Publications

Bile salts act as effective protein-unfolding agents and instigators of disulfide stress in vivo.
Cremers CM1, Knoefler D, Vitvitsky V, Banerjee R, Jakob U.
Proc Natl Acad Sci U S A. 2014 Apr 4. [Epub ahead of print] PMID:24706920. (Abstract)

Thiol-Based Redox Switches.
Groitl B, Jakob U. Epub 2014 Mar 18. 
Biochim Biophys Acta. [Epub ahead of print] Review. PMID:24657586. (Abstract)

Polyphosphate is a primordial chaperone.
Gray MJ, Wholey WY, Wagner NO, Cremers CM, Mueller-Schickert A, Hock NT,
Krieger AG, Smith EM, Bender RA, Bardwell JC, Jakob U. Epub 2014 Feb 20.
Mol Cell.
2014 Mar 6;53(5):689-99. PMID:24560923. (Abstract)

Conditionally and Transiently Disordered Proteins: Awakening Cryptic Disorder To Regulate Protein Function.
Jakob U, Kriwacki R, Uversky VN. Epub . 2014 Feb 6.
Chem Rev.
2014 Feb 6. [Epub ahead of print]. PMID:24502763. (Abstract)

The RclR protein is a reactive chlorine-specific transcription factor in Escherichia coli.
Parker BW, Schwessinger EA, Jakob U, Gray MJ. Epub 2013 Sep 27.
J Biol Chem
. 2013 Nov 8;288(45):32574-84. doi: 10.1074/jbc.M113.503516. PMCID: PMC3820890. (Abstract)

Oxidant sensing by reversible disulfide bond formation.
Cremers CM, Jakob U. Epub 2013 Jul 16.
J Biol Chem. 2013 Sep 13;288(37):26489-96. doi: 10.1074/jbc.R113.462929. Review. PMCID: PMC3772196. (Abstract)

Bacterial responses to reactive chlorine species.
Gray MJ, Wholey WY, Jakob U. Epub 2013 Jun 14.
Annu Rev Microbiol. 2013;67:141-60. doi: 10.1146/annurev-micro-102912-142520. PMCID:PMC3891400. (Abstract)

Nonnative disulfide bond formation activates the σ32-dependent heat shock response in Escherichia coli.
Müller A, Hoffmann JH, Meyer HE, Narberhaus F, Jakob U, Leichert LI. Epub 2013 Apr 12.
J Bacteriol
. 2013 Jun;195(12):2807-16. doi: 10.1128/JB.00127-13. PMCID: PMC3697257. (Abstract)

NemR is a Bleach-Sensing Transcription Factor. 
Gray MJ, Wholey WY, Parker BW, Kim M, Jakob U. March 2013.
J Biol Chem, 288(19):13789-98 (Abstract)

Time line of redox events in aging postmitotic cells. 
Brandes N, Tienson H, Lindemann A, Vitvitsky V, Reichmann D, Banerjee R, Jakob U. March 2013.
Elife, 2:e00306 (Abstract)

The roles of conditional disorder in redox proteins. 
Reichmann D, Jakob U. March 2013.
Curr Opin Struct Biol, pii: S0959-440X(13)00035-3 (Abstract)

Redox Control: A black hole for oxidized glutathione. 
Winther JR, Jakob U. February 2013.
Nat Chem Biol, 9(2):69-70 (Abstract)

Get3 is a holdase chaperone and moves to deposition sites for aggregated proteins when membrane targeting is blocked. 
Powis K, Schrul B, Tienson H, Gostimskaya I, Breker M, High S, Schuldiner M, Jakob U, Schwappach B. January 2013.
J Cell Sci. 126(Pt 2):473-83 (Abstract)

Conditional disorder in chaperone action. 
Bardwell JC, Jakob U. December 2012.
Trends Biochem Sci, 37(12):517-2 (Abstract)

