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Ursula H. Jakob - Publications

Affiliations: 
University of Michigan, Ann Arbor, Ann Arbor, MI 
Area:
Molecular Biology, Microbiology Biology
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102 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
2024 Guan J, Jakob U. The Protein Scaffolding Functions of Polyphosphate. Journal of Molecular Biology. 168504. PMID 38423453 DOI: 10.1016/j.jmb.2024.168504  0.343
2022 Ulrich K, Farkas Á, Chan O, Katamanin O, Schwappach B, Jakob U. From guide to guard-activation mechanism of the stress-sensing chaperone Get3. Molecular Cell. PMID 35839781 DOI: 10.1016/j.molcel.2022.06.015  0.445
2022 Cable J, Weber-Ban E, Clausen T, Walters KJ, Sharon M, Finley DJ, Gu Y, Hanna J, Feng Y, Martens S, Simonsen A, Hansen M, Zhang H, Goodwin JM, Reggio A, ... ... Jakob U, et al. Targeted protein degradation: from small molecules to complex organelles-a Keystone Symposia report. Annals of the New York Academy of Sciences. PMID 35000205 DOI: 10.1111/nyas.14745  0.596
2020 Ulrich K, Schwappach B, Jakob U. Thiol-based switching mechanisms of stress-sensing chaperones. Biological Chemistry. 402: 239-252. PMID 32990643 DOI: 10.1515/hsz-2020-0262  0.405
2020 Becker SH, Ulrich K, Dhabaria A, Ueberheide B, Beavers W, Skaar EP, Iyer LM, Aravind L, Jakob U, Darwin KH. Mycobacterium tuberculosis Rv0991c Is a Redox-Regulated Molecular Chaperone. Mbio. 11. PMID 32843553 DOI: 10.1128/Mbio.01545-20  0.546
2020 Beaufay F, Quarles E, Franz A, Katamanin O, Wholey W, Jakob U. Polyphosphate Functions In Vivo as an Iron Chelator and Fenton Reaction Inhibitor. Mbio. 11. PMID 32723918 DOI: 10.1128/Mbio.01017-20  0.641
2019 Bazopoulou D, Knoefler D, Zheng Y, Ulrich K, Oleson BJ, Xie L, Kim M, Kaufmann A, Lee YT, Dou Y, Chen Y, Quan S, Jakob U. Developmental ROS individualizes organismal stress resistance and lifespan. Nature. PMID 31801997 DOI: 10.1038/S41586-019-1814-Y  0.381
2019 Moayed F, Bezrukavnikov S, Naqvi MM, Groitl B, Cremers CM, Kramer G, Ghosh K, Jakob U, Tans SJ. The Anti-Aggregation Holdase Hsp33 Promotes the Formation of Folded Protein Structures. Biophysical Journal. PMID 31757359 DOI: 10.1016/J.Bpj.2019.10.040  0.425
2019 Currier RB, Ulrich K, Leroux AE, Dirdjaja N, Deambrosi M, Bonilla M, Ahmed YL, Adrian L, Antelmann H, Jakob U, Comini MA, Krauth-Siegel RL. An essential thioredoxin-type protein of Trypanosoma brucei acts as redox-regulated mitochondrial chaperone. Plos Pathogens. 15: e1008065. PMID 31557263 DOI: 10.1371/Journal.Ppat.1008065  0.512
2019 Krewing M, Stepanek JJ, Cremers C, Lackmann JW, Schubert B, Müller A, Awakowicz P, Leichert LIO, Jakob U, Bandow JE. The molecular chaperone Hsp33 is activated by atmospheric-pressure plasma protecting proteins from aggregation. Journal of the Royal Society, Interface. 16: 20180966. PMID 31213177 DOI: 10.1098/Rsif.2018.0966  0.389
2019 Ulrich K, Jakob U. The role of thiols in antioxidant systems. Free Radical Biology and Medicine. 140: 14-27. PMID 31201851 DOI: 10.1016/J.Freeradbiomed.2019.05.035  0.458
2019 Teixeira F, Tse E, Castro H, Makepeace KAT, Meinen BA, Borchers CH, Poole LB, Bardwell JC, Tomás AM, Southworth DR, Jakob U. Chaperone activation and client binding of a 2-cysteine peroxiredoxin. Nature Communications. 10: 659. PMID 30737390 DOI: 10.2210/Pdb6E0G/Pdb  0.49
