F. Ulrich Hartl - Publications

Affiliations: 
Department of Cellular Biochemistry Max Planck Institute for Biochemistry 

285 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2023 Müller MBD, Kasturi P, Jayaraj GG, Hartl FU. Mechanisms of readthrough mitigation reveal principles of GCN1-mediated translational quality control. Cell. PMID 37339632 DOI: 10.1016/j.cell.2023.05.035  0.348
2021 Sitron CS, Hartl FU. A new way of D/Ealing with protein misfolding. Molecular Cell. 81: 4114-4115. PMID 34686313 DOI: 10.1016/j.molcel.2021.09.025  0.3
2021 Zhao L, Castanié-Cornet MP, Kumar S, Genevaux P, Hayer-Hartl M, Hartl FU. Bacterial RF3 senses chaperone function in co-translational folding. Molecular Cell. PMID 34107307 DOI: 10.1016/j.molcel.2021.05.016  0.362
2020 Balchin D, Hayer-Hartl M, Hartl FU. Recent advances in understanding catalysis of protein folding by molecular chaperones. Febs Letters. PMID 32446288 DOI: 10.1002/1873-3468.13844  0.397
2020 Herrmann JM, Hartl FU, Pfanner N. Mitochondria and friends. Biological Chemistry. PMID 32383685 DOI: 10.1515/Hsz-2020-0151  0.462
2020 Singh AK, Balchin D, Imamoglu R, Hayer-Hartl M, Hartl FU. Efficient Catalysis of Protein Folding by GroEL/ES of the Obligate Chaperonin Substrate MetF. Journal of Molecular Biology. PMID 32135190 DOI: 10.1016/j.jmb.2020.02.031  0.366
2020 Bie AS, Cömert C, Körner R, Corydon TJ, Palmfeldt J, Hipp MS, Hartl FU, Bross P. An inventory of interactors of the human HSP60/HSP10 chaperonin in the mitochondrial matrix space. Cell Stress & Chaperones. PMID 32060690 DOI: 10.1007/s12192-020-01080-6  0.353
2020 Imamoglu R, Balchin D, Hayer-Hartl M, Hartl FU. Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein. Nature Communications. 11: 365. PMID 31953415 DOI: 10.1038/s41467-019-14245-4  0.385
2020 Jayaraj GG, Hipp MS, Hartl FU. Functional Modules of the Proteostasis Network. Cold Spring Harbor Perspectives in Biology. 12. PMID 30833457 DOI: 10.1101/cshperspect.a033951  0.546
2020 Hipp MS, Kasturi P, Hartl FU. The proteostasis network and its decline in ageing. Nature Reviews. Molecular Cell Biology. 20: 421-435. PMID 30733602 DOI: 10.1038/s41580-019-0101-y  0.536
2019 Vecchi G, Sormanni P, Mannini B, Vandelli A, Tartaglia GG, Dobson CM, Hartl FU, Vendruscolo M. Proteome-wide observation of the phenomenon of life on the edge of solubility. Proceedings of the National Academy of Sciences of the United States of America. PMID 31892536 DOI: 10.1073/Pnas.1910444117  0.336
2019 Zhao L, Vecchi G, Vendruscolo M, Körner R, Hayer-Hartl M, Hartl FU. The Hsp70 Chaperone System Stabilizes a Thermo-sensitive Subproteome in E. coli. Cell Reports. 28: 1335-1345.e6. PMID 31365874 DOI: 10.1016/J.Celrep.2019.06.081  0.604
2019 Frottin F, Schueder F, Tiwary S, Gupta R, Körner R, Schlichthaerle T, Cox J, Jungmann R, Hartl FU, Hipp MS. The nucleolus functions as a phase-separated protein quality control compartment. Science (New York, N.Y.). PMID 31296649 DOI: 10.1126/Science.Aaw9157  0.561
2019 Su T, Izawa T, Thoms M, Yamashita Y, Cheng J, Berninghausen O, Hartl FU, Inada T, Neupert W, Beckmann R. Publisher Correction: Structure and function of Vms1 and Arb1 in RQC and mitochondrial proteome homeostasis. Nature. PMID 31235950 DOI: 10.1038/S41586-019-1360-7  0.419
2019 Su T, Izawa T, Thoms M, Yamashita Y, Cheng J, Berninghausen O, Hartl FU, Inada T, Neupert W, Beckmann R. Structure and function of Vms1 and Arb1 in RQC and mitochondrial proteome homeostasis. Nature. PMID 31189955 DOI: 10.1038/S41586-019-1307-Z  0.543
2019 van Well EM, Bader V, Patra M, Sánchez-Vicente A, Meschede J, Furthmann N, Schnack C, Blusch A, Longworth J, Petrasch-Parwez E, Mori K, Arzberger T, Trümbach D, Angersbach L, Showkat C, ... ... Hartl FU, et al. A protein quality control pathway regulated by linear ubiquitination. The Embo Journal. PMID 30886048 DOI: 10.15252/Embj.2018100730  0.562
2019 Mönkemeyer L, Klaips CL, Balchin D, Körner R, Hartl FU, Bracher A. Chaperone Function of Hgh1 in the Biogenesis of Eukaryotic Elongation Factor 2. Molecular Cell. 74: 88-100.e9. PMID 30876804 DOI: 10.1016/j.molcel.2019.01.034  0.586
2019 Wilson RH, Thieulin-Pardo G, Hartl FU, Hayer-Hartl M. Improved recombinant expression and purification of functional plant Rubisco. Febs Letters. PMID 30815863 DOI: 10.1002/1873-3468.13352  0.467
2018 Gruber A, Hornburg D, Antonin M, Krahmer N, Collado J, Schaffer M, Zubaite G, Lüchtenborg C, Sachsenheimer T, Brügger B, Mann M, Baumeister W, Hartl FU, Hipp MS, Fernández-Busnadiego R. Molecular and structural architecture of polyQ aggregates in yeast. Proceedings of the National Academy of Sciences of the United States of America. PMID 29581260 DOI: 10.1073/Pnas.1717978115  0.324
2018 Hartl FU. Unfolding the chaperone story. Molecular Biology of the Cell. 28: 2919-2923. PMID 29084909 DOI: 10.1091/mbc.E17-07-0480  0.612
2017 Vincenz-Donnelly L, Holthusen H, Körner R, Hansen EC, Presto J, Johansson J, Sawarkar R, Hartl FU, Hipp MS. High capacity of the endoplasmic reticulum to prevent secretion and aggregation of amyloidogenic proteins. The Embo Journal. 37: 337-350. PMID 29247078 DOI: 10.15252/embj.201695841  0.541
2017 Hosp F, Gutiérrez-Ángel S, Schaefer MH, Cox J, Meissner F, Hipp MS, Hartl FU, Klein R, Dudanova I, Mann M. Spatiotemporal Proteomic Profiling of Huntington's Disease Inclusions Reveals Widespread Loss of Protein Function. Cell Reports. 21: 2291-2303. PMID 29166617 DOI: 10.1016/J.Celrep.2017.10.097  0.558
2017 Klaips CL, Jayaraj GG, Hartl FU. Pathways of cellular proteostasis in aging and disease. The Journal of Cell Biology. 217: 51-63. PMID 29127110 DOI: 10.1083/jcb.201709072  0.523
2017 Izawa T, Park SH, Zhao L, Hartl FU, Neupert W. Cytosolic Protein Vms1 Links Ribosome Quality Control to Mitochondrial and Cellular Homeostasis. Cell. PMID 29107329 DOI: 10.1016/j.cell.2017.10.002  0.525
2017 Zheng J, Yang J, Choe YJ, Hao X, Cao X, Zhao Q, Zhang Y, Franssens V, Hartl FU, Nyström T, Winderickx J, Liu B. Role of the ribosomal quality control machinery in nucleocytoplasmic translocation of polyQ-expanded huntingtin exon-1. Biochemical and Biophysical Research Communications. PMID 28864412 DOI: 10.1016/J.Bbrc.2017.08.126  0.487
2017 Hartl FU. Protein Misfolding Diseases. Annual Review of Biochemistry. 86: 21-26. PMID 28441058 DOI: 10.1146/annurev-biochem-061516-044518  0.585
2017 Walther DM, Kasturi P, Zheng M, Pinkert S, Vecchi G, Ciryam P, Morimoto RI, Dobson CM, Vendruscolo M, Mann M, Hartl FU. Widespread Proteome Remodeling and Aggregation in Aging C. elegans. Cell. 168: 944. PMID 28235202 DOI: 10.1016/J.Cell.2016.12.041  0.443
2017 Bracher A, Whitney SM, Hartl FU, Hayer-Hartl M. Biogenesis and Metabolic Maintenance of Rubisco. Annual Review of Plant Biology. PMID 28125284 DOI: 10.1146/annurev-arplant-043015-111633  0.478
2016 Hartl FU. Susan Lee Lindquist (1949-2016)-pioneer in the study of cellular protein folding and disease. The Embo Journal. PMID 27920028 DOI: 10.15252/embj.201670040  0.562
2016 Kim YE, Hosp F, Frottin F, Ge H, Mann M, Hayer-Hartl M, Hartl FU. Soluble Oligomers of PolyQ-Expanded Huntingtin Target a Multiplicity of Key Cellular Factors. Molecular Cell. PMID 27570076 DOI: 10.1016/J.Molcel.2016.07.022  0.391
2016 Balchin D, Hayer-Hartl M, Hartl FU. In vivo aspects of protein folding and quality control. Science (New York, N.Y.). 353: aac4354. PMID 27365453 DOI: 10.1126/science.aac4354  0.374
2016 Choe YJ, Park SH, Hassemer T, Körner R, Vincenz-Donnelly L, Hayer-Hartl M, Hartl FU. Failure of RQC machinery causes protein aggregation and proteotoxic stress. Nature. PMID 26934223 DOI: 10.1038/nature16973  0.351
2015 Woerner AC, Frottin F, Hornburg D, Feng LR, Meissner F, Patra M, Tatzelt J, Mann M, Winklhofer KF, Hartl FU, Hipp MS. Cytoplasmic protein aggregates interfere with nucleo-cytoplasmic transport of protein and RNA. Science (New York, N.Y.). PMID 26634439 DOI: 10.1126/Science.Aad2033  0.582
2015 Zhang J, Sun CF, Zhang MX, Hartl F, Yin J, Yu GA, Rao L, Liu SH. Asymmetric oxidation of vinyl- and ethynyl terthiophene ligands in triruthenium complexes. Dalton Transactions (Cambridge, England : 2003). PMID 26632006 DOI: 10.1039/c5dt04083c  0.43
2015 Chen L, Willcock H, Wedge CJ, Hartl F, Colquhoun HM, Greenland BW. Efficient access to conjugated 4,4'-bipyridinium oligomers using the Zincke reaction: synthesis, spectroscopic and electrochemical properties. Organic & Biomolecular Chemistry. PMID 26626110 DOI: 10.1039/C5Ob02211H  0.432