Quantitative in vivo redox sensors uncover oxidative stress as an early event in life. 
Knoefler D, Thamsen M, Koniczek M, Niemuth NJ, Diederich AK, Jakob U. September 2012.
Mol Cell, 47(5):767-7 (Abstract)

Redox, haem and CO in enzymatic catalysis and regulation. 
Ragsdale SW, Yi L, Bender G, Gupta N, Kung Y, Yan L, Stich TA, Doukov T, Leichert L, Jenkins PM, Bianchetti CM, George SJ, Cramer SP, Britt RD, Jakob U, Martens JR, Phillips GN Jr, Drennan CL. June 2012.
Biochem Soc Trans, 40(3):501-7 (Abstract)

Hsp33 confers bleach resistance by protecting elongation factor Tu against oxidative degradation in Vibrio cholerae. 
Wholey WY, Jakob U. March 2012.
Mol Microbiol, 83(5):981-91 (Abstract)

Order out of disorder: working cycle of an intrinsically unfolded chaperone. 
Reichmann D, Xu Y, Cremers CM, Ilbert M, Mittelman R, Fitzgerald MC, Jakob U. January 2012.
Cell, 148(5):947-57 (Abstract)

Using quantitative redox proteomics to dissect the yeast redoxome. 
Brandes N, Reichmann D, Tienson H, Leichert LI, Jakob U. December 2011.
J Biol Chem, 286(48):41893-903 (Abstract)

E. coli chaperones DnaK, Hsp33, and Spy inhibit bacterial functional amyloid assembly. 
Evans ML, Schmidt JC, Ilbert M, Doyle SM, Quan S, Bardwell JC, Jakob U, Wickner S, Chapman MR. October 2011.
Prion, 5(4) (Abstract)

Chlorinated phenols control the expression of the multidrug resistance efflux pump MexAB-OprM in Pseudomonas aeruginosa by interacting with NalC. 
Ghosh S, Cremers CM, Jakob U, Love NG. March 2011.
Mol Microbiology, 79(6):1547-56 (Abstract)

Effects of oxidative stress on behavior, physiology, and the redox thiol proteome of Caenorhabditis elegans
Kumsta C, Thamsen M, Jakob U. March 2011.
Antiox Redox Signal, 14(6):1023-37 (Abstract)

Genetic selection designed to stabilize proteins uncovers a chaperone called Spy. 
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. March 2011.
Nat Struct Mol Biol, 18(3):262-9 (Abstract)

Are zinc-finger domains of protein kinase C dynamic structures that unfold by lipid or redox activation?. 
Zhao F, Ilbert M, Varadan R, Cremers CM, Hoyos B, Acin-Perez R, Vinogradov V, Cowburn D, Jakob U, Hammerling U. March 2011.
Antioxid Redox Signal, 14(5):757-66 (Abstract)

The redoxome: Proteomic analysis of cellular redox networks. 
Thamsen M, Jakob U. February 2011.
Curr Opin Chem Biol, 15(1):113-9 (Abstract)

Is overoxidation of peroxiredoxin physiologically significant?. 
Thamsen M, Kumsta C, Li F, Jakob U. February 2011.
Antioxid Redox Signal, 14(4):725-30 (Abstract)

Unfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperone. 
Cremers CM, Reichmann D, Hausmann J, Ilbert M, Jakob U. April 2010.
J Biol Chem, 285(15):11243-51 (Abstract)

Thermodynamic analysis of a molecular chaperone binding to unfolded protein substrates. 
Xu Y, Schmitt S, Tang L, Jakob U, Fitzgerald MC. January 2010.
Biochemistry, 49(6):1346-53 (Abstract)

Protein refolding by pH-triggered chaperone binding and release. 
Tapley TL, Franzmann TM, Chakraborty S, Jakob U, Bardwell JC. January 2010.
Proc Natl Acad Sci U S A, 107(3):1071-6 (Abstract)

