Franz-Ulrich Hartl - Publications

Cellular Biochemistry Max Planck Institute of Biochemistry 
Protein folding

177 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
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  0.36
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  0.6
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  0.6
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  0.36
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  0.6
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  0.44
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  0.36
2016 Neudegger T, Verghese J, Hayer-Hartl M, Hartl FU, Bracher A. Structure of human heat-shock transcription factor 1 in complex with DNA Nature Structural and Molecular Biology. 23: 140-146. DOI: 10.1038/nsmb.3149  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.48
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
2015 Bracher A, Sharma A, Starling-Windhof A, Hartl FU, Hayer-Hartl M. Degradation of potent Rubisco inhibitor by selective sugar phosphatase Nature Plants. 1. DOI: 10.1038/nplants.2014.2  0.72
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  0.72
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  0.6
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  0.48
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  0.36
2014 Vincenz L, Hartl FU. Sugarcoating ER Stress. Cell. 156: 1125-7. PMID 24630714 DOI: 10.1016/j.cell.2014.02.035  0.48
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  0.48
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  0.48
2013 Hartl FU, Hayer-Hartl M. The first chaperonin. Nature Reviews. Molecular Cell Biology. 14: 611. PMID 24061226 DOI: 10.1038/nrm3665  0.48
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  0.48
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  0.48
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  0.6
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
2010 Chakraborty K, Georgescauld F, Hayer-Hartl M, Hartl FU. Role of Molecular Chaperones in Protein Folding Protein Misfolding Diseases: Current and Emerging Principles and Therapies. 47-72. DOI: 10.1002/9780470572702.ch3  0.48
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  0.48
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
2008 Siegers K, Bracher A, Hartl FU. Structure and Function of GimC/Prefoldin Protein Folding Handbook. 2: 756-767. DOI: 10.1002/9783527619498.ch55  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.48
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
2004 Hartl FU. Wolfgang Baumeister--Felix Hoppe-Seyler Lecturer 2004. Biological Chemistry. 385: 863. PMID 15551858 DOI: 10.1515/BC.2004.112  0.72
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  0.72
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  0.72
2004 Etchells SA, Hartl FU. The dynamic tunnel. Nature Structural & Molecular Biology. 11: 391-2. PMID 15114338 DOI: 10.1038/nsmb0504-391  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
2003 Young JC, Barral JM, Ulrich Hartl F. More than folding: localized functions of cytosolic chaperones. Trends in Biochemical Sciences. 28: 541-7. PMID 14559183 DOI: 10.1016/j.tibs.2003.08.009  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
2002 Hartl FU. Kai Simons - Felix Hoppe-Seyler lecturer 2002 Biological Chemistry. 383: 1473-1474. DOI: 10.1515/BC.2002.168  0.72
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  0.72
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  0.72
2001 Hartl FU. Roger D. Kornberg - Felix Hoppe-Seyler Lecturer 2001 Biological Chemistry. 382: 1101-1102. PMID 11592389 DOI: 10.1515/BC.2001.139  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
2000 Ellis RJ, Hartl FU. Folding and binding. Problems with proteins Current Opinion in Structural Biology. 10: 13-15. PMID 10766516 DOI: 10.1016/S0959-440X(99)90003-9  0.72
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  0.72
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  0.72
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  0.72
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  0.72
2000 Langer D, Mettenleiter M, Hartl F, Frohlich C. Imaging laser scanners for 3-D modeling and surveying applications Proceedings - Ieee International Conference On Robotics and Automation. 1: 116-121.  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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/  1
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  0.72
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  0.72
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  0.72
1992 Horwich AL, Caplan S, Wall JS, Hartl FU. Chapter 26 Chaperonin-mediated protein folding New Comprehensive Biochemistry. 22: 329-337. DOI: 10.1016/S0167-7306(08)60103-9  0.48
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  0.72
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  1
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  0.72
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  0.72
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  1
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  1
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  0.72
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  0.72
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  1
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  0.72
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  1
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  0.72
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  0.72
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  0.72
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  0.72
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  1
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  1
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  0.72
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  0.72
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  0.64
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  0.64
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