2019 Lempart J, Jakob U. Role of Polyphosphate in Amyloidogenic Processes. Cold Spring Harbor Perspectives in Biology. 11. PMID 30617049 DOI: 10.1101/Cshperspect.A034041  0.349
2018 Xie L, Jakob U. Inorganic polyphosphate, a multifunctional polyanionic protein scaffold. The Journal of Biological Chemistry. PMID 30425096 DOI: 10.1074/Jbc.Rev118.002808  0.438
2018 Yoo N, Dogra S, Meinen BA, Tse E, Haefliger J, Southworth DR, Gray MJ, Dahl JU, Jakob U. Polyphosphate Stabilizes Protein Unfolding Intermediates as Soluble Amyloid-like Oligomers. Journal of Molecular Biology. PMID 30130556 DOI: 10.1016/J.Jmb.2018.08.016  0.462
2018 Alberti S, Jakob U. Phase shifts in protein folding space: links to stress adaptation and disease. Molecular Biology of the Cell. 29: 695-695. PMID 29535178 DOI: 10.1091/Mbc.E17-11-0685  0.36
2018 Reichmann D, Voth W, Jakob U. Maintaining a Healthy Proteome during Oxidative Stress Molecular Cell. 69: 203-213. PMID 29351842 DOI: 10.1016/J.Molcel.2017.12.021  0.532
2017 Voth W, Jakob U. Stress-Activated Chaperones: A First Line of Defense. Trends in Biochemical Sciences. 42: 899-913. PMID 28893460 DOI: 10.1016/J.Tibs.2017.08.006  0.459
2017 Groitl B, Dahl JU, Schroeder JW, Jakob U. Pseudomonas aeruginosa defense systems against microbicidal oxidants. Molecular Microbiology. PMID 28795780 DOI: 10.1111/Mmi.13768  0.422
2017 Dahl JU, Gray MJ, Bazopoulou D, Beaufay F, Lempart J, Koenigsknecht MJ, Wang Y, Baker JR, Hasler WL, Young VB, Sun D, Jakob U. The anti-inflammatory drug mesalamine targets bacterial polyphosphate accumulation. Nature Microbiology. 2: 16267. PMID 28112760 DOI: 10.1038/Nmicrobiol.2016.267  0.349
2016 Dahl JU, Koldewey P, Bardwell JC, Jakob U. Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo. Journal of Visualized Experiments : Jove. PMID 27805614 DOI: 10.3791/54527  0.491
2016 Cremers CM, Knoefler D, Gates S, Martin N, Dahl JU, Lempart J, Xie L, Chapman MR, Galvan V, Southworth DR, Jakob U. Polyphosphate: A Conserved Modifier of Amyloidogenic Processes. Molecular Cell. PMID 27570072 DOI: 10.1016/J.Molcel.2016.07.016  0.317
2016 Docter BE, Horowitz S, Gray MJ, Jakob U, Bardwell JC. Do nucleic acids moonlight as molecular chaperones? Nucleic Acids Research. PMID 27105849 DOI: 10.1093/Nar/Gkw291  0.386
2016 Groitl B, Horowitz S, Makepeace KA, Petrotchenko EV, Borchers CH, Reichmann D, Bardwell JC, Jakob U. Protein unfolding as a switch from self-recognition to high-affinity client binding. Nature Communications. 7: 10357. PMID 26787517 DOI: 10.1038/Ncomms10357  0.438
2015 Kim H, An S, Ro SH, Teixeira F, Jin Park G, Kim C, Cho CS, Kim JS, Jakob U, Hee Lee J, Cho US. Janus-faced Sestrin2 controls ROS and mTOR signalling through two separate functional domains. Nature Communications. 6: 10025. PMID 26612684 DOI: 10.1038/Ncomms10025  0.391
2015 Gray MJ, Li Y, Leichert LI, Xu Z, Jakob U. Does the Transcription Factor NemR Use a Regulatory Sulfenamide Bond to Sense Bleach? Antioxidants & Redox Signaling. PMID 25867078 DOI: 10.1089/Ars.2015.6346  0.427
2015 Dahl JU, Gray MJ, Jakob U. Protein quality control under oxidative stress conditions. Journal of Molecular Biology. 427: 1549-63. PMID 25698115 DOI: 10.1016/J.Jmb.2015.02.014  0.511
2015 Teixeira F, Castro H, Cruz T, Tse E, Koldewey P, Southworth DR, Tomás AM, Jakob U. Mitochondrial peroxiredoxin functions as crucial chaperone reservoir in Leishmania infantum. Proceedings of the National Academy of Sciences of the United States of America. 112: E616-24. PMID 25646478 DOI: 10.1073/Pnas.1419682112  0.475
