Our Mile Stones
Publications
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, in press
The redox-switch domain of Hsp33 functions as dual stress sensor.
Ilbert, M., Horst, J., Ahrens, S., Winter, J., Graf, P.C., Lilie, H. and U. Jakob. 2007.
Nat Struct Mol Biol 14 (6): 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 U. Jakob. 2006.
Antioxid Redox Signal. 8, 763-772 (Abstract)
Zinc center as redox switch--new function for an old motif.
Ilbert, M., Graf, P.C., and Jakob, U. 2006.
Antioxid Redox Signal. 8 (5-6): 835-846 (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, 775-85 (Abstract)
CoSMoS: Conserved Sequence Motif Search in the proteome.
Liu, X.I., Korde, N., Jakob, U. and L.I. Leichert. 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 U. Jakob. 2005.
Mol Cell 17, 381-392 (Abstract)
Beyond transcription-new mechanisms for the regulation of molecular chaperones.
Winter, J. and U. Jakob. 2004.
Crit Rev Biochem Mol Biol 39, 297-317 (Abstract)
Protein Thiol Modifications Visualized In Vivo.
Leichert, L.I. and U. Jakob. 2004.
PLoS Biology 2, e333 (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 Z. Derewenda. 2004.
Structure 12, 1901-1907 (Abstract)
Substrate binding analysis of the 23S rRNA methyltransferase RrmJ.
Hager, J., Staker, B. and U. Jakob. 2004.
J. Bact. 186, 6634-6642 (Abstract)
Redox regulation of chaperones.
Hoffmann, J.H. and U. Jakob. 2004.
in: Protein Folding Handbook. eds. Buchner, J. and Kiefhaber, T., Wiley-VCH, ISBN: 3-527-30784-2
The zinc-dependent redox switch domain of the chaperone Hsp33 has a novel fold.
Won, H.S., Low, L.Y., De Guzman, R., Martinez-Yamout, M., Jakob, U. and H.J. Dyson. 2004.
J. Mol. Biol. 341, 893-899 (Abstract)
Activation of the redox regulated chaperone Hsp33 by domain unfolding.
Graf, P.C.F., Martinez-Yamout, M., VanHaerents, S., Lilie, H., Dyson H.J. and U. Jakob. 2004.
J. Biol. Chem. 279, 20529-20538 (Abstract)
Identification of a redox regulated chaperone network.
Hoffmann, J.H., Graf, P.C.F., Linke, K., Lilie, H. and U. Jakob. 2004.
EMBO J. 23, 160-168 (Abstract)
Thioredoxin 2, an oxidative stress induced protein, contains a high affinity zinc binding site.
Collet, J.F., D'Souza, J.C., Jakob, U. and J.C.A. Bardwell. 2003.
J. Biol. Chem. 278, 45325-45332 (Abstract)
The roles of the two zinc binding sites in DnaJ.
Linke, K., Wolfram, T., Bussemer, J. and U. Jakob. 2003.
J. Biol. Chem. 278, 44457-44466 (Abstract)
Not every disulfide lasts forever: disulfide bond formation as a redox switch.
Linke, K. and U. Jakob. 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 U. Jakob. 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.
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.
Vijayalakshmi, 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)
