Mogk, A., Huber, D., Bukau, B. Integrating protein homeostasis strategies in prokaryotes. Morimoto et al (ed). (2010) CSH press. 3(4). pii: a004366. doi: 10.1101/cshperspect.a004366. (Abstract).
Tyedmers, J., Mogk, A., Bukau, B. Cellular strategies for controlling protein aggregation. (2010) Nat. Rev. Mol. Cell Biol. 11, 777-788 (Abstract).
Buchberger, A., Sommer, T., Bukau, B. Protein Quality Control in the Cytosol and the Endoplasmic Reticulum: Brothers in Arms. (2010) Mol. Cell 40, 238-252 (Abstract).
Hoffmann, A., Bukau, B., Kramer, G. Structure and function of the molecular chaperone Trigger Factor. Biochim Biophys Acta. (2010) 1803, 650-661 (Abstract).
Andréasson, C., Rampelt, H., Fiaux, J., Druffel-Augustin, S., Bukau, B. The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110. (2010) J Biol Chem. 285, 12445-12453 (Abstract).
Mogk, A., Bukau, B. Cell biology. When the beginning marks the end. (2010) Science 327, 966-967. (no Abstract available).
Winkler, J., Seybert, A., Koenig, L., Pruggnaller, S., Haselmann, U., Sourjik, V., Weiss, M., Frangakis, A.S., Mogk, A., Bukau, B. Quantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing. EMBO J. (2010) 29, 910-923. (Abstract). Comment in: EMBO J. 2010, 29, 869-870.
Haslberger, T., Bukau, B., Mogk, A. Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation. Biochem Cell Biol. (2010) 88, 63-75. (Abstract).
Fiaux, J., Horst, J., Scior, A., Preissler, S., Koplin, A., Bukau, B., Deuerling, E. Structural analysis of the ribosome-associated complex RAC reveals an unusual Hsp70/Hsp40 interaction. J Biol Chem. (2010). 285, 3227-3234. (Abstract).
2009
Hoffmann, A., Bukau, B. Trigger factor finds new jobs and contacts. Nat. Struct. Mol. Biol. (2009) 16, 1006-1008. (No abstract available).
Schmidt, R., Bukau, B., Mogk, A. Principles of general and regulatory proteolysis by AAA+ proteases in Escherichia coli.
Res. Microbiol. (2009) 160, 629-636 (Abstract).
Graf, C., Stankiewicz, M., Kramer, G., Mayer, M.P. Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine. EMBO J. (2009) 28, 602-613 (Abstract).
Rutkowska, A., Beerbaum, M., Rajagopalan, N., Fiaux, J., Schmieder, P., Kramer, G., Oschkinat, H., Bukau, B. Large-scale purification of ribosome nascentchain complexes for biochemical and structural studies. FEBS Lett. (2009) 583, 2407-2413. (Abstract).
Kramer, G., Boehringer, D., Ban, N., Bukau, B. The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins. Nat Struct Mol Biol. (2009) 16, 589-597. (Abstract).
Tessarz, P., Schwarz, M., Mogk, A., Bukau, B. The yeast AAA+ chaperone Hsp104 is part of a network that links the actin cytoskeleton with the inheritance of damaged proteins. Mol Cell Biol. (2009) 29, 3738-3745 (Abstract).
Schmidt, R., Zahn, R., Bukau, B., Mogk, A. ClpS is the recognition component for Escherichia coli substrates of the N-end rule degradation pathway. Mol Microbiol. (2009) 72, 506-517. (Abstract).
Andersson FI, Tryggvesson A, Sharon M, Diemand AV, Classen M, Best C, Schmidt R, Schelin J, Stanne TM, Bukau B, Robinson CV, Witt S, Mogk A, Clarke AK. Structure and function of a novel type of ATP-dependent CLP protease. J. Biol. Chem. (2009) 284, 13519-13532. (Abstract).
Rodriguez F, Arsene-Ploetze F, Rist W, Ruediger S, Schneider-Mergener J, Mayer MP, Bukau B. Molecular basis for regulation of the heat shock transcription factor sigma32 by the DnaK and DnaJ chaperones. Mol Cell (2008) 32, 347-358 (Abstract).