2015 Gray MJ, Jakob U. Oxidative stress protection by polyphosphate--new roles for an old player. Current Opinion in Microbiology. 24: 1-6. PMID 25589044 DOI: 10.1016/J.Mib.2014.12.004  0.468
2015 Dahl JU, Koldewey P, Salmon L, Horowitz S, Bardwell JC, Jakob U. HdeB functions as an acid-protective chaperone in bacteria. The Journal of Biological Chemistry. 290: 65-75. PMID 25391835 DOI: 10.1074/Jbc.M114.612986  0.35
2014 Voth W, Schick M, Gates S, Li S, Vilardi F, Gostimskaya I, Southworth DR, Schwappach B, Jakob U. The protein targeting factor Get3 functions as ATP-independent chaperone under oxidative stress conditions. Molecular Cell. 56: 116-27. PMID 25242142 DOI: 10.1016/J.Molcel.2014.08.017  0.52
2014 Knoefler D, Leichert LI, Thamsen M, Cremers CM, Reichmann D, Gray MJ, Wholey WY, Jakob U. About the dangers, costs and benefits of living an aerobic lifestyle. Biochemical Society Transactions. 42: 917-21. PMID 25109979 DOI: 10.1042/Bst20140108  0.464
2014 Cremers CM, Knoefler D, Vitvitsky V, Banerjee R, Jakob U. Bile salts act as effective protein-unfolding agents and instigators of disulfide stress in vivo. Proceedings of the National Academy of Sciences of the United States of America. 111: E1610-9. PMID 24706920 DOI: 10.1073/Pnas.1401941111  0.497
2014 Groitl B, Jakob U. Thiol-based redox switches. Biochimica Et Biophysica Acta. 1844: 1335-1343. PMID 24657586 DOI: 10.1016/J.Bbapap.2014.03.007  0.466
2014 Gray MJ, Wholey WY, Wagner NO, Cremers CM, Mueller-Schickert A, Hock NT, Krieger AG, Smith EM, Bender RA, Bardwell JC, Jakob U. Polyphosphate is a primordial chaperone. Molecular Cell. 53: 689-99. PMID 24560923 DOI: 10.1016/J.Molcel.2014.01.012  0.493
2014 Jakob U, Kriwacki R, Uversky VN. Conditionally and transiently disordered proteins: Awakening cryptic disorder to regulate protein function Chemical Reviews. 114: 6779-6805. PMID 24502763 DOI: 10.1021/Cr400459C  0.336
2013 Parker BW, Schwessinger EA, Jakob U, Gray MJ. The RclR protein is a reactive chlorine-specific transcription factor in Escherichia coli. The Journal of Biological Chemistry. 288: 32574-84. PMID 24078635 DOI: 10.1074/Jbc.M113.503516  0.431
2013 Cremers CM, Jakob U. Oxidant sensing by reversible disulfide bond formation. The Journal of Biological Chemistry. 288: 26489-96. PMID 23861395 DOI: 10.1074/Jbc.R113.462929  0.499
2013 Gray MJ, Wholey WY, Jakob U. Bacterial responses to reactive chlorine species. Annual Review of Microbiology. 67: 141-60. PMID 23768204 DOI: 10.1146/Annurev-Micro-102912-142520  0.32
2013 Müller A, Hoffmann JH, Meyer HE, Narberhaus F, Jakob U, Leichert LI. Nonnative disulfide bond formation activates the σ32-dependent heat shock response in Escherichia coli. Journal of Bacteriology. 195: 2807-16. PMID 23585533 DOI: 10.1128/Jb.00127-13  0.452
2013 Reichmann D, Jakob U. The roles of conditional disorder in redox proteins. Current Opinion in Structural Biology. 23: 436-442. PMID 23477949 DOI: 10.1016/J.Sbi.2013.02.006  0.482
2013 Brandes N, Tienson H, Lindemann A, Vitvitsky V, Reichmann D, Banerjee R, Jakob U. Time line of redox events in aging postmitotic cells. Elife. 2: e00306. PMID 23390587 DOI: 10.7554/Elife.00306  0.369
