Our Mile Stones
Publications
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. 2009.
J Biol Chem. 284(31):20556-61 (Abstract)
Redox-regulated chaperones.
Kumsta C, Jakob U. 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. 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. 2009.
Proc Natl Acad Sci U S A. 106(14):5557-62 (Abstract)
Bleach activates a redox-regulated chaperone by oxidative protein unfolding.
Winter J, Ilbert M, Graf PC, Ozcelik D, Jakob U. 2008.
Cell, 135(4):691-701 (Abstract)
Thiol-Based Redox Switches in Eukaryotic Proteins.
Brandes N, Schmitt S, Jakob U. 2008.
Antioxid Redox Signal, [Epub ahead of print]. (Abstract)
Special issue: redox regulation of protein folding. Preface.
Herrmann JM, Jakob U. 2008.
Biochim Biophys Acta, 1783(4):519 (Abstract)
Quantifying Changes in the Thiol Redox Proteome Upon Oxidative Stress in Vivo.
Leichert, L.I., Gehrke F., Gudiseva, H.V., Ilbert, M., Blackwell, T., Walker, A.K., Strahler, J.R., Andrews, P.C. and U. Jakob. 2007.
Proc Nat Acad Sci, 105(24):8197-202 (Abstract)
The redox-switch domain of Hsp33 functions as dual stress sensor.
Ilbert, M., Horst, J., Ahrens, S., Winter, J., Graf, P.C., Lilie, H., Jakob, U. 2007.
Nat Struct Mol Biol, 556-563 (Abstract)
Nitrosative stress treatment of E. coli targets distinct set of thiol-containing proteins.
Brandes, N., Rinck, A., Leichert, L.I. and U. Jakob. 2007.
Mol Microbiol, 66 (4): 901-914 (Abstract)
Global Methods to Monitor the Thiol-Disulfide State of Proteins in vivo.
Leichert, L.I. and Jakob, U. 2006.
Antioxid Redox Signal, 8, 763-772 (Abstract)
XIAP Is a copper binding protein deregulated in Wilson's disease and other copper toxicosis disorders.
Mufti, A.R., Burstein, E., Csomos, R.A., Graf, P.C.F., Wilkinson, J.C., Dick, R.D., Challa, M., Son, J.K., Bratton, S.B., Su, G.L., Brewer, G.J., Jakob, U. and C.S. Duckett. 2006.
Mol Cell, 21: 775-785 (Abstract)
CoSMoS: Conserved Sequence Motif Search in the proteome.
Liu, X.I., Korde, N., Jakob, U., and Leichert, L.I.O. 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., and Jakob, U. 2005.
Mo. Cell. 17: 381-392 (Abstract)
Beyond Transcription - Novel Mechanisms to Regulate Molecular Chaperone Activity.
Winter, J. and Jakob, U. 2004.
Critical Review in Biochemistry and Molecular Biology, 39: 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, D.R., Graf, P.C.F., Joachimiak, A., Jakob, U. and Derewenda, Z. 2004.
Structure, 12: 1901-1907 (Abstract)
Protein Thiol Modifications Visualized in vivo.
Leichert, L., and Jakob, U. 2004.
PloS Biology, 2: e333 (Abstract)
The Zinc-dependent Redox Switch Domain of the Chaperone Hsp33 has a Novel Fold.
Won, H.-S., Low, L.Y., DeGuzman, R., Martinez-Yamout, M., Jakob, U. and Dyson, H.J. 2004.
J. Mol. Biol. 341: 893-899 (Abstract)
Substrate binding analysis of the 23S rRNA methyltransferase RrmJ.
Hager, J., Staker, B. and Jakob, U. 2004.
J. Bact. 186: 6634-6642 (Abstract)
Activation of the redox regulated chaperone Hsp33 by domain unfolding.
Graf, P.C.F., Martinez-Yamout, M., VanHaerents, S., Lilie, H., Dyson J. H. and Jakob, U. 2004.
J. Biol. Chem. 279: 20520-20538 (Abstract)
Identification of a redox regulated chaperone network.
Hoffmann, J.H., Graf, P.C.F., Linke, K., Lilie, H. and Jakob, U. 2004.
EMBO J. 23: 160-168 (Abstract)
Redox regulation of chaperones.
Hoffmann, J.H. and U. Jakob. 2004. 2004.
in: Protein Folding Handbook. eds. Buchner, J. and Kiefhaber, T., Wiley-VCH, ISBN: 3-527-30784-2,
The roles of the two zinc binding sites in DnaJ.
Linke, K., Wolfram, T., Bussemer, J. and Jakob, U. 2003.
J. Biol. Chem. 278: 44457-44466 (Abstract)
Thioredoxin 2, an oxidative stress induced protein, contains a high affinity zinc binding site.
Collet, J.F., D'Souza, J.C., Jakob, U., Bardwell, J.C. 2003.
J. Biol. Chem. 278: 45325-45332 (Abstract)
Not every disulfide lasts forever: disulfide bond formation as a redox switch.
Linke, K. and Jakob, U. 2003.
Antioxid Redox Signal, 5: 425-434 (Abstract)
Active site in RrmJ, a heat shock induced methyltransferase.
