Ulrich Hartl

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M. Hayer-Hartl; M.K. Hayer; M.K. Haye...Max Planck Institute of BiochemistryPatvirtintas el. paštas biochem.mpg.de
Andreas BracherGroup Leader, Max Planck Institute of Biochemistry, Martinsried, GermanyPatvirtintas el. paštas biochem.mpg.de
Mark S. HippUniversity Medical Center Groningen, Rijksuniversiteit Groningen, University of OldenburgPatvirtintas el. paštas umcg.nl
Jason YoungMcGill UniversityPatvirtintas el. paštas mcgill.ca
Matthias MannMax Planck Institute of Biochemistry, Munich and CPR, University of CopenhagenPatvirtintas el. paštas biochem.mpg.de
Thomas LangerMax Planck Institute for Biology of Ageing, Cologne, GermanyPatvirtintas el. paštas age.mpg.de
Ismail MoarefiCrelux GmbHPatvirtintas el. paštas moarefi.de
Christopher DobsonUniversity of CambridgePatvirtintas el. paštas cam.ac.uk
C GeorgopoulosResearch professor of biochemistryPatvirtintas el. paštas biochem.utah.edu
David BalchinGroup Leader, The Francis Crick institutePatvirtintas el. paštas crick.ac.uk
Roman KörnerGroup Leader Mass Spectrometry, Max Planck Institute of BiochemistryPatvirtintas el. paštas biochem.mpg.de
James RothmanYale UniversityPatvirtintas el. paštas yale.edu
Konstanze WinklhoferRuhr University BochumPatvirtintas el. paštas ruhr-uni-bochum.de
Irina DudanovaProfessor of Anatomy, University Hospital ColognePatvirtintas el. paštas uk-koeln.de
Prasad KasturiIndian Institute of Technology MandiPatvirtintas el. paštas iitmandi.ac.in
Michele VendruscoloProfessor of Biophysics, University of CambridgePatvirtintas el. paštas cam.ac.uk
Frédéric FrottinPatvirtintas el. paštas biochem.mpg.de
Stefan PinkertDISPOPatvirtintas el. paštas hhu.de
Michel LerouxSimon Fraser UniversityPatvirtintas el. paštas sfu.ca
Sae-Hun ParkMPI of BiochemistryPatvirtintas el. paštas biochem.mpg.de

Stebėti

Ulrich Hartl

Director, Max Planck Institute of Biochemistry

Patvirtintas el. paštas biochem.mpg.de

Protein folding molecular chaperones protein aggregation neurodegenerative disease


Pavadinimas Rūšiuoti pagal šaltinius Rūšiuoti pagal metus Rūšiuoti pagal pavadinimą	Cituota Cituota	Metai
Molecular chaperones in cellular protein folding FU Hartl Nature 381 (6583), 571-580, 1996	5122	1996
Molecular chaperones in the cytosol: from nascent chain to folded protein FU Hartl, M Hayer-Hartl Science 295 (5561), 1852-1858, 2002	4562	2002
Molecular chaperones in protein folding and proteostasis FU Hartl, A Bracher, M Hayer-Hartl Nature 475 (7356), 324-332, 2011	4075	2011
Molecular chaperone functions of heat-shock proteins JP Hendrick, FU Hartl Annual review of biochemistry 62 (1), 349-384, 1993	2259	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	1845	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	1763	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	1548	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	1538	2000
In vivo aspects of protein folding and quality control D Balchin, M Hayer-Hartl, FU Hartl Science 353 (6294), aac4354, 2016	1471	2016
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	1460	2004
The proteostasis network and its decline in ageing MS Hipp, P Kasturi, FU Hartl Nature reviews Molecular cell biology 20 (7), 421-435, 2019	1304	2019
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	1260	1992
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	1167	1989
Hsp90: a specialized but essential protein-folding tool JC Young, I Moarefi, FU Hartl The Journal of cell biology 154 (2), 267, 2001	1135	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	1058	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	1037	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	892	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	869	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	862	1989
Pathways of cellular proteostasis in aging and disease CL Klaips, GG Jayaraj, FU Hartl Journal of Cell Biology 217 (1), 51-63, 2018	850	2018

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