Ulrich Hartl

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M. Hayer-Hartl; M.K. Hayer; M.K. Haye...Max Planck Institute of BiochemistryEmail verificata su biochem.mpg.de
Andreas BracherGroup Leader, Max Planck Institute of Biochemistry, Martinsried, GermanyEmail verificata su biochem.mpg.de
Mark S. HippUniversity Medical Center Groningen, Rijksuniversiteit Groningen, University of OldenburgEmail verificata su umcg.nl
Jason YoungMcGill UniversityEmail verificata su mcgill.ca
Matthias MannMax Planck Institute of Biochemistry, Munich and CPR, University of CopenhagenEmail verificata su biochem.mpg.de
Thomas LangerMax Planck Institute for Biology of Ageing, Cologne, GermanyEmail verificata su age.mpg.de
Ismail MoarefiCrelux GmbHEmail verificata su moarefi.de
C GeorgopoulosResearch professor of biochemistryEmail verificata su biochem.utah.edu
Christopher DobsonUniversity of CambridgeEmail verificata su cam.ac.uk
David BalchinGroup Leader, The Francis Crick instituteEmail verificata su crick.ac.uk
James RothmanYale UniversityEmail verificata su yale.edu
Roman KörnerGroup Leader Mass Spectrometry, Max Planck Institute of BiochemistryEmail verificata su biochem.mpg.de
Konstanze WinklhoferRuhr University BochumEmail verificata su ruhr-uni-bochum.de
Michele VendruscoloProfessor of Biophysics, University of CambridgeEmail verificata su cam.ac.uk
Prasad KasturiIndian Institute of Technology MandiEmail verificata su iitmandi.ac.in
Frédéric FrottinEmail verificata su biochem.mpg.de
Irina DudanovaProfessor of Anatomy, University Hospital CologneEmail verificata su uk-koeln.de
Michel LerouxSimon Fraser UniversityEmail verificata su sfu.ca
Stefan PinkertDISPOEmail verificata su hhu.de
Sae-Hun ParkMPI of BiochemistryEmail verificata su biochem.mpg.de

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Ulrich Hartl

Director, Max Planck Institute of Biochemistry

Email verificata su biochem.mpg.de

Protein folding molecular chaperones protein aggregation neurodegenerative disease


Titolo Ordina per citazioni Ordina per anno Ordina per titolo	Citata da Citata da	Anno
Molecular chaperones in cellular protein folding FU Hartl Nature 381 (6583), 571-580, 1996	5117	1996
Molecular chaperones in the cytosol: from nascent chain to folded protein FU Hartl, M Hayer-Hartl Science 295 (5561), 1852-1858, 2002	4555	2002
Molecular chaperones in protein folding and proteostasis FU Hartl, A Bracher, M Hayer-Hartl Nature 475 (7356), 324-332, 2011	3993	2011
Molecular chaperone functions of heat-shock proteins JP Hendrick, FU Hartl Annual review of biochemistry 62 (1), 349-384, 1993	2246	1993
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 (1), 323-355, 2013	1802	2013
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	1754	1997
Converging concepts of protein folding in vitro and in vivo FU Hartl, M Hayer-Hartl Nature structural & molecular biology 16 (6), 574-581, 2009	1536	2009
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	1531	2000
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	1451	2004
In vivo aspects of protein folding and quality control D Balchin, M Hayer-Hartl, FU Hartl Science 353 (6294), aac4354, 2016	1439	2016
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	1266	1992
The proteostasis network and its decline in ageing MS Hipp, P Kasturi, FU Hartl Nature reviews Molecular cell biology 20 (7), 421-435, 2019	1231	2019
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	1157	1989
Hsp90: a specialized but essential protein-folding tool JC Young, I Moarefi, FU Hartl The Journal of cell biology 154 (2), 267, 2001	1134	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	1043	2003
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	1036	1991
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	884	1994
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	859	1989
Mitochondrial protein import FU Hartl, N Pfanner, DW Nicholson, W Neupert Biochimica et Biophysica Acta (BBA)-Reviews on Biomembranes 988 (1), 1-45, 1989	859	1989
Pathways of cellular proteostasis in aging and disease CL Klaips, GG Jayaraj, FU Hartl Journal of Cell Biology 217 (1), 51-63, 2018	828	2018

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