2013 Winther JR, Jakob U. Redox control: A black hole for oxidized glutathione Nature Chemical Biology. 9: 69-70. PMID 23334544 DOI: 10.1038/Nchembio.1161  0.347
2013 Powis K, Schrul B, Tienson H, Gostimskaya I, Breker M, High S, Schuldiner M, Jakob U, Schwappach B. Get3 is a holdase chaperone and moves to deposition sites for aggregated proteins when membrane targeting is blocked. Journal of Cell Science. 126: 473-83. PMID 23203805 DOI: 10.1242/Jcs.112151  0.42
2012 Bardwell JC, Jakob U. Conditional disorder in chaperone action. Trends in Biochemical Sciences. 37: 517-25. PMID 23018052 DOI: 10.1016/J.Tibs.2012.08.006  0.38
2012 Knoefler D, Thamsen M, Koniczek M, Niemuth NJ, Diederich AK, Jakob U. Quantitative in vivo redox sensors uncover oxidative stress as an early event in life. Molecular Cell. 47: 767-76. PMID 22819323 DOI: 10.1016/J.Molcel.2012.06.016  0.43
2012 Reichmann D, Xu Y, Cremers CM, Ilbert M, Mittelman R, Fitzgerald MC, Jakob U. Order out of disorder: working cycle of an intrinsically unfolded chaperone. Cell. 148: 947-57. PMID 22385960 DOI: 10.1016/J.Cell.2012.01.045  0.493
2012 Wholey WY, Jakob U. Hsp33 confers bleach resistance by protecting elongation factor Tu against oxidative degradation in Vibrio cholerae Molecular Microbiology. 83: 981-991. PMID 22296329 DOI: 10.1111/J.1365-2958.2012.07982.X  0.494
2011 Evans ML, Schmidt JC, Ilbert M, Doyle SM, Quan S, Bardwell JC, Jakob U, Wickner S, Chapman MR. E. coli chaperones DnaK, Hsp33 and Spy inhibit bacterial functional amyloid assembly. Prion. 5: 323-34. PMID 22156728 DOI: 10.4161/Pri.18555  0.441
2011 Brandes N, Reichmann D, Tienson H, Leichert LI, Jakob U. Using quantitative redox proteomics to dissect the yeast redoxome. The Journal of Biological Chemistry. 286: 41893-903. PMID 21976664 DOI: 10.1074/Jbc.M111.296236  0.491
2011 Quan S, Koldewey P, Tapley T, Kirsch N, Ruane KM, Pfizenmaier J, Shi R, Hofmann S, Foit L, Ren G, Jakob U, Xu Z, Cygler M, Bardwell JC. Genetic selection designed to stabilize proteins uncovers a chaperone called Spy. Nature Structural & Molecular Biology. 18: 262-9. PMID 21317898 DOI: 10.1038/Nsmb.2016  0.425
2011 Ghosh S, Cremers CM, Jakob U, Love NG. Chlorinated phenols control the expression of the multidrug resistance efflux pump MexAB-OprM in Pseudomonas aeruginosa by interacting with NalC. Molecular Microbiology. 79: 1547-56. PMID 21231970 DOI: 10.1111/J.1365-2958.2011.07544.X  0.307
2011 Thamsen M, Jakob U. The redoxome: Proteomic analysis of cellular redox networks. Current Opinion in Chemical Biology. 15: 113-119. PMID 21130023 DOI: 10.1016/J.Cbpa.2010.11.013  0.459
2011 Zhao F, Ilbert M, Varadan R, Cremers CM, Hoyos B, Acin-Perez R, Vinogradov V, Cowburn D, Jakob U, Hammerling U. Are zinc-finger domains of protein kinase C dynamic structures that unfold by lipid or redox activation? Antioxidants & Redox Signaling. 14: 757-66. PMID 21067413 DOI: 10.1089/Ars.2010.3773  0.388
2011 Thamsen M, Kumsta C, Li F, Jakob U. Is overoxidation of peroxiredoxin physiologically significant Antioxidants & Redox Signaling. 14: 725-730. PMID 20964547 DOI: 10.1089/Ars.2010.3717  0.736
2011 Kumsta C, Thamsen M, Jakob U. Effects of Oxidative Stress on Behavior, Physiology, and the Redox Thiol Proteome of Caenorhabditis elegans Antioxidants & Redox Signaling. 14: 1023-1037. PMID 20649472 DOI: 10.1089/Ars.2010.3203  0.749