Heme regulatory motifs in heme oxygenase-2 form a thiol/disulfide redox switch that responds to the cellular redox state. 
Yi L, Jenkins PM, Leichert LI, Jakob U, Martens JR, Ragsdale SW. July 2009.
J Biol Chem. 284(31):20556-61 (Abstract)

Redox-regulated chaperones. 
Kumsta C, Jakob U. June 2009.
Biochemistry, 48(22):4666-76 (Abstract)

Interplay of cellular cAMP levels, {sigma}S activity and oxidative stress resistance in Escherichia coli. 
Barth E, Gora KV, Gebendorfer KM, Settele F, Jakob U, Winter J. May 2009.
Microbiology, 155(Pt 5):1680-9 (Abstract)

Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding. 
Tapley TL, Körner JL, Barge MT, Hupfeld J, Schauerte JA, Gafni A, Jakob U, Bardwell JC. May 2009.
Proc Natl Acad Sci USA, 106(14):5557-62 (Abstract)

Protein refolding by pH-triggered chaperone binding and release. 
Tapley TL, Franzmann TM, Chakraborty S, Jakob U, Bardwell JC. January 2009.
Proc Natl Acad Sci USA, 107(3):1071-6 (Abstract)

Bleach activates a redox-regulated chaperone by oxidative protein unfolding. 
Winter J, Ilbert M, Graf PC, Ozcelik D, Jakob U. November 2008.
Cell, 135(4):691-701 (Abstract)

Thiol-Based Redox Switches in Eukaryotic Proteins. 
Brandes N, Schmitt S, Jakob U. November 2008.
Antioxid Redox Signal, [Epub ahead of print]. (Abstract)

Quantifying Changes in the Thiol Redox Proteome Upon Oxidative Stress in Vivo
Leichert LI, Gehrke F, Gudiseva HV, Ilbert M, Blackwell T, Walker AK, Strahler JR, Andrews PC, Jakob U. June 2008.
Proc Nat Acad Sci, 105(24):8197-202 (Abstract)

Special issue: redox regulation of protein folding. Preface. 
Herrmann JM, Jakob U. April 2008.
Biochim Biophys Acta, 1783(4):519 (Abstract)

Nitrosative stress treatment of E. coli targets distinct set of thiol-containing proteins. 
Brandes N, Rinck A, Leichert LI, Jakob U. November 2007.
Mol Microbiol, 66(4):901-14 (Abstract)

The redox-switch domain of Hsp33 functions as dual stress sensor. 
Ilbert M, Horst J, Ahrens S, Winter J, Graf PC, Lilie H, Jakob U. June 2007.
Nat Struct Mol Biol, 14(6):556-63 (Abstract)

XIAP Is a copper binding protein deregulated in Wilson's disease and other copper toxicosis disorders. 
Mufti AR, Burstein E, Csomos RA, Graf PCF, Wilkinson JC, Dick RD, Challa M, Son JK, Bratton SB, Su GL, Brewer GJ, Jakob U, Duckett CS. August 2006.
Mol Cell, 21(6):775-85 (Abstract)

Global Methods to Monitor the Thiol-Disulfide State of Proteins in vivo
Leichert LI, Jakob U. May 2006.
Antioxid Redox Signal, 8(5-6):763-72 (Abstract)

CoSMoS: Conserved Sequence Motif Search in the proteome. 
Liu XI, Korde N, Jakob U, Leichert LIO. January 2006.
BMC Bioinformatics, 7:37 (Abstract)

Severe Oxidative Stress Causes Inactivation of DnaK and Activation of the Redox Regulated Chaperone Hsp33. 
Winter J, Linke K, Jatzek A, Jakob U. February 2005.
Mol Cell, 17(3):381-92 (Abstract)

Protein Thiol Modifications Visualized in vivo
Leichert L, Jakob U. November 2004.
PloS Biology, 2(11):e333 (Abstract)

Beyond Transcription - Novel Mechanisms to Regulate Molecular Chaperone Activity. 
Winter J, Jakob U. September 2004.
Critical Review in Biochemistry and Molecular Biology, 39(5-6):297-317 (Abstract)