Andreasson C, Fiaux J, Rampelt H, Druffel-Augustin S, Bukau B. Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity. Proc Natl Acad Sci U S A (2008) 105, 16519-16524 (Abstract).
Huber, D. and Bukau, B. DegP: a Protein "Death Star". Structure (2008) 16, 989-990 (Abstract).
Haslberger, T., Zdanowicz, A., Brand, I., Kirstein, J., Turgay, K., Mogk, A., Bukau, B. Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments. Nat. Struct. Mol. Biol. (2008) 15, 641-650 (Abstract).
Merz, F., Boehringer, D., Schaffitzel, D., Preissler, S, Hoffmann, A., Maier, T., Rutkowska, A., Lozza, J., Ban, N., Bukau, B., Deuerling, D. Molecular mechanism and structure of trigger factor bound to the translating ribosome. EMBO J. (2008), 27, 1622-1632 (Abstract).
Sadlish, H., Rampelt, H., Shorter, J., Wegrzyn, R.D., Andreasson, C., Lindquist, S., Bukau, B. Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities. PLoS ONE. (2008) 3, e1763 (Abstract).
Tessarz, P., Mogk, A., Bukau, B. Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation. Mol. Microbiol. (2008), 68, 87-97 (Abstract).
Bingel-Erlenmeyer, R., Kohler, R., Kramer, G., Sandikci, A., Antolic, S., Maier, T., Schaffitzel, C., Wiedmann, B., Bukau, B., Ban., N. A peptide deformylase-ribosome complex reveals mechanism of nascent chain processing. Nature (2008), 452, 108-11 (Abstract).
Erbse, A.H., Wagner, J.N., Truscott, K.N., Spall, S.K., Kirstein, J., Zeth, K., Turgay, K., Mogk, A., Bukau, B., Dougan, D.A. Conserved residues in the N-domain of the AAA+ chaperone ClpA regulate substrate recognition and unfolding. FEBS J. (2008), 275, 1400-10 (Abstract).
Rutkowska, A., Mayer, M.P., Hoffmann, A., Merz, F., Zachmann-Brand, B., Schaffitzel, C., Ban, N., Deuerling, E., Bukau, B. Dynamics of trigger factor interaction with translating ribosomes. J Biol Chem. (2008), 283, 4124-32 (Abstract).
Andreasson, C., Fiaux, J., Rampelt, H., Mayer, M. P., Bukau, B. Hsp110 is a nucleotide-activated exchange factor for Hsp70. J. Biol. Chem. (2008), 283, 8877-84 (Abstract).
Mogk, A., Haslberger, T., Tessarz, P., Bukau, B. Common and specific mechanisms of AAA+ proteins involved in protein quality control. Biochem Soc Trans. (2008), 36(Pt 1):120-125 (Abstract).
2007
de Marco, A., Deuerling, E., Mogk, A., Tomoyasu, T., Bukau, B. Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli. BMC Biotechnol. (2007), 7, 32 (Abstract).
Mogk, A., Schmidt, R., Bukau, B. The N-end rule pathway for regulated proteolysis: prokaryotic and eukaryotic strategies. Trends Cell Biol. (2007), 17, 165-172 (Abstract).
Haslberger, T., Weibezahn, J., Zahn, R., Lee, S., Tsai, F.T.F., Bukau, B., Mogk, A. M-domains couple the ClpB threading motor with the DnaK chaperone activity. Mol. Cell (2007), 25, 247-260 (Abstract).
2006
Vogel, M., Mayer, M.P., Bukau, B. Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker. J Biol Chem. (2006), 281, 38705-38711. (Abstract).
Merz, F., Hoffmann, A., Rutkowska, A., Zachmann-Brand, B., Bukau, B., Deuerling, E. The C-terminal domain of E. coli trigger factor represents the central module of its chaperone activity. J Biol Chem. (2006), 281, 31963-31971 (Abstract).
Rist, W., Graf, C., Bukau, B., Mayer, M.P. Amide hydrogen exchange reveals conformational changes in Hsp70 chaperones important for allosteric regulation. J Biol Chem. (2006), 281, 16493-16501 (Abstract).