2010 Cremers CM, Reichmann D, Hausmann J, Ilbert M, Jakob U. Unfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperone Journal of Biological Chemistry. 285: 11243-11251. PMID 20139072 DOI: 10.1074/Jbc.M109.084350  0.509
2010 Tapley TL, Franzmann TM, Chakraborty S, Jakob U, Bardwell JC. Protein refolding by pH-triggered chaperone binding and release. Proceedings of the National Academy of Sciences of the United States of America. 107: 1071-6. PMID 20080625 DOI: 10.1073/Pnas.0911610107  0.415
2010 Xu Y, Schmitt S, Tang L, Jakob U, Fitzgerald MC. Thermodynamic analysis of a molecular chaperone binding to unfolded protein substrates. Biochemistry. 49: 1346-53. PMID 20073505 DOI: 10.1021/Bi902010T  0.429
2009 Yi L, Jenkins PM, Leichert LI, Jakob U, Martens JR, Ragsdale SW. Heme regulatory motifs in heme oxygenase-2 form a thiol/disulfide redox switch that responds to the cellular redox state. The Journal of Biological Chemistry. 284: 20556-61. PMID 19473966 DOI: 10.1074/Jbc.M109.015651  0.463
2009 Barth E, Gora KV, Gebendorfer KM, Settele F, Jakob U, Winter J. Interplay of cellular cAMP levels, σS activity and oxidative stress resistance in Escherichia coli Microbiology. 155: 1680-1689. PMID 19372151 DOI: 10.1099/Mic.0.026021-0  0.445
2009 Kumsta C, Jakob U. Redox-regulated chaperones. Biochemistry. 48: 4666-4676. PMID 19368357 DOI: 10.1021/Bi9003556  0.798
2009 Tapley TL, Körner JL, Barge MT, Hupfeld J, Schauerte JA, Gafni A, Jakob U, Bardwell JC. Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding. Proceedings of the National Academy of Sciences of the United States of America. 106: 5557-62. PMID 19321422 DOI: 10.1073/Pnas.0811811106  0.381
2009 Brandes N, Schmitt S, Jakob U. Thiol-based redox switches in eukaryotic proteins. Antioxidants & Redox Signaling. 11: 997-1014. PMID 18999917 DOI: 10.1089/Ars.2008.2285  0.469
2008 Winter J, Ilbert M, Graf PC, Ozcelik D, Jakob U. Bleach activates a redox-regulated chaperone by oxidative protein unfolding. Cell. 135: 691-701. PMID 19013278 DOI: 10.1016/J.Cell.2008.09.024  0.769
2008 Herrmann JM, Jakob U. Special issue: redox regulation of protein folding. Preface. Biochimica Et Biophysica Acta. 1783: 519. PMID 18395585 DOI: 10.1016/J.Bbamcr.2008.03.002  0.399
2008 Leichert LI, Gehrke F, Gudiseva HV, Blackwell T, Ilbert M, Walker AK, Strahler JR, Andrews PC, Jakob U. Quantifying changes in the thiol redox proteome upon oxidative stress in vivo. Proceedings of the National Academy of Sciences of the United States of America. 105: 8197-202. PMID 18287020 DOI: 10.1073/Pnas.0707723105  0.493
2007 Brandes N, Rinck A, Leichert LI, Jakob U. Nitrosative stress treatment of E. coli targets distinct set of thiol-containing proteins Molecular Microbiology. 66: 901-914. PMID 17919278 DOI: 10.1111/J.1365-2958.2007.05964.X  0.466
2007 Ilbert M, Horst J, Ahrens S, Winter J, Graf PC, Lilie H, Jakob U. The redox-switch domain of Hsp33 functions as dual stress sensor. Nature Structural & Molecular Biology. 14: 556-63. PMID 17515905 DOI: 10.1038/Nsmb1244  0.754
2006 Ilbert M, Graf PC, Jakob U. Zinc center as redox switch--new function for an old motif. Antioxidants & Redox Signaling. 8: 835-46. PMID 16771674 DOI: 10.1089/Ars.2006.8.835  0.776
2006 Leichert LI, Jakob U. Global methods to monitor the thiol-disulfide state of proteins in vivo. Antioxidants & Redox Signaling. 8: 763-772. PMID 16771668 DOI: 10.1089/Ars.2006.8.763  0.482