2015 Osorio HM, Catarelli S, Cea P, Gluyas JB, Hartl F, Higgins SJ, Leary E, Low PJ, Martín S, Nichols RJ, Tory J, Ulstrup J, Vezzoli A, Milan DC, Zeng Q. Electrochemical Single-Molecule Transistors with Optimized Gate Coupling. Journal of the American Chemical Society. PMID 26488257 DOI: 10.1021/Jacs.5B08431  0.401
2015 Hayer-Hartl M, Bracher A, Hartl FU. The GroEL-GroES Chaperonin Machine: A Nano-Cage for Protein Folding. Trends in Biochemical Sciences. PMID 26422689 DOI: 10.1016/j.tibs.2015.07.009  0.591
2015 Bracher A, Hauser T, Liu C, Hartl FU, Hayer-Hartl M. Structural Analysis of the Rubisco-Assembly Chaperone RbcX-II from Chlamydomonas reinhardtii. Plos One. 10: e0135448. PMID 26305355 DOI: 10.1371/journal.pone.0135448  0.559
2015 Hauser T, Bhat JY, Miličić G, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M. Structure and mechanism of the Rubisco-assembly chaperone Raf1. Nature Structural & Molecular Biology. 22: 720-8. PMID 26237510 DOI: 10.1038/nsmb.3062  0.509
2015 Kirstein J, Morito D, Kakihana T, Sugihara M, Minnen A, Hipp MS, Nussbaum-Krammer C, Kasturi P, Hartl FU, Nagata K, Morimoto RI. Proteotoxic stress and ageing triggers the loss of redox homeostasis across cellular compartments. The Embo Journal. 34: 2334-49. PMID 26228940 DOI: 10.15252/Embj.201591711  0.522
2015 Walther DM, Kasturi P, Zheng M, Pinkert S, Vecchi G, Ciryam P, Morimoto RI, Dobson CM, Vendruscolo M, Mann M, Hartl FU. Widespread Proteome Remodeling and Aggregation in Aging C. elegans. Cell. 161: 919-32. PMID 25957690 DOI: 10.1016/J.Cell.2015.03.032  0.586
2015 Haldar S, Gupta AJ, Yan X, Mili?i? G, Hartl FU, Hayer-Hartl M. Chaperonin-Assisted Protein Folding: Relative Population of Asymmetric and Symmetric GroEL:GroES Complexes. Journal of Molecular Biology. 427: 2244-55. PMID 25912285 DOI: 10.1016/J.Jmb.2015.04.009  0.551
2015 Nunes JM, Mayer-Hartl M, Hartl FU, Müller DJ. Action of the Hsp70 chaperone system observed with single proteins. Nature Communications. 6: 6307. PMID 25686738 DOI: 10.1038/ncomms7307  0.584
2015 Sun B, Hartl F, Castiglione K, Weuster-Botz D. Dynamic mechanistic modeling of the multienzymatic one-pot reduction of dehydrocholic acid to 12-keto ursodeoxycholic acid with competing substrates and cofactors. Biotechnology Progress. 31: 375-86. PMID 25641915 DOI: 10.1002/btpr.2036  0.393
2015 Durão P, Aigner H, Nagy P, Mueller-Cajar O, Hartl FU, Hayer-Hartl M. Opposing effects of folding and assembly chaperones on evolvability of Rubisco. Nature Chemical Biology. 11: 148-55. PMID 25558973 DOI: 10.1038/nchembio.1715  0.502
2015 Joshi J, Mueller-Cajar O, Tsai YC, Hartl FU, Hayer-Hartl M. Role of small subunit in mediating assembly of red-type form I Rubisco. The Journal of Biological Chemistry. 290: 1066-74. PMID 25371207 DOI: 10.1074/jbc.M114.613091  0.48
2014 Ripaud L, Chumakova V, Antonin M, Hastie AR, Pinkert S, Körner R, Ruff KM, Pappu RV, Hornburg D, Mann M, Hartl FU, Hipp MS. Overexpression of Q-rich prion-like proteins suppresses polyQ cytotoxicity and alters the polyQ interactome. Proceedings of the National Academy of Sciences of the United States of America. 111: 18219-24. PMID 25489109 DOI: 10.1073/Pnas.1421313111  0.59
2014 Domingos SR, Sanders HJ, Hartl F, Buma WJ, Woutersen S. Switchable amplification of vibrational circular dichroism as a probe of local chiral structure. Angewandte Chemie (International Ed. in English). 53: 14042-5. PMID 25212702 DOI: 10.1002/Anie.201407376  0.41
2014 Hashem E, Platts JA, Hartl F, Lorusso G, Evangelisti M, Schulzke C, Baker RJ. Thiocyanate complexes of uranium in multiple oxidation states: a combined structural, magnetic, spectroscopic, spectroelectrochemical, and theoretical study. Inorganic Chemistry. 53: 8624-37. PMID 25072532 DOI: 10.1021/Ic501236J  0.41
2014 Ferrón CC, Capdevila-Cortada M, Balster R, Hartl F, Niu W, He M, Novoa JJ, López Navarrete JT, Hernández V, Ruiz Delgado MC. Multistep π dimerization of tetrakis(n-decyl)heptathienoacene radical cations: a combined experimental and theoretical study. Chemistry (Weinheim An Der Bergstrasse, Germany). 20: 10351-9. PMID 25043826 DOI: 10.1002/chem.201402182  0.445
2014 Hipp MS, Park SH, Hartl FU. Proteostasis impairment in protein-misfolding and -aggregation diseases. Trends in Cell Biology. 24: 506-14. PMID 24946960 DOI: 10.1016/j.tcb.2014.05.003  0.572
2014 Gupta AJ, Haldar S, Mili?i? G, Hartl FU, Hayer-Hartl M. Active cage mechanism of chaperonin-assisted protein folding demonstrated at single-molecule level. Journal of Molecular Biology. 426: 2739-54. PMID 24816391 DOI: 10.1018/J.Jmb.2014.04.018  0.592
2014 Georgescauld F, Popova K, Gupta AJ, Bracher A, Engen JR, Hayer-Hartl M, Hartl FU. GroEL/ES chaperonin modulates the mechanism and accelerates the rate of TIM-barrel domain folding. Cell. 157: 922-34. PMID 24813614 DOI: 10.1016/J.Cell.2014.03.038  0.576
2014 Li P, Amirjalayer S, Hartl F, Lutz M, de Bruin B, Becker R, Woutersen S, Reek JN. Direct probing of photoinduced electron transfer in a self-assembled biomimetic [2Fe2S]-hydrogenase complex using ultrafast vibrational spectroscopy. Inorganic Chemistry. 53: 5373-83. PMID 24766080 DOI: 10.1021/Ic500777D  0.437
2014 Derossi S, Becker R, Li P, Hartl F, Reek JN. A phosphoramidite-based [FeFe]H2ase functional mimic displaying fast electrocatalytic proton reduction. Dalton Transactions (Cambridge, England : 2003). 43: 8363-7. PMID 24733487 DOI: 10.1039/C3Dt53471E  0.432
2014 Vincenz L, Hartl FU. Sugarcoating ER Stress. Cell. 156: 1125-7. PMID 24630714 DOI: 10.1016/j.cell.2014.02.035  0.472
2014 Leitman J, Barak B, Benyair R, Shenkman M, Ashery U, Hartl FU, Lederkremer GZ. ER stress-induced eIF2-alpha phosphorylation underlies sensitivity of striatal neurons to pathogenic huntingtin. Plos One. 9: e90803. PMID 24594939 DOI: 10.1371/Journal.Pone.0090803  0.466
2014 Raychaudhuri S, Loew C, Körner R, Pinkert S, Theis M, Hayer-Hartl M, Buchholz F, Hartl FU. Interplay of acetyltransferase EP300 and the proteasome system in regulating heat shock transcription factor 1. Cell. 156: 975-85. PMID 24581496 DOI: 10.1016/j.cell.2014.01.055  0.54
2014 Ou YP, Zhang J, Xu M, Xia J, Hartl F, Yin J, Yu GA, Liu SH. Bridge-localized HOMO-binding character of divinylanthracene-bridged dinuclear ruthenium carbonyl complexes: spectroscopic, spectroelectrochemical, and computational studies. Chemistry, An Asian Journal. 9: 1152-60. PMID 24449396 DOI: 10.1002/Asia.201301544  0.422
2013 Hartl FU, Hayer-Hartl M. The first chaperonin. Nature Reviews. Molecular Cell Biology. 14: 611. PMID 24061226 DOI: 10.1038/nrm3665  0.496
2013 Li Z, Hartl FU, Bracher A. Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle. Nature Structural & Molecular Biology. 20: 929-35. PMID 23812373 DOI: 10.1038/nsmb.2608  0.591
2013 Park SH, Kukushkin Y, Gupta R, Chen T, Konagai A, Hipp MS, Hayer-Hartl M, Hartl FU. PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone. Cell. 154: 134-45. PMID 23791384 DOI: 10.1016/j.cell.2013.06.003  0.604
2013 Kim YE, Hipp MS, Bracher A, Hayer-Hartl M, Hartl FU. Molecular chaperone functions in protein folding and proteostasis. Annual Review of Biochemistry. 82: 323-55. PMID 23746257 DOI: 10.1146/annurev-biochem-060208-092442  0.631
2013 Domingos SR, Luyten H, van Anrooij F, Sanders HJ, Bakker BH, Buma WJ, Hartl F, Woutersen S. An optically transparent thin-layer electrochemical cell for the study of vibrational circular dichroism of chiral redox-active molecules. The Review of Scientific Instruments. 84: 033103. PMID 23556803 DOI: 10.1063/1.4793722  0.409
2012 Rüßmann F, Stemp MJ, Mönkemeyer L, Etchells SA, Bracher A, Hartl FU. Folding of large multidomain proteins by partial encapsulation in the chaperonin TRiC/CCT. Proceedings of the National Academy of Sciences of the United States of America. 109: 21208-15. PMID 23197838 DOI: 10.1073/pnas.1218836109  0.579
2012 Herzog F, Kahraman A, Boehringer D, Mak R, Bracher A, Walzthoeni T, Leitner A, Beck M, Hartl FU, Ban N, Malmström L, Aebersold R. Structural probing of a protein phosphatase 2A network by chemical cross-linking and mass spectrometry. Science (New York, N.Y.). 337: 1348-52. PMID 22984071 DOI: 10.1126/Science.1221483  0.551
2012 Chippindale AM, Hibble SJ, Bilbé EJ, Marelli E, Hannon AC, Allain C, Pansu R, Hartl F. Mixed copper, silver, and gold cyanides, (M(x)M'(1-x))CN: tailoring chain structures to influence physical properties. Journal of the American Chemical Society. 134: 16387-400. PMID 22954066 DOI: 10.1021/Ja307087D  0.399
