Ulrich Hartl - Citas de Google Académico

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M. Hayer-Hartl; M.K. Hayer, M.K. Haye...Max Planck Institute of BiochemistryDirección de correo verificada de biochem.mpg.de
Jason YoungMcGill UniversityDirección de correo verificada de mcgill.ca
Mark S. HippGroupleader, Max Planck Institute of Biochemistry Dirección de correo verificada de biochem.mpg.de
Judith FrydmanStanford UniversityDirección de correo verificada de stanford.edu
Matthias MannMax Planck Institute of Biochemistry, Munich and CPR, University of CopenhagenDirección de correo verificada de biochem.mpg.de
Ismail MoarefiCrelux GmbHDirección de correo verificada de moarefi.de
Christopher DobsonUniversity of CambridgeDirección de correo verificada de cam.ac.uk
R. Martin VabulasGoethe University FrankfurtDirección de correo verificada de em.uni-frankfurt.de
James RothmanYale UniversityDirección de correo verificada de yale.edu
Clemens ScheuflerNovartis Pharma AG, BaselDirección de correo verificada de novartis.com
Michel LerouxSimon Fraser UniversityDirección de correo verificada de sfu.ca
Stefan PinkertDISPODirección de correo verificada de hhu.de
Holger SondermannCornell UniversityDirección de correo verificada de cornell.edu
Carol V RobinsonProfessor of Chemistry University of OxfordDirección de correo verificada de chem.ox.ac.uk
Walid HouryProfessor of Biochemistry, University of TorontoDirección de correo verificada de utoronto.ca
Michele VendruscoloProfessor of Biophysics, University of CambridgeDirección de correo verificada de cam.ac.uk
Dmitrij FrishmanProfessor of Bioinformatics, Technische Universität MünchenDirección de correo verificada de wzw.tum.de
Pierre GENEVAUXCNRS Research DirectorDirección de correo verificada de ibcg.biotoul.fr
Oliver Mueller-CajarAssociate Professor, Nanyang Technological UniversityDirección de correo verificada de ntu.edu.sg
Peter WalterHHMI/UCSFDirección de correo verificada de walterlab.ucsf.edu

Ulrich Hartl

Director, Max Planck Institute of Biochemsitry

Dirección de correo verificada de biochem.mpg.de

Protein folding molecular chaperones protein aggregation neurodegenerative disease


Título	Citado por	Año
Molecular chaperones in cellular protein folding FU Hartl Nature 381 (6583), 571, 1996	4293	1996
Molecular chaperones in the cytosol: from nascent chain to folded protein FU Hartl, M Hayer-Hartl Science 295 (5561), 1852-1858, 2002	3708	2002
Molecular chaperones in protein folding and proteostasis FU Hartl, A Bracher, M Hayer-Hartl Nature 475 (7356), 324, 2011	2188	2011
Molecular chaperone functions of heat-shock proteins JP Hendrick, FU Hartl Annual review of biochemistry 62 (1), 349-384, 1993	1914	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	1449	1997
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	1216	2004
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	1199	2000
Converging concepts of protein folding in vitro and in vivo FU Hartl, M Hayer-Hartl Nature structural & molecular biology 16 (6), 574, 2009	1041	2009
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	1040	1992
Hsp90: a specialized but essential protein-folding tool JC Young, I Moarefi, FU Hartl The Journal of cell biology 154 (2), 267, 2001	924	2001
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	921	2013
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	915	1989
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	871	1991
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	741	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, 1994	724	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	717	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	661	2000
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	656	1989
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	613	1993
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	610	1998

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