |
| Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils PJ Muchowski, G Schaffar, A Sittler, EE Wanker, MK Hayer-Hartl, FU Hartl Proceedings of the National Academy of Sciences 97 (14), 7841-7846, 2000 | 806 | 2000 |
| Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions H Olzscha, SM Schermann, AC Woerner, S Pinkert, MH Hecht, ... Cell 144 (1), 67-78, 2011 | 762 | 2011 |
| Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli MJ Kerner, DJ Naylor, Y Ishihama, T Maier, HC Chang, AP Stines, ... Cell 122 (2), 209-220, 2005 | 761 | 2005 |
| Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK CJ Harrison, M Hayer-Hartl, MD Liberto, FU Hartl, J Kuriyan Science 276 (5311), 431-435, 1997 | 613 | 1997 |
| Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington’s disease A Sittler, R Lurz, G Lueder, J Priller, MK Hayer-Hartl, FU Hartl, H Lehrach, ... Human molecular genetics 10 (12), 1307-1315, 2001 | 545 | 2001 |
| Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation G Schaffar, P Breuer, R Boteva, C Behrends, N Tzvetkov, N Strippel, ... Molecular cell 15 (1), 95-105, 2004 | 525 | 2004 |
| Protein folding in the cytoplasm and the heat shock response RM Vabulas, S Raychaudhuri, M Hayer-Hartl, FU Hartl Cold Spring Harbor perspectives in biology 2 (12), a004390, 2010 | 511 | 2010 |
| DnaK functions as a central hub in the E. coli chaperone network G Calloni, T Chen, SM Schermann, H Chang, P Genevaux, F Agostini, ... Cell reports 1 (3), 251-264, 2012 | 416 | 2012 |
| PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone SH Park, Y Kukushkin, R Gupta, T Chen, A Konagai, MS Hipp, ... Cell 154 (1), 134-145, 2013 | 396 | 2013 |
| The GroEL–GroES chaperonin machine: a nano-cage for protein folding M Hayer-Hartl, A Bracher, FU Hartl Trends in biochemical sciences 41 (1), 62-76, 2016 | 383 | 2016 |
| Dual function of protein confinement in chaperonin-assisted protein folding A Brinker, G Pfeifer, MJ Kerner, DJ Naylor, FU Hartl, M Hayer-Hartl Cell 107 (2), 223-233, 2001 | 364 | 2001 |
| Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein YC Tang, HC Chang, A Roeben, D Wischnewski, N Wischnewski, ... Cell 125 (5), 903-914, 2006 | 346 | 2006 |
| Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity H Sakahira, P Breuer, MK Hayer-Hartl, FU Hartl Proceedings of the National Academy of Sciences 99 (suppl_4), 16412-16418, 2002 | 309 | 2002 |
| Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed VR Agashe, S Guha, HC Chang, P Genevaux, M Hayer-Hartl, M Stemp, ... Cell 117 (2), 199-209, 2004 | 288 | 2004 |
Ulrich HartlDirector, Max Planck Institute of BiochemistryVerified email at biochem.mpg.de
