M. Hayer-Hartl; M.K. Hayer; M.K. Hayer-Hartl; Mayer-Hartl, M
M. Hayer-Hartl; M.K. Hayer; M.K. Hayer-Hartl; Mayer-Hartl, M
Verified email at biochem.mpg.de - Homepage
Cited by
Cited by
Molecular chaperones in the cytosol: from nascent chain to folded protein
FU Hartl, M Hayer-Hartl
Science 295 (5561), 1852-1858, 2002
Molecular chaperones in protein folding and proteostasis
FU Hartl, A Bracher, M Hayer-Hartl
Nature 475 (7356), 324-332, 2011
Converging concepts of protein folding in vitro and in vivo
FU Hartl, M Hayer-Hartl
Nature structural & molecular biology 16 (6), 574, 2009
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
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
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
In vivo aspects of protein folding and quality control
D Balchin, M Hayer-Hartl, FU Hartl
Science 353 (6294), 2016
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
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
Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
CJ Harrison, M Hayer-Hartl, M Di Liberto, FU Hartl, J Kuriyan
Science 276 (5311), 431-435, 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
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
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
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
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
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
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
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
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
Real-time observation of trigger factor function on translating ribosomes
CM Kaiser, HC Chang, VR Agashe, SK Lakshmipathy, SA Etchells, ...
Nature 444 (7118), 455-460, 2006
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