Pastore, C., Adinolfi, S., Huynen, M.A., Rybin, V., Martin, S., Mayer, M., Bukau, B., Pastore, A. YfhJ, a molecular adaptor in iron-sulfur cluster formation or a frataxin-like protein? Structure (2006), 14, 857-867 (Abstract).
Raviol, H., Sadlish, H., Rodriguez, F., Mayer, M.P., Bukau, B. Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. EMBO J. (2006), 25, 2510-2518 (Abstract).
Bukau, B., Weissman, J., Horwich, A. Molecular Chaperones and Protein Quality Control. Cell (2006), 125, 443-451 (Abstract).
Kirstein, J., Schlothauer, T., Dougan, D.A., Lilie, H., Tischendorf, G., Mogk, A., Bukau, B., Turgay, K. Adaptor protein controlled oligomerization activates the AAA+ protein ClpC. EMBO J. (2006), 25, 1481-1491 (Abstract).
Erbse, A., Schmidt, R., Bornemann, T., Schneider-Mergener, J., Mogk A., Zahn, R., Dougan, D.A., Bukau, B. ClpS is an essential component of the N-end rule pathway in Escherichia coli. Nature (2006), 439, 753-756. (Abstract).
Hoffmann, A., Merz, F., Rutkowska, A., Zachmann-Brand, B., Deuerling, E., Bukau, B. Trigger factor forms a protective shield for nascent polypeptides at the ribosome. J Biol Chem. (2006). 281, 6539-6545. (Abstract).
Andersson, F.I., Blakytny, R., Kirstein J., Turgay, K., Bukau, B., Mogk, A., Clarke, A.K. Cyanobacterial ClpC/HSP100 protein displays intrinsic chaperone activity. J. Biol. Chem. (2006). 281, 5468-5475. (Abstract).
Vogel, M., Bukau, B., Mayer, M.P. Allosteric regulation of Hsp70 chaperones by a proline switch. Mol. Cell (2006) 21, 359-367. (Abstract).
Raviol, H., Bukau, B., Mayer, M.P. Human and yeast Hsp110 chaperones exhibit functional differences. FEBS Lett. (2006) 580, 168-174. (Abstract).
2005
Schlieker, C., Zentgraf, H., Dersch, P., Mogk, A.. ClpV, a unique Hsp100/Clp member of pathogenic proteobacteria. Biol Chem. (2005) 386, 1115-1127. (Abstract).
Weibezahn, J., Schlieker, C., Tessarz, P., Mogk, A., Bukau, B. Novel insights into the mechanism of chaperone-assisted protein disaggregation. Biol. Chem. (2005) 386, 739-744. (Abstract).
Mayer, M.P., Bukau. B. Hsp70 chaperones: Cellular functions and molecular Mechanism. Cell. Mol. Life Sci. (2005) 62, 670-684 (Abstract).
Mayer, M.P., Bukau, B. Regulation of Hsp70 chaperones by cochaperones. In: Handbook of Protein Folding. Vol. II/I&2 (J. Buchner, T. Kiefhaber, eds.) (2005) 516-562.
Deuerling, E., Rauch, T., Patzelt, H., Bukau, B. The role of Trigger Factor in folding of newly synthesized proteins. In: Handbook of Protein Folding. Vol. II/I&2 (J. Buchner, T. Kiefhaber, eds.) (2005) 459-489.
Rauch, T., Hundley, H.A., Pfund, C., Wegrzyn, R.D., Walter, W., Kramer, G., Kim, S.Y., Craig, E.A., Deuerling, E. Dissecting functional similarities of ribosome-associated chaperones from Saccharomyces cerevisiae and Escherichia coli. Mol Microbiol. (2005) 57, 357-365. (Abstract).
2004
Deuerling, E., Bukau, B. Chaperone-assisted folding of newly synthesized proteins in the cytosol. CRBMB (2004) 39, 261-277. (Abstract).
Schlieker, C., Tews, I., Bukau, B., Mogk, A. Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides. FEBS Lett. (2004), 578:351-356. (Abstract).