Hager, J., Staker, B.L., Bugl, H and Jakob, U. 2002.
J. Biol. Chem. 277: 41978-41986 (Abstract)
Redox regulated molecular chaperones.
Graf, P.C.F. and U. Jakob. 2002.
Cell. Mol. Life Sci. 59: 1624-1631 (Abstract)
Overexpression of two different GTPases rescues a null mutation in a heat-induced rRNA methyltransferase.
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Tan, J., Jakob, U. and J.C.A. Bardwell. 2002.
J. Bact. 184, 2692-2698 (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. and M. Saper. 2001.
Structure, 9: 367-375 (Abstract)
Activation of the Redox Regulated Molecular Chaperone Hsp33-A Two Step Mechanism.
Graumann, J., Lilie, H., Tang, X., Tucker, K.C., Hoffmann, J.H., Vijayalakshmi, J., Saper, M., Bardwell, J.C.A. and U. Jakob. 2001.
Structure, 9, 377-387 (Abstract)
Hsp33's Redox Switch has a Novel Zinc-Binding Motif.
Jakob, U., Eser, M. and J.C.A. Bardwell. 2000.
J. Biol. Chem. 275, 38302-38310 (Abstract)
RNA Methylation under Heat Shock Control.
Bügl, H., Fauman, E.B., Staker, B.L., Zheng, F., Kusher, S.R., Saper, M.A., Bardwell, J.C.A., and U. Jakob. 2000.
Mol. Cell, 6, 349-360 (Abstract)
Mass Spectrometry Unravels Disulfide Bond Formation as Mechanism to Activate a Molecular Chaperone.
Barbirz, S., Jakob, U. and M. Glocker. 2000.
J. Biol. Chem. 275, 18759-66 (Abstract)
DsbG, a Protein Disulfide Isomerase With Chaperone Activity.
Shao, F., Bader, M., Muse, W., Jakob, U. and J.C.A. Bardwell. 2000.
J. Biol. Chem. 275, 13349-13352 (Abstract)
Heating Greatly Speeds Coomassie Blue Staining and Destaining.
Wong, C., Bardwell, J.C.A. and U. Jakob. 2000.
BioTechniques, 28, 426-432 (Abstract)
Chaperone Activity with a Redox Switch.
Jakob, U., Muse, W., Eser, M. and J.C.A. Bardwell. 1999.
Cell, 96:341-352 (Abstract)
Analysis of Chaperone Function Using Citrate Synthase as a Nonnative Substrate.
Buchner, J., Grallert, H. and U. Jakob. 1998.
Methods Enzymol. 290: 323-338 (Abstract)
Purification and Characterization of Pro- and Eukaryotic Hsp90.
Buchner, J., Bose, S. and U. Jakob. 1998.
Methods Enzymol. 290: 409-418 (Abstract)
Hsp90-News from the Front.
Jakob, U. 1998.
Frontiers in Bioscience, 1: 309-317 (Abstract)
Mammalian Hsp90.
Jakob, U. and J. Buchner. 1997.
in: Guidebook to the Molecular Chaperones and Protein Folding Catalysts. ed. Gething, M.J., Oxford University Press,
HtpG.
Jakob, U. and J.C.A Bardwell. 1997.
in: Guidebook to the Molecular Chaperones and Protein Folding Catalysts. ed. Gething, M.J. Oxford University Press,
Assessment of the ATP Binding Properties of Hsp90.
Jakob, U., Scheibel, T., Bose, S., Reinstein, J. and J. Buchner. . 1996.
J. Biol. Chem. 271: 10035-10041 (Abstract)
Method for the stabilization of proteins using heat shock protein Hsp90.
Jakob, U., Buchner, J., Zimmermann, R. and R. Rudolph. 1995.
United States Patent # 5,474,892.
Structural Organization of Eu- and Procaryotic Hsp90-Influence of Divalent Cations on Structure and Function.
Jakob, U., Meyer, I., Bügl, H., Andrè, S., Bardwell, J.C.A. and J. Buchner. 1995.
J. Biol. Chem. 14412-14419 (Abstract)
Transient Interaction of Hsp90 with Early Unfolding Intermediates of Citrate Synthase-Implications for Heat Shock in vivo.
Jakob, U., Lilie, H., Meyer, I. and J. Buchner. 1995.
J. Biol. Chem. 7288-7294 (Abstract)
Assisting Spontaneity: The Role of Hsp90 and Small Hsps as Molecular Chaperones.
Jakob, U. and J. Buchner. 1994.
Trends Biochem. Sci, 19: 205-211 (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. and M. Gaestel. 1994.
EMBO J. 13: 54-60 (Abstract)
Small Heat Shock Proteins are Molecular Chaperones.
Jakob, U., Gaestel, M., Engel, K. and J. Buchner. 1993.
J. Biol. Chem. 268: 1517-1520 (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. and U. Jakob. 1993.
J. Biol. Chem. 268: 7414-7421 (Abstract)
Hsp90 Chaperones-Protein Folding in vitro.
Wiech, H., Buchner, J., Zimmermann, R. and U. Jakob. 1992.
Nature, 358: 169-170 (Abstract)