The Crystal Structure of the Reduced Zn2+-Bound Form of the B. subtilis Hsp33 Chaperone and its Implications for the Activation Mechanism. 
Janda I, Devedjiev Y, Derewenda U, Dauter Z, Bielnicki J, Cooper DR, Graf PCF, Joachimiak A, Jakob U, Derewenda Z. August 2004.
Structure, 12(10):1901-7 (Abstract)

The Zinc-dependent Redox Switch Domain of the Chaperone Hsp33 has a Novel Fold. 
Won HS, Low LY, DeGuzman R, Martinez-Yamout M, Jakob U, Dyson HJ. August 2004.
J Mol Biol, 341(4):893-99 (Abstract)

Substrate binding analysis of the 23S rRNA methyltransferase RrmJ. 
Hager J, Staker B, Jakob U. May 2004.
J Bact, 186(19):6634-42 (Abstract)

Activation of the redox regulated chaperone Hsp33 by domain unfolding. 
Graf PCF, Martinez-Yamout M, VanHaerents S, Lilie H, Dyson JH, Jakob U. April 2004.
J Biol Chem, 279(19):20520-38 (Abstract)

Identification of a redox regulated chaperone network. 
Hoffmann JH, Graf PCF, Linke K, Lilie H, Jakob U. January 2004.
EMBO J, 23(1):160-8 (Abstract)

Redox regulation of chaperones. 
Hoffmann JH, Jakob U. January 2004.
Protein Folding Handbook. eds. Buchner, J. and Kiefhaber, T., Wiley-VCH, ISBN: 3-527-30784-2.

Thioredoxin 2, an oxidative stress induced protein, contains a high affinity zinc binding site. 
Collet JF, D'Souza JC, Jakob U, Bardwell JCA. November 2003.
J Biol Chem, 278(46):45325-32 (Abstract)

The roles of the two zinc binding sites in DnaJ. 
Linke K, Wolfram T, Bussemer J, Jakob U. September 2003.
J Biol Chem, 278(45):44457-66 (Abstract)

Not every disulfide lasts forever: disulfide bond formation as a redox switch. 
Linke K, Jakob U. August 2003.
Antioxid Redox Signal, 5(4):425-34 (Abstract)

Redox regulated molecular chaperones. 
Graf PCF, Jakob U. October 2002.
Cell Mol Life Sci, 59(10):1624-31 (Abstract)

Active site in RrmJ, a heat shock induced methyltransferase. 
Hager J, Staker BL, Bugl H, Jakob U. September 2002.
J Biol Chem, 277:41978-86 (Abstract)

Overexpression of two different GTPases rescues a null mutation in a heat-induced rRNA methyltransferase. 
Tan J, Jakob U, Bardwell JCA. January 2002.
J Bact, 184(10):2692-8 (Abstract)

The 2.2 Å Crystal Structure of Hsp33: A Heat Shock Protein with Redox-regulated Chaperone Activity. 
Vijayalakshm J, Mukherjee M, Graumann J, Jakob U, Saper M. May 2001.
Structure, 9(5):367-75 (Abstract)

Activation of the Redox Regulated Molecular Chaperone Hsp33-A Two Step Mechanism. 
Graumann J, Lilie H, Tang X, Tucker KC, Hoffmann JH, Vijayalakshmi J, Saper M, Bardwell JCA, Jakob U. January 2001.
Structure, 9(5):377-87 (Abstract)

Hsp33's Redox Switch has a Novel Zinc-Binding Motif. 
Jakob U, Eser M, Bardwell JCA. December 2000.
J Biol Chem, 275(49):38302-10 (Abstract)

RNA Methylation under Heat Shock Control. 
Bügl H, Fauman EB, Staker BL, Zheng F, Kusher SR, Saper MA, Bardwell JCA, Jakob U. August 2000.
Mol Cell, 6:2)349-60 (Abstract)