2012 Calloni G, Chen T, Schermann SM, Chang HC, Genevaux P, Agostini F, Tartaglia GG, Hayer-Hartl M, Hartl FU. DnaK functions as a central hub in the E. coli chaperone network. Cell Reports. 1: 251-64. PMID 22832197 DOI: 10.1016/J.Celrep.2011.12.007  0.595
2012 Wragg AB, Derossi S, Easun TL, George MW, Sun XZ, Hartl F, Shelton AH, Meijer AJ, Ward MD. Solvent-dependent modulation of metal-metal electronic interactions in a dinuclear cyanoruthenate complex: a detailed electrochemical, spectroscopic and computational study. Dalton Transactions (Cambridge, England : 2003). 41: 10354-71. PMID 22810117 DOI: 10.1039/C2Dt31001E  0.409
2012 Schnöckelborg EM, Khusniyarov MM, De Bruin B, Hartl F, Langer T, Eul M, Schulz S, Pöttgen R, Wolf R. Unraveling the electronic structures of low-valent naphthalene and anthracene iron complexes: X-ray, spectroscopic, and density functional theory studies Inorganic Chemistry. 51: 6719-6730. PMID 22639983 DOI: 10.1021/ic300366m  0.419
2012 Tsai YC, Mueller-Cajar O, Saschenbrecker S, Hartl FU, Hayer-Hartl M. Chaperonin cofactors, Cpn10 and Cpn20, of green algae and plants function as hetero-oligomeric ring complexes. The Journal of Biological Chemistry. 287: 20471-81. PMID 22518837 DOI: 10.1074/jbc.M112.365411  0.58
2012 Leitner A, Joachimiak LA, Bracher A, Mönkemeyer L, Walzthoeni T, Chen B, Pechmann S, Holmes S, Cong Y, Ma B, Ludtke S, Chiu W, Hartl FU, Aebersold R, Frydman J. The molecular architecture of the eukaryotic chaperonin TRiC/CCT. Structure (London, England : 1993). 20: 814-25. PMID 22503819 DOI: 10.1016/J.Str.2012.03.007  0.657
2012 Lamond AI, Uhlen M, Horning S, Makarov A, Robinson CV, Serrano L, Hartl FU, Baumeister W, Werenskiold AK, Andersen JS, Vorm O, Linial M, Aebersold R, Mann M. Advancing cell biology through proteomics in space and time (PROSPECTS). Molecular & Cellular Proteomics : McP. 11: O112.017731. PMID 22311636 DOI: 10.1074/Mcp.O112.017731  0.525
2012 Sharma K, Vabulas RM, Macek B, Pinkert S, Cox J, Mann M, Hartl FU. Quantitative proteomics reveals that Hsp90 inhibition preferentially targets kinases and the DNA damage response. Molecular & Cellular Proteomics : McP. 11: M111.014654. PMID 22167270 DOI: 10.1074/Mcp.M111.014654  0.744
2012 Domingos SR, Panman MR, Bakker BH, Hartl F, Buma WJ, Woutersen S. Amplifying vibrational circular dichroism by manipulation of the electronic manifold. Chemical Communications (Cambridge, England). 48: 353-5. PMID 22002107 DOI: 10.1039/C1Cc15369B  0.401
2011 Stotz M, Mueller-Cajar O, Ciniawsky S, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M. Structure of green-type Rubisco activase from tobacco. Nature Structural & Molecular Biology. 18: 1366-70. PMID 22056769 DOI: 10.1038/nsmb.2171  0.508
2011 Mueller-Cajar O, Stotz M, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M. Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase. Nature. 479: 194-9. PMID 22048315 DOI: 10.1038/nature10568  0.591
2011 Capel Ferrón C, Ruiz Delgado MC, Hernández V, López Navarrete JT, Vercelli B, Zotti G, Capdevila Cortada M, Novoa JJ, Niu W, He M, Hartl F. Substituent and counterion effects on the formation of π-dimer dications of end-capped heptathienoacenes. Chemical Communications (Cambridge, England). 47: 12622-4. PMID 22039584 DOI: 10.1039/c1cc14566e  0.438
2011 Hartl FU. Chaperone-assisted protein folding: the path to discovery from a personal perspective. Nature Medicine. 17: 1206-10. PMID 21989011 DOI: 10.1038/nm.2467  0.547
2011 Fox MA, Le Guennic B, Roberts RL, Brue DA, Yufit DS, Howard JA, Manca G, Halet JF, Hartl F, Low PJ. Simultaneous bridge-localized and mixed-valence character in diruthenium radical cations featuring diethynylaromatic bridging ligands. Journal of the American Chemical Society. 133: 18433-46. PMID 21958078 DOI: 10.1021/Ja207827M  0.418
2011 Gupta R, Kasturi P, Bracher A, Loew C, Zheng M, Villella A, Garza D, Hartl FU, Raychaudhuri S. Firefly luciferase mutants as sensors of proteome stress. Nature Methods. 8: 879-84. PMID 21892152 DOI: 10.1038/nmeth.1697  0.495
2011 Hartl FU, Bracher A, Hayer-Hartl M. Molecular chaperones in protein folding and proteostasis. Nature. 475: 324-32. PMID 21776078 DOI: 10.1038/nature10317  0.602
2011 Bracher A, Starling-Windhof A, Hartl FU, Hayer-Hartl M. Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco. Nature Structural & Molecular Biology. 18: 875-80. PMID 21765418 DOI: 10.1038/nsmb.2090  0.522
2011 Wolf P, Hartl F, Brischwein M, Wolf B. Determination of dynamic doxorubicin-EC 50 value in an automated high-content workstation for cellular assays Toxicology in Vitro. 25: 1889-1894. PMID 21693178 DOI: 10.1016/j.tiv.2011.05.031  0.389
2011 Vabulas RM, Hartl FU. Aberrant protein interactions in amyloid disease. Cell Cycle (Georgetown, Tex.). 10: 1512-3. PMID 21464615  0.523
2011 Resenberger UK, Harmeier A, Woerner AC, Goodman JL, Müller V, Krishnan R, Vabulas RM, Kretzschmar HA, Lindquist S, Hartl FU, Multhaup G, Winklhofer KF, Tatzelt J. The cellular prion protein mediates neurotoxic signalling of β-sheet-rich conformers independent of prion replication. The Embo Journal. 30: 2057-70. PMID 21441896 DOI: 10.1038/emboj.2011.86  0.507
2011 Olzscha H, Schermann SM, Woerner AC, Pinkert S, Hecht MH, Tartaglia GG, Vendruscolo M, Hayer-Hartl M, Hartl FU, Vabulas RM. Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. Cell. 144: 67-78. PMID 21215370 DOI: 10.1016/J.Cell.2010.11.050  0.599
2011 Alatorre-Meda M, Taboada P, Hartl F, Wagner T, Freis M, Rodríguez JR. The influence of chitosan valence on the complexation and transfection of DNA: the weaker the DNA-chitosan binding the higher the transfection efficiency. Colloids and Surfaces. B, Biointerfaces. 82: 54-62. PMID 20828996 DOI: 10.1016/j.colsurfb.2010.08.013  0.419
2010 Wolf R, Ehlers AW, Khusniyarov MM, Hartl F, de Bruin B, Long GJ, Grandjean F, Schappacher FM, Pöttgen R, Slootweg JC, Lutz M, Spek AL, Lammertsma K. Homoleptic diphosphacyclobutadiene complexes [M(η(4)-P2C2R2)2]x- (M = Fe, Co; x = 0, 1). Chemistry (Weinheim An Der Bergstrasse, Germany). 16: 14322-34. PMID 21125622 DOI: 10.1002/Chem.201001913  0.415
2010 Vabulas RM, Raychaudhuri S, Hayer-Hartl M, Hartl FU. Protein folding in the cytoplasm and the heat shock response. Cold Spring Harbor Perspectives in Biology. 2: a004390. PMID 21123396 DOI: 10.1101/cshperspect.a004390  0.608
2010 Brandt F, Carlson LA, Hartl FU, Baumeister W, Grünewald K. The three-dimensional organization of polyribosomes in intact human cells. Molecular Cell. 39: 560-9. PMID 20797628 DOI: 10.1016/J.Molcel.2010.08.003  0.49
2010 Ortiz JO, Brandt F, Matias VR, Sennels L, Rappsilber J, Scheres SH, Eibauer M, Hartl FU, Baumeister W. Structure of hibernating ribosomes studied by cryoelectron tomography in vitro and in situ. The Journal of Cell Biology. 190: 613-21. PMID 20733057 DOI: 10.1083/Jcb.201005007  0.503
2010 Gupta R, Lakshmipathy SK, Chang HC, Etchells SA, Hartl FU. Trigger factor lacking the PPIase domain can enhance the folding of eukaryotic multi-domain proteins in Escherichia coli. Febs Letters. 584: 3620-4. PMID 20659464 DOI: 10.1016/j.febslet.2010.07.036  0.567
2010 Polier S, Hartl FU, Bracher A. Interaction of the Hsp110 molecular chaperones from S. cerevisiae with substrate protein. Journal of Molecular Biology. 401: 696-707. PMID 20624400 DOI: 10.1016/j.jmb.2010.07.004  0.575
2010 Chakraborty K, Chatila M, Sinha J, Shi Q, Poschner BC, Sikor M, Jiang G, Lamb DC, Hartl FU, Hayer-Hartl M. Chaperonin-catalyzed rescue of kinetically trapped states in protein folding. Cell. 142: 112-22. PMID 20603018 DOI: 10.1016/J.Cell.2010.05.027  0.594
2010 Lakshmipathy SK, Gupta R, Pinkert S, Etchells SA, Hartl FU. Versatility of trigger factor interactions with ribosome-nascent chain complexes. The Journal of Biological Chemistry. 285: 27911-23. PMID 20595383 DOI: 10.1074/jbc.M110.134163  0.558
2010 Tartaglia GG, Dobson CM, Hartl FU, Vendruscolo M. Physicochemical determinants of chaperone requirements. Journal of Molecular Biology. 400: 579-88. PMID 20416322 DOI: 10.1016/J.Jmb.2010.03.066  0.531
2010 Lewiecki EM, Cooper C, Thompson E, Hartl F, Mehta D, Papapoulos SE. Ibandronate does not increase risk of atrial fibrillation in analysis of pivotal clinical trials International Journal of Clinical Practice. 64: 821-826. PMID 20337751 DOI: 10.1111/j.1742-1241.2010.02335.x  0.378