2006 Mufti AR, Burstein E, Csomos RA, Graf PC, Wilkinson JC, Dick RD, Challa M, Son JK, Bratton SB, Su GL, Brewer GJ, Jakob U, Duckett CS. XIAP Is a copper binding protein deregulated in Wilson's disease and other copper toxicosis disorders. Molecular Cell. 21: 775-85. PMID 16543147 DOI: 10.1016/J.Molcel.2006.01.033  0.708
2005 Winter J, Linke K, Jatzek A, Jakob U. Severe Oxidative Stress Causes Inactivation of DnaK and Activation of the Redox-Regulated Chaperone Hsp33 Molecular Cell. 17: 381-392. PMID 15694339 DOI: 10.1016/J.Molcel.2004.12.027  0.539
2004 Winter J, Jakob U. Beyond Transcription—New Mechanisms for the Regulation of Molecular Chaperones Critical Reviews in Biochemistry and Molecular Biology. 39: 297-317. PMID 15763707 DOI: 10.1080/10409230490900658  0.504
2004 Leichert LI, Jakob U. Protein thiol modifications visualized in vivo. Plos Biology. 2. PMID 15502869 DOI: 10.1371/Journal.Pbio.0020333  0.504
2004 Janda I, Devedjiev Y, Derewenda U, Dauter Z, Bielnicki J, Cooper DR, Graf PC, Joachimiak A, Jakob U, Derewenda ZS. The crystal structure of the reduced, Zn2+-bound form of the B. subtilis Hsp33 chaperone and its implications for the activation mechanism. Structure (London, England : 1993). 12: 1901-7. PMID 15458638 DOI: 10.1016/J.Str.2004.08.003  0.743
2004 Hager J, Staker BL, Jakob U. Substrate binding analysis of the 23S rRNA methyltransferase RrmJ. Journal of Bacteriology. 186: 6634-42. PMID 15375145 DOI: 10.1128/Jb.186.19.6634-6642.2004  0.331
2004 Won HS, Low LY, De Guzman R, Martinez-Yamout M, Jakob U, Jane Dyson H. The zinc-dependent redox switch domain of the chaperone Hsp33 has a novel fold Journal of Molecular Biology. 341: 893-899. PMID 15328602 DOI: 10.1016/J.Jmb.2004.06.046  0.462
2004 Graf PC, Martinez-Yamout M, VanHaerents S, Lilie H, Dyson HJ, Jakob U. Activation of the redox-regulated chaperone Hsp33 by domain unfolding. The Journal of Biological Chemistry. 279: 20529-38. PMID 15023991 DOI: 10.1074/Jbc.M401764200  0.77
2004 Hoffmann JH, Linke K, Graf PC, Lilie H, Jakob U. Identification of a redox-regulated chaperone network. The Embo Journal. 23: 160-8. PMID 14685279 DOI: 10.1038/Sj.Emboj.7600016  0.766
2003 Linke K, Jakob U. Not every disulfide lasts forever: disulfide bond formation as a redox switch. Antioxidants & Redox Signaling. 5: 425-434. PMID 13678530 DOI: 10.1089/152308603768295168  0.478
2003 Collet JF, D'Souza JC, Jakob U, Bardwell JC. Thioredoxin 2, an oxidative stress-induced protein, contains a high affinity zinc binding site. The Journal of Biological Chemistry. 278: 45325-32. PMID 12952960 DOI: 10.1074/Jbc.M307818200  0.482
2003 Linke K, Wolfram T, Bussemer J, Jakob U. The roles of the two zinc binding sites in DnaJ. Journal of Biological Chemistry. 278: 44457-44466. PMID 12941935 DOI: 10.1074/Jbc.M307491200  0.397
2002 Graf PC, Jakob U. Redox-regulated molecular chaperones. Cellular and Molecular Life Sciences : Cmls. 59: 1624-31. PMID 12475172 DOI: 10.1007/Pl00012489  0.779
2002 Hager J, Staker BL, Bugl H, Jakob U. Active site in RrmJ, a heat shock-induced methyltransferase. The Journal of Biological Chemistry. 277: 41978-86. PMID 12181314 DOI: 10.1074/Jbc.M205423200  0.359
2002 Tan J, Jakob U, Bardwell JC. Overexpression of two different GTPases rescues a null mutation in a heat-induced rRNA methyltransferase. Journal of Bacteriology. 184: 2692-8. PMID 11976298 DOI: 10.1128/Jb.184.10.2692-2698.2002  0.311