Mass Spectrometry Unravels Disulfide Bond Formation as Mechanism to Activate a Molecular Chaperone. 
Barbirz S, Jakob U, Glocker MO. June 2000.
J Biol Chem, 275(25):18759-66 (Abstract)

DsbG, a Protein Disulfide Isomerase With Chaperone Activity. 
Shao F, Bader M, Muse W, Jakob U, Bardwell JCA. May 2000.
J Biol Chem, 275(18):13349-52 (Abstract)

Heating Greatly Speeds Coomassie Blue Staining and Destaining. 
Wong C, Bardwell JCA, Jakob U. March 2000.
Biotechniques, 28(3):426-8, 430, 432 (Abstract)

Chaperone Activity with a Redox Switch. 
Jakob U, Muse W, Eser M, Bardwell JCA. January 1999.
Cell, 96(3):341-52 (Abstract)

Analysis of Chaperone Function Using Citrate Synthase as a Nonnative Substrate. 
Buchner J, Grallert H, Jakob U. March 1998.
Methods Enzymol, 290:323-38 (Abstract)

Purification and Characterization of Pro- and Eukaryotic Hsp90. 
Buchner J, Bose S, Jakob U. February 1998.
Methods Enzymol, 290:409-18 (Abstract)

Mammalian Hsp90. 
Jakob U, Buchner J. February 1997.
Guidebook to the Molecular Chaperones and Protein Folding Catalysts. ed. Gething, M.J., Oxford University Press.

HtpG. 
Jakob U, Bardwell JCA. January 1997.
Guidebook to the Molecular Chaperones and Protein Folding Catalysts. ed. Gething, M.J. Oxford University Press.

Hsp90-News from the Front. 
Jakob U. October 1996.
Frontiers in Bioscience, 1:d309-17 (Abstract)

Assessment of the ATP Binding Properties of Hsp90. 
Jakob U, Scheibel T, Bose S, Reinstein J, Buchner J . January 1996.
J Biol Chem, 271(17):10035-41 (Abstract)

Method for the stabilization of proteins using heat shock protein Hsp90. 
Jakob U, Buchner J, Zimmermann R, Rudolph R. March 1995.
United States Patent # 5,474,892.

Transient Interaction of Hsp90 with Early Unfolding Intermediates of Citrate Synthase-Implications for Heat Shock in vivo. 
Jakob U, Lilie H, Meyer I, Buchner J. March 1995.
J Biol Chem, 270(13):7288-94 (Abstract)

Structural Organization of Eu- and Procaryotic Hsp90-Influence of Divalent Cations on Structure and Function. 
Jakob U, Meyer I, Bügl H, Andrè S, Bardwell JCA, Buchner J. February 1995.
J Biol Chem, 270(24):14412-9 (Abstract)

Assisting Spontaneity: The Role of Hsp90 and Small Hsps as Molecular Chaperones. 
Jakob U, Buchner J. May 1994.
Trends Biochem Sci, 19(5):205-11 (Abstract)

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. 
Knauf U, Jakob U, Engel K, Buchner J, Gaestel M. January 1994.
EMBO J, 13(1):54-60 (Abstract)

Small Heat Shock Proteins are Molecular Chaperones. 
Jakob U, Gaestel M, Engel K, Buchner J. January 1993.
J Biol Chem, 268(3):1517-20 (Abstract)

Hsc70, Immunoglobulin Heavy Chain Binding Protein, and Hsp90 Differ in their Ability to Stimulate Transport of Precursor Proteins into Mammalian Microsomes. 
Wiech H, Buchner J, Zimmermann M, Zimmermann R, Jakob U. January 1993.
J Biol Chem, 268(10):7414-21 (Abstract)

Hsp90 Chaperones-Protein Folding in vitro. 
Wiech H, Buchner J, Zimmermann R, Jakob U. July 1992.
Nature, 358(6382):169-70 (Abstract)

milestones

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