2010 Jürgens M, Laubender RP, Hartl F, Weidinger M, Seiderer J, Wagner J, Wetzke M, Beigel F, Pfennig S, Stallhofer J, Schnitzler F, Tillack C, Lohse P, Göke B, Glas J, et al. Disease activity, ANCA, and IL23R genotype status determine early response to infliximab in patients with ulcerative colitis American Journal of Gastroenterology. 105: 1811-1819. PMID 20197757 DOI: 10.1038/ajg.2010.95  0.389
2010 Liu C, Young AL, Starling-Windhof A, Bracher A, Saschenbrecker S, Rao BV, Rao KV, Berninghausen O, Mielke T, Hartl FU, Beckmann R, Hayer-Hartl M. Coupled chaperone action in folding and assembly of hexadecameric Rubisco. Nature. 463: 197-202. PMID 20075914 DOI: 10.1038/Nature08651  0.524
2009 Wadman SH, Havenith RW, Hartl F, Lutz M, Spek AL, van Klink GP, van Koten G. Redox chemistry and electronic properties of 2,3,5,6-tetrakis(2-pyridyl)pyrazine-bridged diruthenium complexes controlled by N,C,N'-biscyclometalated ligands. Inorganic Chemistry. 48: 5685-96. PMID 20507098 DOI: 10.1021/Ic801897K  0.413
2009 Roy S, Maheswari PU, Lutz M, Spek AL, den Dulk H, Barends S, van Wezel GP, Hartl F, Reedijk J. DNA cleavage and antitumour activity of platinum(II) and copper(II) compounds derived from 4-methyl-2-N-(2-pyridylmethyl)aminophenol: spectroscopic, electrochemical and biological investigation. Dalton Transactions (Cambridge, England : 2003). 10846-60. PMID 20023915 DOI: 10.1039/B911542K  0.426
2009 Hirtreiter AM, Calloni G, Forner F, Scheibe B, Puype M, Vandekerckhove J, Mann M, Hartl FU, Hayer-Hartl M. Differential substrate specificity of group I and group II chaperonins in the archaeon Methanosarcina mazei. Molecular Microbiology. 74: 1152-68. PMID 19843217 DOI: 10.1111/J.1365-2958.2009.06924.X  0.551
2009 Tejel C, del Río MP, Ciriano MA, Reijerse EJ, Hartl F, Zális S, Hetterscheid DG, Tsichlis i Spithas N, de Bruin B. Ligand-centred reactivity of bis(picolyl)amine iridium: sequential deprotonation, oxidation and oxygenation of a "non-innocent" ligand. Chemistry (Weinheim An Der Bergstrasse, Germany). 15: 11878-89. PMID 19790209 DOI: 10.1002/chem.200901017  0.416
2009 Hartl FU, Hayer-Hartl M. Converging concepts of protein folding in vitro and in vivo. Nature Structural & Molecular Biology. 16: 574-81. PMID 19491934 DOI: 10.1038/nsmb.1591  0.6
2009 Jukes RT, Kühni J, Salluce N, Belser P, De Cola L, Hartl F. Photochemical, photophysical and redox properties of novel fulgimide derivatives with attached 2,2'-bipyridine (bpy) and [M(bpy)(3)](2+) (M = Ru and Os) moieties. Dalton Transactions (Cambridge, England : 2003). 3993-4002. PMID 19440599 DOI: 10.1039/B821637C  0.423
2009 Broadley SA, Hartl FU. The role of molecular chaperones in human misfolding diseases. Febs Letters. 583: 2647-53. PMID 19393652 DOI: 10.1016/j.febslet.2009.04.029  0.572
2009 Reid DM, Devogelaer JP, Saag K, Roux C, Lau CS, Reginster JY, Papanastasiou P, Ferreira A, Hartl F, Fashola T, Mesenbrink P, Sambrook PN. Zoledronic acid and risedronate in the prevention and treatment of glucocorticoid-induced osteoporosis (HORIZON): a multicentre, double-blind, double-dummy, randomised controlled trial. Lancet (London, England). 373: 1253-63. PMID 19362675 DOI: 10.1016/S0140-6736(09)60250-6  0.387
2009 Gamerdinger M, Hajieva P, Kaya AM, Wolfrum U, Hartl FU, Behl C. Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3. The Embo Journal. 28: 889-901. PMID 19229298 DOI: 10.1038/emboj.2009.29  0.566
2009 Brandt F, Etchells SA, Ortiz JO, Elcock AH, Hartl FU, Baumeister W. The native 3D organization of bacterial polysomes. Cell. 136: 261-71. PMID 19167328 DOI: 10.1016/J.Cell.2008.11.016  0.49
2009 Kluwer AM, Kapre R, Hartl F, Lutz M, Spek AL, Brouwer AM, van Leeuwen PW, Reek JN. Molecular recognition and self-assembly special feature: Self-assembled biomimetic [2Fe2S]-hydrogenase-based photocatalyst for molecular hydrogen evolution. Proceedings of the National Academy of Sciences of the United States of America. 106: 10460-5. PMID 19164541 DOI: 10.1073/Pnas.0809666106  0.444
2009 Wolf R, Slootweg JC, Ehlers AW, Hartl F, de Bruin B, Lutz M, Spek AL, Lammertsma K. A phosphorus analogue of Bis(eta4-cyclobutadiene)iron(0). Angewandte Chemie (International Ed. in English). 48: 3104-7. PMID 19142921 DOI: 10.1002/Anie.200805193  0.412
2008 Schiffer NW, Céraline J, Hartl FU, Broadley SA. N-terminal polyglutamine-containing fragments inhibit androgen receptor transactivation function. Biological Chemistry. 389: 1455-66. PMID 18844449 DOI: 10.1515/BC.2008.169  0.493
2008 Zitzler S, Hellwig A, Hartl FU, Wieland F, Diestelkötter-Bachert P. Distinct binding sites for the ATPase and substrate-binding domain of human Hsp70 on the cell surface of antigen presenting cells. Molecular Immunology. 45: 3974-83. PMID 18657319 DOI: 10.1016/j.molimm.2008.06.022  0.514
2008 Polier S, Dragovic Z, Hartl FU, Bracher A. Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding. Cell. 133: 1068-79. PMID 18555782 DOI: 10.1016/j.cell.2008.05.022  0.594
2008 Tang YC, Chang HC, Chakraborty K, Hartl FU, Hayer-Hartl M. Essential role of the chaperonin folding compartment in vivo. The Embo Journal. 27: 1458-68. PMID 18418386 DOI: 10.1038/emboj.2008.77  0.588
2008 Sharma S, Chakraborty K, Müller BK, Astola N, Tang YC, Lamb DC, Hayer-Hartl M, Hartl FU. Monitoring protein conformation along the pathway of chaperonin-assisted folding. Cell. 133: 142-53. PMID 18394994 DOI: 10.1016/J.Cell.2008.01.048  0.6
2008 Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D. Protein abundance profiling of the Escherichia coli cytosol. Bmc Genomics. 9: 102. PMID 18304323 DOI: 10.1186/1471-2164-9-102  0.529
2008 Siegers K, Bölter B, Schwarz JP, Böttcher UM, Guha S, Hartl FU. TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. The Embo Journal. 27: 301. PMID 18185496 DOI: 10.1038/sj.emboj.7601964  0.571
2008 Broadley SA, Hartl FU. Mitochondrial stress signaling: a pathway unfolds. Trends in Cell Biology. 18: 1-4. PMID 18068368 DOI: 10.1016/j.tcb.2007.11.003  0.513
2007 Chang HC, Tang YC, Hayer-Hartl M, Hartl FU. SnapShot: molecular chaperones, Part I. Cell. 128: 212. PMID 17990378 DOI: 10.1016/j.cell.2007.01.001  0.469
2007 Grallath S, Schwarz JP, Bottcher UM, Bracher A, Hartl FU, Siegers K. L25 functions as a conserved ribosomal docking site shared by nascent chain-associated complex and signal-recognition particle. Embo Reports. 8: 1086. PMID 17972903 DOI: 10.1038/sj.embor.7401114  0.438
2007 Saschenbrecker S, Bracher A, Rao KV, Rao BV, Hartl FU, Hayer-Hartl M. Structure and function of RbcX, an assembly chaperone for hexadecameric Rubisco. Cell. 129: 1189-200. PMID 17574029 DOI: 10.1016/j.cell.2007.04.025  0.549
2007 Haacke A, Hartl FU, Breuer P. Calpain inhibition is sufficient to suppress aggregation of polyglutamine-expanded ataxin-3. The Journal of Biological Chemistry. 282: 18851-6. PMID 17488727 DOI: 10.1074/jbc.M611914200  0.487
2007 Lakshmipathy SK, Tomic S, Kaiser CM, Chang HC, Genevaux P, Georgopoulos C, Barral JM, Johnson AE, Hartl FU, Etchells SA. Identification of nascent chain interaction sites on trigger factor. The Journal of Biological Chemistry. 282: 12186-93. PMID 17296610 DOI: 10.1074/Jbc.M609871200  0.512
2007 Tang YC, Chang HC, Hayer-Hartl M, Hartl FU. SnapShot: molecular chaperones, Part II. Cell. 128: 412. PMID 17254976 DOI: 10.1016/j.cell.2007.01.013  0.437
2007 Schiffer NW, Broadley SA, Hirschberger T, Tavan P, Kretzschmar HA, Giese A, Haass C, Hartl FU, Schmid B. Identification of anti-prion compounds as efficient inhibitors of polyglutamine protein aggregation in a zebrafish model. The Journal of Biological Chemistry. 282: 9195-203. PMID 17170113 DOI: 10.1074/Jbc.M607865200  0.528
2006 Dragovic Z, Shomura Y, Tzvetkov N, Hartl FU, Bracher A. Fes1p acts as a nucleotide exchange factor for the ribosome-associated molecular chaperone Ssb1p. Biological Chemistry. 387: 1593-600. PMID 17132105 DOI: 10.1515/BC.2006.198  0.571
2006 Kaiser CM, Chang HC, Agashe VR, Lakshmipathy SK, Etchells SA, Hayer-Hartl M, Hartl FU, Barral JM. Real-time observation of trigger factor function on translating ribosomes. Nature. 444: 455-60. PMID 17051157 DOI: 10.1038/Nature05225  0.544
2006 Fonseca R, Vabulas RM, Hartl FU, Bonhoeffer T, Nägerl UV. A balance of protein synthesis and proteasome-dependent degradation determines the maintenance of LTP. Neuron. 52: 239-45. PMID 17046687 DOI: 10.1016/j.neuron.2006.08.015  0.528
