Ulrich Hartl

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M. Hayer-Hartl; M.K. Hayer; M.K. Haye...Max Planck Institute of BiochemistryVerified email at biochem.mpg.de
Andreas BracherGroup Leader, Max Planck Institute of Biochemistry, Martinsried, GermanyVerified email at biochem.mpg.de
Mark S. HippUniversity Medical Center Groningen, Rijksuniversiteit Groningen, University of OldenburgVerified email at umcg.nl
Jason YoungMcGill UniversityVerified email at mcgill.ca
Thomas LangerMax Planck Institute for Biology of Ageing, Cologne, GermanyVerified email at age.mpg.de
Matthias MannMax Planck Institute of Biochemistry, Munich and CPR, University of CopenhagenVerified email at biochem.mpg.de
Judith FrydmanStanford UniversityVerified email at stanford.edu
Ismail MoarefiCrelux GmbHVerified email at moarefi.de
C GeorgopoulosResearch professor of biochemistryVerified email at biochem.utah.edu
Christopher DobsonUniversity of CambridgeVerified email at cam.ac.uk
James RothmanYale UniversityVerified email at yale.edu
R. Martin VabulasCharité - University Medicine BerlinVerified email at charite.de
David BalchinGroup Leader, The Francis Crick instituteVerified email at crick.ac.uk
Roman KörnerGroup Leader Mass Spectrometry, Max Planck Institute of BiochemistryVerified email at biochem.mpg.de
Michele VendruscoloProfessor of Biophysics, University of CambridgeVerified email at cam.ac.uk
Frédéric FrottinVerified email at biochem.mpg.de
Stefan PinkertDISPOVerified email at hhu.de
Michel LerouxSimon Fraser UniversityVerified email at sfu.ca
Clemens ScheuflerNovartis Pharma AG, BaselVerified email at novartis.com
Konstanze WinklhoferVerified email at ruhr-uni-bochum.de

Ulrich Hartl

Director, Max Planck Institute of Biochemistry

Verified email at biochem.mpg.de

Protein folding molecular chaperones protein aggregation neurodegenerative disease


Title Sort by citations Sort by year Sort by title	Cited by Cited by	Year
Molecular chaperones in cellular protein folding FU Hartl Nature 381 (6583), 571-580, 1996	4930	1996
Molecular chaperones in the cytosol: from nascent chain to folded protein FU Hartl, M Hayer-Hartl Science 295 (5561), 1852-1858, 2002	4334	2002
Molecular chaperones in protein folding and proteostasis FU Hartl, A Bracher, M Hayer-Hartl Nature 475 (7356), 324-332, 2011	3384	2011
Molecular chaperone functions of heat-shock proteins JP Hendrick, FU Hartl Annual review of biochemistry 62 (1), 349-384, 1993	2204	1993
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	1688	1997
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	1530	2013
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	1454	2000
Converging concepts of protein folding in vitro and in vivo FU Hartl, M Hayer-Hartl Nature structural & molecular biology 16 (6), 574-581, 2009	1395	2009
Pathways of chaperone-mediated protein folding in the cytosol JC Young, VR Agashe, K Siegers, FU Hartl Nature reviews Molecular cell biology 5 (10), 781-791, 2004	1378	2004
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), 683-689, 1992	1247	1992
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), 36-42, 1991	1185	1991
In vivo aspects of protein folding and quality control D Balchin, M Hayer-Hartl, FU Hartl Science 353 (6294), aac4354, 2016	1136	2016
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), 620-625, 1989	1121	1989
Hsp90: a specialized but essential protein-folding tool JC Young, I Moarefi, FU Hartl The Journal of cell biology 154 (2), 267, 2001	1112	2001
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	942	2003
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), 111-117, 1994	860	1994
Mitochondrial protein import FU Hartl, N Pfanner, DW Nicholson, W Neupert Biochimica et Biophysica Acta (BBA)-Reviews on Biomembranes 988 (1), 1-45, 1989	850	1989
Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis J Ostermann, AL Horwich, W Neupert, FU Hartl Nature 341 (6238), 125-130, 1989	828	1989
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	778	2000
The proteostasis network and its decline in ageing MS Hipp, P Kasturi, FU Hartl Nature reviews Molecular cell biology 20 (7), 421-435, 2019	768	2019

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