2001 Graumann J, Lilie H, Tang X, Tucker KA, Hoffmann JH, Vijayalakshmi J, Saper M, Bardwell JC, Jakob U. Activation of the redox-regulated molecular chaperone Hsp33--a two-step mechanism. Structure (London, England : 1993). 9: 377-87. PMID 11377198 DOI: 10.1016/S0969-2126(01)00599-8  0.469
2001 Vijayalakshmi J, Mukhergee MK, Graumann J, Jakob U, Saper MA. The 2.2 Å crystal structure of Hsp33: A heat shock protein with redox-regulated chaperone activity Structure. 9: 367-375. PMID 11377197 DOI: 10.1016/S0969-2126(01)00597-4  0.503
2001 Jakob U, Eser M, Bardwell JC. Redox switch of hsp33 has a novel zinc-binding motif. The Journal of Biological Chemistry. 275: 38302-10. PMID 10976105 DOI: 10.1074/Jbc.M005957200  0.461
2000 Bügl H, Fauman EB, Staker BL, Zheng F, Kushner SR, Saper MA, Bardwell JC, Jakob U. RNA methylation under heat shock control. Molecular Cell. 6: 349-60. PMID 10983982 DOI: 10.1016/S1097-2765(00)00035-6  0.349
2000 Shao F, Bader MW, Jakob U, Bardwell JC. DsbG, a protein disulfide isomerase with chaperone activity. The Journal of Biological Chemistry. 275: 13349-52. PMID 10788443 DOI: 10.1074/Jbc.275.18.13349  0.467
2000 Barbirz S, Jakob U, Glocker MO. Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone. Journal of Biological Chemistry. 275: 18759-18766. PMID 10764757 DOI: 10.1074/Jbc.M001089200  0.452
1999 Jakob U, Muse W, Eser M, Bardwell JCA. Chaperone Activity with a Redox Switch Cell. 96: 341-352. PMID 10025400 DOI: 10.1016/S0092-8674(00)80547-4  0.536
1998 Buchner J, Bose S, Mayr C, Jakob U. Purification and characterization of prokaryotic and eukaryotic Hsp90. Methods in Enzymology. 290: 409-18. PMID 9534178 DOI: 10.1016/S0076-6879(98)90034-9  0.473
1998 Buchner J, Grallert H, Jakob U. Analysis of chaperone function using citrate synthase as nonnative substrate protein. Methods in Enzymology. 290: 323-338. PMID 9534173 DOI: 10.1016/S0076-6879(98)90029-5  0.441
1996 Jakob U. HSP90--news from the front. Frontiers in Bioscience. 1. PMID 9159187 DOI: 10.2741/A133  0.443
1996 Jakob U, Scheibel T, Bose S, Reinstein J, Buchner J. Assessment of the ATP binding properties of Hsp90. The Journal of Biological Chemistry. 271: 10035-41. PMID 8626558 DOI: 10.1074/Jbc.271.17.10035  0.383
1995 Jakob U, Meyer I, Bügl H, André S, Bardwell JC, Buchner J. Structural organization of procaryotic and eucaryotic Hsp90. Influence of divalent cations on structure and function. The Journal of Biological Chemistry. 270: 14412-9. PMID 7782303 DOI: 10.1074/Jbc.270.24.14412  0.437
1995 Jakob U, Lilie H, Meyer I, Buchner J. Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo. The Journal of Biological Chemistry. 270: 7288-94. PMID 7706269 DOI: 10.1074/Jbc.270.13.7288  0.432
1994 Jakob U, Buchner J. Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones Trends in Biochemical Sciences. 19: 205-211. PMID 7914036 DOI: 10.1016/0968-0004(94)90023-X  0.466
1994 Knauf U, Jakob U, Engel K, Buchner J, Gaestel M. Stress- and mitogen-induced phosphorylation of the small heat shock protein Hsp25 by MAPKAP kinase 2 is not essential for chaperone properties and cellular thermoresistance. The Embo Journal. 13: 54-60. DOI: 10.1002/J.1460-2075.1994.Tb06234.X  0.423
1992 Wiech H, Buchner J, Zimmermann R, Jakob U. Hsp90 chaperones protein folding in vitro. Nature. 358: 169-170. PMID 1614549 DOI: 10.1038/358169A0  0.49
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