2006 Behrends C, Langer CA, Boteva R, Böttcher UM, Stemp MJ, Schaffar G, Rao BV, Giese A, Kretzschmar H, Siegers K, Hartl FU. Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers. Molecular Cell. 23: 887-97. PMID 16973440 DOI: 10.1016/j.molcel.2006.08.017  0.593
2006 Bracher A, Hartl FU. Hsp90 structure: when two ends meet. Nature Structural & Molecular Biology. 13: 478-80. PMID 16757946 DOI: 10.1038/nsmb0606-478  0.47
2006 Tang YC, Chang HC, Roeben A, Wischnewski D, Wischnewski N, Kerner MJ, Hartl FU, Hayer-Hartl M. Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein. Cell. 125: 903-14. PMID 16751100 DOI: 10.1016/j.cell.2006.04.027  0.594
2006 Dragovic Z, Broadley SA, Shomura Y, Bracher A, Hartl FU. Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. The Embo Journal. 25: 2519-28. PMID 16688212 DOI: 10.1038/sj.emboj.7601138  0.591
2006 Roeben A, Kofler C, Nagy I, Nickell S, Hartl FU, Bracher A. Crystal structure of an archaeal actin homolog. Journal of Molecular Biology. 358: 145-56. PMID 16500678 DOI: 10.1016/j.jmb.2006.01.096  0.5
2006 Haacke A, Broadley SA, Boteva R, Tzvetkov N, Hartl FU, Breuer P. Proteolytic cleavage of polyglutamine-expanded ataxin-3 is critical for aggregation and sequestration of non-expanded ataxin-3. Human Molecular Genetics. 15: 555-68. PMID 16407371 DOI: 10.1093/hmg/ddi472  0.51
2006 Tomic S, Johnson AE, Hartl FU, Etchells SA. Exploring the capacity of trigger factor to function as a shield for ribosome bound polypeptide chains. Febs Letters. 580: 72-6. PMID 16359675 DOI: 10.1016/J.Febslet.2005.11.050  0.499
2006 Grallath S, Schwarz JP, Böttcher UM, Bracher A, Hartl FU, Siegers K. L25 functions as a conserved ribosomal docking site shared by nascent chain-associated complex and signal-recognition particle. Embo Reports. 7: 78-84. PMID 16239928 DOI: 10.1038/sj.embor.7400551  0.565
2005 Vabulas RM, Hartl FU. Protein synthesis upon acute nutrient restriction relies on proteasome function. Science (New York, N.Y.). 310: 1960-3. PMID 16373576 DOI: 10.1126/science.1121925  0.51
2005 Stemp MJ, Guha S, Hartl FU, Barral JM. Efficient production of native actin upon translation in a bacterial lysate supplemented with the eukaryotic chaperonin TRiC. Biological Chemistry. 386: 753-7. PMID 16201870 DOI: 10.1515/BC.2005.088  0.535
2005 Chang HC, Kaiser CM, Hartl FU, Barral JM. De novo folding of GFP fusion proteins: high efficiency in eukaryotes but not in bacteria. Journal of Molecular Biology. 353: 397-409. PMID 16171814 DOI: 10.1016/J.Jmb.2005.08.052  0.573
2005 Hartl FU. Paper of the year 2004: award to Yin Wang and Iris Lorenzi. Biological Chemistry. 386: 815. PMID 16164406 DOI: 10.1515/BC.2005.096  0.367
2005 Martin J, Hartl FU. Protein folding in the cell: molecular chaperones pave the way. Structure (London, England : 1993). 1: 161-4. PMID 16100950 DOI: 10.1016/0969-2126(93)90017-B  0.607
2005 Kerner MJ, Naylor DJ, Ishihama Y, Maier T, Chang HC, Stines AP, Georgopoulos C, Frishman D, Hayer-Hartl M, Mann M, Hartl FU. Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. Cell. 122: 209-20. PMID 16051146 DOI: 10.1016/J.Cell.2005.05.028  0.614
2005 Bertsch U, Winklhofer KF, Hirschberger T, Bieschke J, Weber P, Hartl FU, Tavan P, Tatzelt J, Kretzschmar HA, Giese A. Systematic identification of antiprion drugs by high-throughput screening based on scanning for intensely fluorescent targets. Journal of Virology. 79: 7785-91. PMID 15919931 DOI: 10.1128/Jvi.79.12.7785-7791.2005  0.483
2005 Bracher A, Hartl FU. Towards a complete structure of Hsp90. Structure (London, England : 1993). 13: 501-2. PMID 15837187 DOI: 10.1016/j.str.2005.03.004  0.474
2005 Shomura Y, Dragovic Z, Chang HC, Tzvetkov N, Young JC, Brodsky JL, Guerriero V, Hartl FU, Bracher A. Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange. Molecular Cell. 17: 367-79. PMID 15694338 DOI: 10.1016/j.molcel.2004.12.023  0.566
2004 Hartl FU. Wolfgang Baumeister--Felix Hoppe-Seyler Lecturer 2004. Biological Chemistry. 385: 863. PMID 15551858 DOI: 10.1515/BC.2004.112  0.366
2004 Young JC, Agashe VR, Siegers K, Hartl FU. Pathways of chaperone-mediated protein folding in the cytosol. Nature Reviews. Molecular Cell Biology. 5: 781-91. PMID 15459659 DOI: 10.1038/nrm1492  0.578
2004 Schaffar G, Breuer P, Boteva R, Behrends C, Tzvetkov N, Strippel N, Sakahira H, Siegers K, Hayer-Hartl M, Hartl FU. Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation. Molecular Cell. 15: 95-105. PMID 15225551 DOI: 10.1016/j.molcel.2004.06.029  0.574
2004 Etchells SA, Hartl FU. The dynamic tunnel. Nature Structural & Molecular Biology. 11: 391-2. PMID 15114338 DOI: 10.1038/nsmb0504-391  0.369
2004 Agashe VR, Guha S, Chang HC, Genevaux P, Hayer-Hartl M, Stemp M, Georgopoulos C, Hartl FU, Barral JM. Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed. Cell. 117: 199-209. PMID 15084258 DOI: 10.1016/S0092-8674(04)00299-5  0.583
2004 Barral JM, Broadley SA, Schaffar G, Hartl FU. Roles of molecular chaperones in protein misfolding diseases. Seminars in Cell & Developmental Biology. 15: 17-29. PMID 15036203 DOI: 10.1016/j.semcdb.2003.12.010  0.572
2004 Wochnik GM, Young JC, Schmidt U, Holsboer F, Hartl FU, Rein T. Inhibition of GR-mediated transcription by p23 requires interaction with Hsp90. Febs Letters. 560: 35-8. PMID 14987994 DOI: 10.1016/S0014-5793(04)00066-3  0.513
2004 Genevaux P, Keppel F, Schwager F, Langendijk-Genevaux PS, Hartl FU, Georgopoulos C. In vivo analysis of the overlapping functions of DnaK and trigger factor. Embo Reports. 5: 195-200. PMID 14726952 DOI: 10.1038/sj.embor.7400067  0.597
2004 Figueiredo L, Klunker D, Ang D, Naylor DJ, Kerner MJ, Georgopoulos C, Hartl FU, Hayer-Hartl M. Functional characterization of an archaeal GroEL/GroES chaperonin system: significance of substrate encapsulation. The Journal of Biological Chemistry. 279: 1090-9. PMID 14576149 DOI: 10.1074/jbc.M310914200  0.588
2003 Siegers K, Bölter B, Schwarz JP, Böttcher UM, Guha S, Hartl FU. TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. The Embo Journal. 22: 5230-40. PMID 14517260 DOI: 10.1093/emboj/cdg483  0.615
2003 Hartl FU. Paper of the Year 2002: Award to Cordelia Schiene-Fischer. Biological Chemistry. 384: 1253-4. PMID 14515984 DOI: 10.1515/bchm.2003.384.9.1253  0.366
2003 Rosenhagen MC, Sōti C, Schmidt U, Wochnik GM, Hartl FU, Holsboer F, Young JC, Rein T. The heat shock protein 90-targeting drug cisplatin selectively inhibits steroid receptor activation. Molecular Endocrinology (Baltimore, Md.). 17: 1991-2001. PMID 12869591 DOI: 10.1210/Me.2003-0141  0.514
2003 Brychzy A, Rein T, Winklhofer KF, Hartl FU, Young JC, Obermann WM. Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system. The Embo Journal. 22: 3613-23. PMID 12853476 DOI: 10.1093/emboj/cdg362  0.547
2003 Klunker D, Haas B, Hirtreiter A, Figueiredo L, Naylor DJ, Pfeifer G, Müller V, Deppenmeier U, Gottschalk G, Hartl FU, Hayer-Hartl M. Coexistence of group I and group II chaperonins in the archaeon Methanosarcina mazei. The Journal of Biological Chemistry. 278: 33256-67. PMID 12796498 DOI: 10.1074/jbc.M302018200  0.525
2003 Young JC, Hartl FU. A stress sensor for the bacterial periplasm. Cell. 113: 1-2. PMID 12679025 DOI: 10.1016/S0092-8674(03)00192-2  0.456
2003 Young JC, Hoogenraad NJ, Hartl FU. Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell. 112: 41-50. PMID 12526792 DOI: 10.1016/S0092-8674(02)01250-3  0.547
2003 Dou F, Netzer WJ, Tanemura K, Li F, Hartl FU, Takashima A, Gouras GK, Greengard P, Xu H. Chaperones increase association of tau protein with microtubules. Proceedings of the National Academy of Sciences of the United States of America. 100: 721-6. PMID 12522269 DOI: 10.1073/Pnas.242720499  0.537
2003 Schmidt U, Wochnik GM, Rosenhagen MC, Young JC, Hartl FU, Holsboer F, Rein T. Essential role of the unusual DNA-binding motif of BAG-1 for inhibition of the glucocorticoid receptor. The Journal of Biological Chemistry. 278: 4926-31. PMID 12482863 DOI: 10.1074/Jbc.M212000200  0.477
2002 Hartl FU. Paper of the Year 2001: Award to Peter Hacke. Biological Chemistry. 383: 1481. PMID 12452425 DOI: 10.1515/bchm.2002.383.10.1481  0.366
2002 Becker T, Hartl FU, Wieland F. CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes. The Journal of Cell Biology. 158: 1277-85. PMID 12356871 DOI: 10.1083/jcb.200208083  0.506
2002 Young JC, Hartl FU. Chaperones and transcriptional regulation by nuclear receptors. Nature Structural Biology. 9: 640-2. PMID 12198482 DOI: 10.1038/nsb0902-640  0.423