Weibezahn, J., Tessarz, P., Schlieker, C., Zahn, R., Maglica, Z., Lee, S., Zentgraf, H., Weber-Ban, E., Dougan, D., Tsai, F.T.F., Mogk, A., Bukau, B. Thermortolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell, (2004) 119(5):653-665. (Abstract).
Comment by A. Horwich in Cell, 2004, 119, 579-581
Ferbitz, L., Maier, T., Patzelt, H., Bukau, B., Deuerling, E., Ban, N. Structure of the Trigger Factor chaperone complex with the ribosome defines the molecular environment of the emerging nascent protein chain Nature (2004) 431, 590-596 (Abstract).
Comment by A. Horwich in Nature. 2004 Sep 30;431(7008):520-2.
Erbse, A., Mayer, M.P., Bukau, B. Mechanism of substrate recognition by Hsp70 chaperones. Biochem. Transactions (2004) 32(Pt 4), 617-621 (Abstract).
Brehmer, D., Gaessler, C., Rist, W., Mayer, M.P., Bukau, B. Influence of GrpE on DnaK-substrate interactions. J. Biol. Chem. (2004) 279, 27957-27964 (Abstract).
Becker, T., Hritz J., Vogel, M., Caliebe, A., Bukau, B., Soll, J., Schleiff, E. Toc12, A Novel Subunit of the Intermembrane Space Preprotein Translocon of Chloroplasts. Mol. Biol. Cell (2004) 15, 5130-3144 (Abstract).
Schlieker, C., Weibezahn, J., Patzelt, H., Strub, C., Zeth, K., Erbse, A., Schneider-Mergener, J., Chin, J.W., Schultz, P.G., Bukau, B., Mogk, A. Substrate recognition by the AAA+ chaperone ClpB. Nat. Struct. Mol. Biol. (2004) 11, 607-615 (Abstract).
Buskiewicz, I., Deuerling, E., Gu, S.-Q., Joeckel, J., Rodnina, M.V., Bukau, B., Wintermeyer, W. Trigger factor binds to ribosome-SRP complexes and is excluded by binding of the SRP receptor. Proc. Soc. Natl. USA (2004) 101, 7902-7906 (Abstract).
Kramer, G., Rutkowska, A., Wegrzyn, R.D., Patzelt, H., Kurz, T.A. , Merz, F., Rauch, T., Vorderwuelbecke, S., Deuerling, E., Bukau, B. Functional dissection of Escherichia coli Trigger Factor: Unraveling the function of individual domains. J. Bacteriol. (2004) 186, 3777-3784 (Abstract).
Schlieker, C., Mogk, A,. Bukau, B. A PDZ switch for a cellular stress response. Cell (2004) 117, 417-419 (Abstract).
Mogk, A., Dougan, D., Weibezahn, J., Schlieker, C., Turgay, K., Bukau, B. Broad yet high substrate specificity: the challenge of AAA+ proteins. J. Struct. Biol. (2004) 146, 90-98 (Abstract).
Kramer, G., Patzelt, H., Rauch, T., Kurz, T.A., Vorderwulbecke, S., Bukau, B., Deuerling, E. Trigger factor's peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli. J. Biol. Chem. (2004) 279, 14165- 14170 (Abstract).
Weibezahn, J., Bukau, B., Mogk, A. Unscrambling an egg: protein disaggregation by AAA+ proteins. Microb. Cell. Fact. (2004) 3, 1-12 (Abstract).
Vorderwuelbecke, S., Kramer, G., Merz, F., Kurz, T.A., Rauch, T., Zachmann-Brand, B., Bukau, B., Deuerling, E. Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK. FEBS Lett. (2004) 559, 181-187 (Abstract).
Mogk., A. and Bukau, B. Molecular Chaperones: Structure of a Protein Disaggregase. Curr. Biol. (2004) 14, R78-R80 (Abstract).
Nikolay, R., Wiederkehr, T., Rist, W., Kramer, G., Mayer, M.P., Bukau, B. Dimerization of the Human E3 Ligase CHIP via a Coiled-coil Domain Is Essential for Its Activity. J. Biol. Chem. (2004) 279, 2673-2678 (Abstract).
