Ulrich Hartl
TitleCited byYear
Molecular chaperones in cellular protein folding
FU Hartl
Nature 381 (6583), 571, 1996
42061996
Molecular chaperones in the cytosol: from nascent chain to folded protein
FU Hartl, M Hayer-Hartl
Science 295 (5561), 1852-1858, 2002
36582002
Molecular chaperones in protein folding and proteostasis
FU Hartl, A Bracher, M Hayer-Hartl
Nature 475 (7356), 324, 2011
21122011
Molecular chaperone functions of heat-shock proteins
JP Hendrick, FU Hartl
Annual review of biochemistry 62 (1), 349-384, 1993
18961993
Crystal structure of an Hsp90–geldanamycin complex: targeting of a protein chaperone by an antitumor agent
CE Stebbins, AA Russo, C Schneider, N Rosen, FU Hartl, NP Pavletich
Cell 89 (2), 239-250, 1997
14321997
Pathways of chaperone-mediated protein folding in the cytosol
JC Young, VR Agashe, K Siegers, FU Hartl
Nature reviews Molecular cell biology 5 (10), 781, 2004
11932004
Structure of TPR domain–peptide complexes: critical elements in the assembly of the Hsp70–Hsp90 multichaperone machine
C Scheufler, A Brinker, G Bourenkov, S Pegoraro, L Moroder, H Bartunik, ...
Cell 101 (2), 199-210, 2000
11752000
Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
T Langer, C Lu, H Echols, J Flanagan, MK Hayer, FU Hartl
Nature 356 (6371), 683, 1992
10361992
Converging concepts of protein folding in vitro and in vivo
FU Hartl, M Hayer-Hartl
Nature structural & molecular biology 16 (6), 574, 2009
10072009
Hsp90: a specialized but essential protein-folding tool
JC Young, I Moarefi, FU Hartl
The Journal of cell biology 154 (2), 267, 2001
9062001
Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria
MY Cheng, FU Hartl, J Martin, RA Pollock, F Kalousek, W Neuper, ...
Nature 337 (6208), 620, 1989
9061989
Chaperonin-mediated protein folding at the surface of groEL through a'molten globule'-like intermediate
J Martin, T Langer, R Boteva, A Schramel, AL Horwich, FU Hartl
Nature 352 (6330), 36, 1991
8701991
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
8652013
Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
JC Young, NJ Hoogenraad, FU Hartl
Cell 112 (1), 41-50, 2003
7322003
Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
J Frydman, E Nimmesgern, K Ohtsuka, FU Hartl
Nature 370 (6485), 111, 1994
7211994
Mitochondrial protein import
FU Hartl, N Pfanner, DW Nicholson, W Neupert
Biochimica et Biophysica Acta (BBA)-Reviews on Biomembranes 988 (1), 1-45, 1989
7151989
Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
J Ostermann, AL Horwich, W Neupert, FU Hartl
Nature 341 (6238), 125, 1989
6511989
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
6482000
DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat‐induced protein damage.
H Schröder, T Langer, FU Hartl, B Bukau
The EMBO journal 12 (11), 4137-4144, 1993
6081993
In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis
WMJ Obermann, H Sondermann, AA Russo, NP Pavletich, FU Hartl
The Journal of cell biology 143 (4), 901-910, 1998
5991998
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