2002 Sakahira H, Breuer P, Hayer-Hartl MK, Hartl FU. Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity. Proceedings of the National Academy of Sciences of the United States of America. 99: 16412-8. PMID 12189209 DOI: 10.1073/pnas.182426899  0.583
2002 Sondermann H, Ho AK, Listenberger LL, Siegers K, Moarefi I, Wente SR, Hartl FU, Young JC. Prediction of novel Bag-1 homologs based on structure/function analysis identifies Snl1p as an Hsp70 co-chaperone in Saccharomyces cerevisiae. The Journal of Biological Chemistry. 277: 33220-7. PMID 12105220 DOI: 10.1074/Jbc.M204624200  0.553
2002 Hartl FU, Hayer-Hartl M. Protein folding. Molecular chaperones in the cytosol: From nascent chain to folded protein Science. 295: 1852-1858. PMID 11884745 DOI: 10.1126/science.1068408  0.621
2002 Barral JM, Hutagalung AH, Brinker A, Hartl FU, Epstein HF. Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin. Science (New York, N.Y.). 295: 669-71. PMID 11809970 DOI: 10.1126/science.1066648  0.565
2001 Stöckel J, Hartl FU. Chaperonin-mediated de novo generation of prion protein aggregates Journal of Molecular Biology. 313: 861-872. PMID 11697909 DOI: 10.1006/jmbi.2001.5085  0.532
2001 Brinker A, Pfeifer G, Kerner MJ, Naylor DJ, Hartl FU, Hayer-Hartl M. Dual function of protein confinement in chaperonin-assisted protein folding Cell. 107: 223-233. PMID 11672529 DOI: 10.1016/S0092-8674(01)00517-7  0.619
2001 Hartl FU. Roger D. Kornberg - Felix Hoppe-Seyler Lecturer 2001 Biological Chemistry. 382: 1101-1102. PMID 11592389 DOI: 10.1515/BC.2001.139  0.367
2001 Naylor DJ, Hartl FU. Contribution of molecular chaperones to protein folding in the cytoplasm of prokaryotic and eukaryotic cells Biochemical Society Symposium. 68: 45-68. PMID 11573347  0.614
2001 Winklhofer KF, Hartl FU, Tatzelt J. A sensitive filter retention assay for the detection of PrPSc and the screening of anti-prion compounds Febs Letters. 503: 41-45. PMID 11513851 DOI: 10.1016/S0014-5793(01)02692-8  0.451
2001 Young JC, Moarefi I, Hartl FU. Hsp90: a specialized but essential protein-folding tool. The Journal of Cell Biology. 154: 267-73. PMID 11470816 DOI: 10.1083/jcb.200104079  0.361
2001 Sittler A, Lurz R, Lueder G, Priller J, Lehrach H, Hayer-Hartl MK, Hartl FU, Wanker EE. Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease. Human Molecular Genetics. 10: 1307-15. PMID 11406612 DOI: 10.1093/Hmg/10.12.1307  0.525
2001 Rosenhagen MC, Young JC, Wochnik GM, Herr AS, Schmidt U, Hartl FU, Holsboer F, Rein T. Synergistic inhibition of the glucocorticoid receptor by radicicol and benzoquinone ansamycins. Biological Chemistry. 382: 499-504. PMID 11347901 DOI: 10.1515/Bc.2001.063  0.52
2001 Sondermann H, Scheufler C, Schneider C, Höhfeld J, Hartl FU, Moarefi I. Structure of a Bag/Hsc70 complex: Convergent functional evolution of Hsp70 nucleotide exchange factors Science. 291: 1553-1557. PMID 11222862 DOI: 10.1126/Science.1057268  0.573
2000 Sondermann H, Becker T, Mayhew M, Wieland F, Hartl FU. Characterization of a receptor for heat shock protein 70 on macrophages and monocytes Biological Chemistry. 381: 1165-1174. PMID 11209751 DOI: 10.1515/Bc.2000.144  0.51
2000 Siegert R, Leroux MR, Scheufler C, Hartl FU, Moarefi I. Structure of the molecular chaperone prefoldin: Unique interaction of multiple coiled coil tentacles with unfolded proteins Cell. 103: 621-632. PMID 11106732  0.602
2000 Fändrich M, Tito MA, Leroux MR, Rostom AA, Hartl FU, Dobson CM, Robinson CV. Observation of the noncovalent assembly and disassembly pathways of the chaperone complex MtGimC by mass spectrometry Proceedings of the National Academy of Sciences of the United States of America. 97: 14151-14155. PMID 11087821 DOI: 10.1073/Pnas.240326597  0.47
2000 Young JC, Hartl FU. Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23. The Embo Journal. 19: 5930-40. PMID 11060043 DOI: 10.1093/emboj/19.21.5930  0.51
2000 Muchowski PJ, Schaffar G, Sittler A, Wanker EE, Hayer-Hartl MK, Hartl FU. Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils. Proceedings of the National Academy of Sciences of the United States of America. 97: 7841-6. PMID 10859365 DOI: 10.1073/Pnas.140202897  0.569
2000 Rostom AA, Fucini P, Benjamin DR, Juenemann R, Nierhaus KH, Hartl FU, Dobson CM, Robinson CV. Detection and selective dissociation of intact ribosomes in a mass spectrometer Proceedings of the National Academy of Sciences of the United States of America. 97: 5185-5190. PMID 10805779 DOI: 10.1073/Pnas.97.10.5185  0.49
2000 Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, Bartunik H, Hartl FU, Moarefi I. Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine Cell. 101: 199-210. PMID 10786835 DOI: 10.1016/S0092-8674(00)80830-2  0.517
2000 Leroux MR, Hartl FU. Protein folding: Versatility of the cytosolic chaperonin TRiC/CCT Current Biology. 10: R260-R264. PMID 10753735 DOI: 10.1016/S0960-9822(00)00432-2  0.59
2000 Buchczyk DP, Briviba K, Hartl FU, Sies H. Responses to peroxynitrite in yeast: glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as a sensitive intracellular target for nitration and enhancement of chaperone expression and ubiquitination. Biological Chemistry. 381: 121-6. PMID 10746743 DOI: 10.1515/BC.2000.017  0.555
2000 Agashe VR, Hartl FU. Roles of molecular chaperones in cytoplasmic protein folding Seminars in Cell and Developmental Biology. 11: 15-25. PMID 10736260 DOI: 10.1006/scdb.1999.0347  0.598
2000 Moroi Y, Mayhew M, Trcka J, Hoe MH, Takechi Y, Hartl FU, Rothman JE, Houghton AN. Induction of cellular immunity by immunization with novel hybrid peptides complexed to heat shock protein 70. Proceedings of the National Academy of Sciences of the United States of America. 97: 3485-90. PMID 10725409 DOI: 10.1073/Pnas.97.7.3485  0.458
1999 Houry WA, Frishman D, Eckerskorn C, Lottspeich F, Hartl FU. Identification of in vivo substrates of the chaperonin GroEL. Nature. 402: 147-54. PMID 10647006 DOI: 10.1038/45977  0.598
1999 Leroux MR, Fändrich M, Klunker D, Siegers K, Lupas AN, Brown JR, Schiebel E, Dobson CM, Hartl FU. MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin. The Embo Journal. 18: 6730-43. PMID 10581246 DOI: 10.1093/Emboj/18.23.6730  0.615
1999 Hayer-Hartl MK, Ewalt KL, Hartl FU. On the role of symmetrical and asymmetrical chaperonin complexes in assisted protein folding. Biological Chemistry. 380: 531-40. PMID 10384959 DOI: 10.1515/BC.1999.068  0.565
1999 Teter SA, Houry WA, Ang D, Tradler T, Rockabrand D, Fischer G, Blum P, Georgopoulos C, Hartl FU. Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains. Cell. 97: 755-65. PMID 10380927 DOI: 10.1016/S0092-8674(00)80787-4  0.56
1999 Ellis RJ, Hartl FU. Principles of protein folding in the cellular environment. Current Opinion in Structural Biology. 9: 102-10. PMID 10047582 DOI: 10.1016/S0959-440X(99)80013-X  0.596
1999 Siegers K, Waldmann T, Leroux MR, Grein K, Shevchenko A, Schiebel E, Hartl FU. Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. The Embo Journal. 18: 75-84. PMID 9878052 DOI: 10.1093/Emboj/18.1.75  0.637
1998 Obermann WM, Sondermann H, Russo AA, Pavletich NP, Hartl FU. In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. The Journal of Cell Biology. 143: 901-10. PMID 9817749 DOI: 10.1083/Jcb.143.4.901  0.569
1998 Weber F, Keppel F, Georgopoulos C, Hayer-Hartl MK, Hartl FU. The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding. Nature Structural Biology. 5: 977-85. PMID 9808043 DOI: 10.1038/2952  0.333
1998 Benjamin DR, Robinson CV, Hendrick JP, Hartl FU, Dobson CM. Mass spectrometry of ribosomes and ribosomal subunits. Proceedings of the National Academy of Sciences of the United States of America. 95: 7391-5. PMID 9636159 DOI: 10.1073/pnas.95.13.7391  0.552
1998 Heyrovská N, Frydman J, Höhfeld J, Hartl FU. Directionality of polypeptide transfer in the mitochondrial pathway of chaperone-mediated protein folding Biological Chemistry. 379: 301-309. PMID 9563826  0.653
1998 Netzer WJ, Hartl FU. Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms. Trends in Biochemical Sciences. 23: 68-73. PMID 9538692 DOI: 10.1016/s0968-0004(97)01171-7  0.412
1997 Young JC, Schneider C, Hartl FU. In vitro evidence that hsp90 contains two independent chaperone sites. Febs Letters. 418: 139-43. PMID 9414113 DOI: 10.1016/S0014-5793(97)01363-X  0.482
1997 Ewalt KL, Hendrick JP, Houry WA, Hartl FU. In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell. 90: 491-500. PMID 9267029 DOI: 10.1016/S0092-8674(00)80509-7  0.609
