| 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 |
0.396 |
|
| 2020 |
Herrmann JM, Hartl FU, Pfanner N. Mitochondria and friends. Biological Chemistry. PMID 32383685 DOI: 10.1515/Hsz-2020-0151 |
0.461 |
|
| 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 |
0.575 |
|
| 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 |
0.655 |
|
| 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 |
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| 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 RÃo 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 |
0.571 |
|
| 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 |
0.57 |
|
| 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, SÅti 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 |
0.505 |
|
| 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 |
0.651 |
|
| 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 |
0.402 |
|
| 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 |
0.618 |
|
| 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 |
0.624 |
|
| 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 |
0.582 |
|
| 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 |
0.668 |
|
| 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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