1997 Netzer WJ, Hartl FU. Recombination of protein domains facilitated by co-translational folding in eukaryotes. Nature. 388: 343-9. PMID 9237751 DOI: 10.1038/41024  0.308
1997 Stebbins CE, Russo AA, Schneider C, Rosen N, Hartl FU, Pavletich NP. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell. 89: 239-50. PMID 9108479 DOI: 10.1016/S0092-8674(00)80203-2  0.3
1997 Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science (New York, N.Y.). 276: 431-5. PMID 9103205 DOI: 10.1126/Science.276.5311.431  0.302
1997 Martin J, Hartl FU. The effect of macromolecular crowding on chaperonin-mediated protein folding. Proceedings of the National Academy of Sciences of the United States of America. 94: 1107-12. PMID 9037014 DOI: 10.1073/pnas.94.4.1107  0.586
1997 Martin J, Hartl FU. Chaperone-assisted protein folding. Current Opinion in Structural Biology. 7: 41-52. PMID 9032064 DOI: 10.1016/S0959-440X(97)80006-1  0.598
1997 Gross M, Robinson CV, Mayhew M, Hartl FU, Radford SE. Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling. Protein Science : a Publication of the Protein Society. 5: 2506-13. PMID 8976559 DOI: 10.1002/pro.5560051213  0.309
1997 Schneider C, Sepp-Lorenzino L, Nimmesgern E, Ouerfelli O, Danishefsky S, Rosen N, Hartl FU. Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90. Proceedings of the National Academy of Sciences of the United States of America. 93: 14536-41. PMID 8962087 DOI: 10.1073/pnas.93.25.14536  0.574
1997 Hayer-Hartl MK, Weber F, Hartl FU. Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis. The Embo Journal. 15: 6111-21. PMID 8947033  0.358
1996 Schneider C, Hartl FU. Hats off to the tricorn protease. Science (New York, N.Y.). 274: 1323-4. PMID 8966603 DOI: 10.1126/science.274.5291.1323  0.434
1996 Minami Y, Höhfeld J, Ohtsuka K, Hartl FU. Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40. The Journal of Biological Chemistry. 271: 19617-24. PMID 8702658 DOI: 10.1074/jbc.271.32.19617  0.324
1996 Hartl FU. Molecular chaperones in cellular protein folding. Nature. 381: 571-9. PMID 8637592 DOI: 10.1038/381571a0  0.394
1996 Frydman J, Hartl FU. Principles of chaperone-assisted protein folding: Differences between in vitro and in vivo mechanisms Science. 272: 1497-1502. PMID 8633246 DOI: 10.1126/Science.272.5267.1497  0.746
1996 Szabo A, Korszun R, Hartl FU, Flanagan J. A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates. The Embo Journal. 15: 408-17. PMID 8617216  0.342
1996 Georgellis D, Sohlberg B, Hartl FU, von Gabain A. Identification of GroEL as a constituent of an mRNA-protection complex in Escherichia coli. Molecular Microbiology. 16: 1259-68. PMID 8577258 DOI: 10.1111/j.1365-2958.1995.tb02347.x  0.475
1996 Ellis RJ, Hartl FU. Protein folding in the cell: competing models of chaperonin function. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 10: 20-6. PMID 8566542 DOI: 10.1096/fasebj.10.1.8566542  0.602
1996 Mayhew M, da Silva AC, Martin J, Erdjument-Bromage H, Tempst P, Hartl FU. Protein folding in the central cavity of the GroEL-GroES chaperonin complex. Nature. 379: 420-6. PMID 8559246 DOI: 10.1038/379420A0  0.35
1996 Mayhew M, Hartl FU. Lord of the rings: GroES structure. Science (New York, N.Y.). 271: 161-2. PMID 8539614 DOI: 10.1126/science.271.5246.161  0.407
1996 Hendrick JP, Hartl FU. The role of molecular chaperones in protein folding. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 9: 1559-69. PMID 8529835 DOI: 10.1096/fasebj.9.15.8529835  0.637
1995 Höhfeld J, Hartl FU. Post-translational protein import and folding. Current Opinion in Cell Biology. 6: 499-509. PMID 7986525 DOI: 10.1016/0955-0674(94)90068-X  0.61
1995 Hartl FU, Martin J. Molecular chaperones in cellular protein folding. Current Opinion in Structural Biology. 5: 92-102. PMID 7773752 DOI: 10.1016/0959-440X(95)80014-R  0.615
1995 Hartl FU. Principles of chaperone-mediated protein folding. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 348: 107-12. PMID 7770479 DOI: 10.1098/rstb.1995.0051  0.403
1995 Hayer-Hartl MK, Martin J, Hartl FU. Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding. Science (New York, N.Y.). 269: 836-41. PMID 7638601 DOI: 10.1126/science.7638601  0.57
1995 Engel A, Hayer-Hartl MK, Goldie KN, Pfeifer G, Hegerl R, Müller S, da Silva AC, Baumeister W, Hartl FU. Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes. Science (New York, N.Y.). 269: 832-6. PMID 7638600 DOI: 10.1126/Science.7638600  0.579
1995 Höhfeld J, Minami Y, Hartl FU. Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell. 83: 589-98. PMID 7585962 DOI: 10.1016/0092-8674(95)90099-3  0.352
1994 Li WZ, Lin P, Frydman J, Boal TR, Cardillo TS, Richard LM, Toth D, Lichtman MA, Hartl FU, Sherman F, Segel GB. Tcp20, a subunit of the eukaryotic TRiC chaperonin from humans and yeast Journal of Biological Chemistry. 269: 18616-18622. PMID 8034610  0.62
1994 Frydman J, Nimmesgern E, Ohtsuka K, Hartl FU. Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones Nature. 370: 111-117. PMID 8022479 DOI: 10.1038/370111A0  0.626
1994 Martin J, Hartl FU. Molecular chaperones in cellular protein folding. Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. 16: 689-92. PMID 7980496 DOI: 10.1002/bies.950160916  0.369
1994 Szabo A, Langer T, Schröder H, Flanagan J, Bukau B, Hartl FU. The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system - DnaK, DnaJ, and GrpE Proceedings of the National Academy of Sciences of the United States of America. 91: 10345-10349. PMID 7937953 DOI: 10.1073/Pnas.91.22.10345  0.589
1994 Hartl FU. Protein folding. Secrets of a double-doughnut. Nature. 371: 557-9. PMID 7935786 DOI: 10.1038/371557a0  0.346
1994 Höhfeld J, Hartl FU. Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria. The Journal of Cell Biology. 126: 305-15. PMID 7913473 DOI: 10.1083/jcb.126.2.305  0.622
1994 Hartl FU, Hlodan R, Langer T. Molecular chaperones in protein folding: the art of avoiding sticky situations. Trends in Biochemical Sciences. 19: 20-5. PMID 7908149 DOI: 10.1016/0968-0004(94)90169-4  0.41
1993 Hendrick JP, Langer T, Davis TA, Hartl FU, Wiedmann M. Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides. Proceedings of the National Academy of Sciences of the United States of America. 90: 10216-20. PMID 8234279 DOI: 10.1073/Pnas.90.21.10216  0.612
1993 Nimmesgern E, Hartl FU. ATP-dependent protein refolding activity in reticulocyte lysate. Evidence for the participation of different chaperone components. Febs Letters. 331: 25-30. PMID 8104824 DOI: 10.1016/0014-5793(93)80290-B  0.601
1993 Hendrick JP, Hartl FU. Molecular chaperone functions of heat-shock proteins. Annual Review of Biochemistry. 62: 349-84. PMID 8102520 DOI: 10.1146/Annurev.Bi.62.070193.002025  0.596
1993 Evers ME, Huhse B, Titorenko VI, Kunau WH, Hartl FU, Harder W, Veenhuis M. Affinity purification of molecular chaperones of the yeast Hansenula polymorpha using immobilized denatured alcohol oxidase. Febs Letters. 321: 32-6. PMID 8096822 DOI: 10.1016/0014-5793(93)80615-2  0.583
1993 Hayer-Hartl MK, Hartl FU. A comment on: 'The aromatic amino acid content of the bacterial chaperone protein groEL (cpn60): evidence for the presence of a single tryptophan', by N.C. Price, S.M. Kelly, S. Wood and A. auf der Mauer (1991) FEBS Lett. 292, 9-12. Febs Letters. 320: 83-4; discussion 85. PMID 8096465 DOI: 10.1016/0014-5793(93)81663-K  0.484
1993 Sohlberg B, Lundberg U, Hartl FU, von Gabain A. Functional interaction of heat shock protein GroEL with an RNase E-like activity in Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 90: 277-81. PMID 8093559 DOI: 10.1073/pnas.90.1.277  0.499
1993 Martin J, Geromanos S, Tempst P, Hartl FU. Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES. Nature. 366: 279-82. PMID 7901771 DOI: 10.1038/366279a0  0.535
1993 Martin J, Mayhew M, Langer T, Hartl FU. The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding. Nature. 366: 228-33. PMID 7901770 DOI: 10.1038/366228A0  0.378
1993 Schroder H, Langer T, Hartl FU, Bukau B. DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage Embo Journal. 12: 4137-4144. PMID 7900997 DOI: 10.1002/J.1460-2075.1993.Tb06097.X  0.319
1993 Langer T, Pfeifer G, Martin J, Baumeister W, Hartl FU. Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity. The Embo Journal. 11: 4757-65. PMID 1361169 DOI: 10.1002/j.1460-2075.1992.tb05581.x  0.355
1992 Hartl FU, Martin J, Neupert W. Protein folding in the cell: the role of molecular chaperones Hsp70 and Hsp60. Annual Review of Biophysics and Biomolecular Structure. 21: 293-322. PMID 1525471 DOI: 10.1146/annurev.bb.21.060192.001453  0.686
1992 West AH, Clark DJ, Martin J, Neupert W, Hartl FU, Horwich AL. Two related genes encoding extremely hydrophobic proteins suppress a lethal mutation in the yeast mitochondrial processing enhancing protein. The Journal of Biological Chemistry. 267: 24625-33. PMID 1447206  0.675
1992 Frydman J, Nimmesgern E, Erdjument-Bromage H, Wall JS, Tempst P, Hartl FU. Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits Embo Journal. 11: 4767-4778. PMID 1361170 DOI: 10.1002/J.1460-2075.1992.Tb05582.X  0.67
1992 Martin J, Horwich AL, Hartl FU. Prevention of protein denaturation under heat stress by the chaperonin Hsp60. Science (New York, N.Y.). 258: 995-8. PMID 1359644 DOI: 10.1126/Science.1359644  0.565
1992 Evers ME, Langer T, Harder W, Hartl FU, Veenhuis M. Formation and quantification of protein complexes between peroxisomal alcohol oxidase and GroEL. Febs Letters. 305: 51-4. PMID 1353025 DOI: 10.1016/0014-5793(92)80653-X  0.556
1992 Langer T, Lu C, Echols H, Flanagan J, Hayer MK, Hartl FU. Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding Nature. 356: 683-689. PMID 1349157 DOI: 10.1038/356683A0  0.389
1992 Koll H, Guiard B, Rassow J, Ostermann J, Horwich AL, Neupert W, Hartl FU. Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space. Cell. 68: 1163-75. PMID 1347713 DOI: 10.1016/0092-8674(92)90086-R  0.673
1991 Trent JD, Nimmesgern E, Wall JS, Hartl FU, Horwich AL. A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1. Nature. 354: 490-3. PMID 1836250 DOI: 10.1038/354490A0  0.606
1991 Wickner W, Driessen AJ, Hartl FU. The enzymology of protein translocation across the Escherichia coli plasma membrane. Annual Review of Biochemistry. 60: 101-24. PMID 1831965 DOI: 10.1146/Annurev.Bi.60.070191.000533  0.691
1991 Schiebel E, Driessen AJ, Hartl FU, Wickner W. Delta mu H+ and ATP function at different steps of the catalytic cycle of preprotein translocase. Cell. 64: 927-39. PMID 1825804 DOI: 10.1016/0092-8674(91)90317-R  0.717
1991 Hartl FU. Heat shock proteins in protein folding and membrane translocation. Seminars in Immunology. 3: 5-16. PMID 1680013  0.416
1991 Martin J, Langer T, Boteva R, Schramel A, Horwich AL, Hartl FU. Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature. 352: 36-42. PMID 1676490 DOI: 10.1038/352036A0  0.587
1990 Hartl FU, Neupert W. Protein sorting to mitochondria: evolutionary conservations of folding and assembly. Science (New York, N.Y.). 247: 930-8. PMID 2406905 DOI: 10.1126/Science.2406905  0.671
1990 Pfanner N, Ostermann J, Rassow J, Hartl FU, Neupert W. Stress proteins and mitochondrial protein import. Antonie Van Leeuwenhoek. 58: 191-3. PMID 2256680 DOI: 10.1007/Bf00548932  0.662
1990 Neupert W, Hartl FU, Craig EA, Pfanner N. How do polypeptides cross the mitochondrial membranes? Cell. 63: 447-50. PMID 2225059 DOI: 10.1016/0092-8674(90)90437-J  0.606
1990 Hartl FU, Lecker S, Schiebel E, Hendrick JP, Wickner W. The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane. Cell. 63: 269-79. PMID 2170023 DOI: 10.1016/0092-8674(90)90160-G  0.74
1990 Rassow J, Hartl FU, Guiard B, Pfanner N, Neupert W. Polypeptides traverse the mitochondrial envelope in an extended state. Febs Letters. 275: 190-4. PMID 2148157 DOI: 10.1016/0014-5793(90)81469-5  0.643
1990 Mahlke K, Pfanner N, Martin J, Horwich AL, Hartl FU, Neupert W. Sorting pathways of mitochondrial inner membrane proteins. European Journal of Biochemistry / Febs. 192: 551-5. PMID 2145157 DOI: 10.1111/J.1432-1033.1990.Tb19260.X  0.679
1990 Pfanner N, Rassow J, Guiard B, Söllner T, Hartl FU, Neupert W. Energy requirements for unfolding and membrane translocation of precursor proteins during import into mitochondria. The Journal of Biological Chemistry. 265: 16324-9. PMID 2144529  0.67
1990 Cheng MY, Hartl FU, Horwich AL. The mitochondrial chaperonin hsp60 is required for its own assembly. Nature. 348: 455-8. PMID 1978929 DOI: 10.1038/348455a0  0.6
1990 Horwich AL, Neupert W, Hartl FU. Protein-catalysed protein folding. Trends in Biotechnology. 8: 126-31. PMID 1369433 DOI: 10.1016/0167-7799(90)90153-O  0.676
1989 Just WW, Gorgas K, Hartl FU, Heinemann P, Salzer M, Schimassek H. Biochemical effects and zonal heterogeneity of peroxisome proliferation induced by perfluorocarboxylic acids in rat liver. Hepatology (Baltimore, Md.). 9: 570-81. PMID 2925163 DOI: 10.1002/Hep.1840090411  0.432
1989 Cheng MY, Hartl FU, Martin J, Pollock RA, Kalousek F, Neupert W, Hallberg EM, Hallberg RL, Horwich AL. Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature. 337: 620-5. PMID 2645524 DOI: 10.1038/337620A0  0.699
1989 Hartl FU, Pfanner N, Nicholson DW, Neupert W. Mitochondrial protein import. Biochimica Et Biophysica Acta. 988: 1-45. PMID 2642391 DOI: 10.5282/Ubm/Epub.7536  0.663
1989 Hartl FU, Neupert W. Import of proteins into the various submitochondrial compartments. Journal of Cell Science. Supplement. 11: 187-98. PMID 2559090 DOI: 10.1242/Jcs.1989.Supplement_11.15  0.647
1989 Rassow J, Guiard B, Wienhues U, Herzog V, Hartl FU, Neupert W. Translocation arrest by reversible folding of a precursor protein imported into mitochondria. A means to quantitate translocation contact sites. The Journal of Cell Biology. 109: 1421-8. PMID 2529262 DOI: 10.1083/Jcb.109.4.1421  0.649
1989 Ostermann J, Horwich AL, Neupert W, Hartl FU. Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Nature. 341: 125-30. PMID 2528694 DOI: 10.1038/341125A0  0.7
1988 Pollock RA, Hartl FU, Cheng MY, Ostermann J, Horwich A, Neupert W. The processing peptidase of yeast mitochondria: the two co-operating components MPP and PEP are structurally related. The Embo Journal. 7: 3493-500. PMID 3061797 DOI: 10.1002/J.1460-2075.1988.Tb03225.X  0.674
1988 Pfanner N, Hartl FU, Neupert W. Import of proteins into mitochondria: a multi-step process. European Journal of Biochemistry / Febs. 175: 205-12. PMID 3042397 DOI: 10.1111/J.1432-1033.1988.Tb14185.X  0.669
1988 Tropschug M, Nicholson DW, Hartl FU, Köhler H, Pfanner N, Wachter E, Neupert W. Cyclosporin A-binding protein (cyclophilin) of Neurospora crassa. One gene codes for both the cytosolic and mitochondrial forms. The Journal of Biological Chemistry. 263: 14433-40. PMID 2971658  0.645
1988 Hawlitschek G, Schneider H, Schmidt B, Tropschug M, Hartl FU, Neupert W. Mitochondrial protein import: identification of processing peptidase and of PEP, a processing enhancing protein. Cell. 53: 795-806. PMID 2967109 DOI: 10.1016/0092-8674(88)90096-7  0.656
1987 Hartl FU, Just WW. Integral membrane polypeptides of rat liver peroxisomes: topology and response to different metabolic states. Archives of Biochemistry and Biophysics. 255: 109-19. PMID 3592654 DOI: 10.1016/0003-9861(87)90300-6  0.483
1987 Hartl FU, Pfanner N, Neupert W. Translocation intermediates on the import pathway of proteins into mitochondria. Biochemical Society Transactions. 15: 95-7. PMID 3030846 DOI: 10.1042/Bst0150095  0.647
1987 Pfanner N, Hartl FU, Guiard B, Neupert W. Mitochondrial precursor proteins are imported through a hydrophilic membrane environment. European Journal of Biochemistry / Febs. 169: 289-93. PMID 2891506 DOI: 10.1111/J.1432-1033.1987.Tb13610.X  0.627
1987 Hartl FU, Ostermann J, Guiard B, Neupert W. Successive translocation into and out of the mitochondrial matrix: targeting of proteins to the intermembrane space by a bipartite signal peptide. Cell. 51: 1027-37. PMID 2826012 DOI: 10.1016/0092-8674(87)90589-7  0.622
1986 Hartl FU, Schmidt B, Wachter E, Weiss H, Neupert W. Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c reductase. Cell. 47: 939-51. PMID 3022944 DOI: 10.1016/0092-8674(86)90809-3  0.649
1985 Hartl FU, Just WW, Köster A, Schimassek H. Improved isolation and purification of rat liver peroxisomes by combined rate zonal and equilibrium density centrifugation. Archives of Biochemistry and Biophysics. 237: 124-34. PMID 3970541 DOI: 10.1016/0003-9861(85)90261-9  0.467
1984 Just WW, Hartl FU. Rat liver peroxisomes, II. Stimulation of peroxisomal fatty-acid beta-oxidation by thyroid hormones. Hoppe-Seyler's Zeitschrift Fur Physiologische Chemie. 364: 1541-7. PMID 6662502 DOI: 10.1515/bchm2.1983.364.2.1541  0.44
1982 Just WW, Hartl FU, Schimassek H. Rat liver peroxisomes. I. New peroxisome population induced by thyroid hormones in the liver of male rats. European Journal of Cell Biology. 26: 249-54. PMID 6121707  0.417
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