Bernd Bukau - Publications

Affiliations: 
Molecular Biology University of Heidelberg, Heidelberg, Baden-Württemberg, Germany 
Area:
Protein folding and quality control; Molecular chaperones and proteases; Cellular stress response
Website:
http://www.zmbh.uni-heidelberg.de/bukau/

211 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
2019 Ho CT, Grousl T, Shatz O, Jawed A, Ruger-Herreros C, Semmelink M, Zahn R, Richter K, Bukau B, Mogk A. Cellular sequestrases maintain basal Hsp70 capacity ensuring balanced proteostasis. Nature Communications. 10: 4851. PMID 31649258 DOI: 10.1038/s41467-019-12868-1  0.52
2019 Deville C, Franke K, Mogk A, Bukau B, Saibil HR. Two-Step Activation Mechanism of the ClpB Disaggregase for Sequential Substrate Threading by the Main ATPase Motor. Cell Reports. 27: 3433-3446.e4. PMID 31216466 DOI: 10.1016/j.celrep.2019.05.075  0.52
2019 Maurer M, Linder D, Franke KB, Jäger J, Taylor G, Gloge F, Gremer S, Le Breton L, Mayer MP, Weber-Ban E, Carroni M, Bukau B, Mogk A. Toxic Activation of an AAA+ Protease by the Antibacterial Drug Cyclomarin A. Cell Chemical Biology. PMID 31204287 DOI: 10.1016/j.chembiol.2019.05.008  0.52
2019 Mogk A, Ruger-Herreros C, Bukau B. Cellular Functions and Mechanisms of Action of Small Heat Shock Proteins. Annual Review of Microbiology. PMID 31091419 DOI: 10.1146/annurev-micro-020518-115515  0.52
2018 Grousl T, Ungelenk S, Miller S, Ho CT, Khokhrina M, Mayer MP, Bukau B, Mogk A. A prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins. The Journal of Cell Biology. PMID 29362223 DOI: 10.1083/jcb.201708116  0.52
2018 Mogk A, Bukau B, Kampinga HH. Cellular Handling of Protein Aggregates by Disaggregation Machines. Molecular Cell. 69: 214-226. PMID 29351843 DOI: 10.1016/j.molcel.2018.01.004  0.52
2017 Carroni M, Franke KB, Maurer M, Jäger J, Hantke I, Gloge F, Linder D, Gremer S, Turgay K, Bukau B, Mogk A. Regulatory coiled-coil domains promote head-to-head assemblies of AAA+ chaperones essential for tunable activity control. Elife. 6. PMID 29165246 DOI: 10.7554/eLife.30120  0.52
2017 Deville C, Carroni M, Franke KB, Topf M, Bukau B, Mogk A, Saibil HR. Structural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase. Science Advances. 3: e1701726. PMID 28798962 DOI: 10.1126/sciadv.1701726  0.52
2017 Franke KB, Bukau B, Mogk A. Mutant Analysis Reveals Allosteric Regulation of ClpB Disaggregase. Frontiers in Molecular Biosciences. 4: 6. PMID 28275610 DOI: 10.3389/fmolb.2017.00006  0.52
2017 Żwirowski S, Kłosowska A, Obuchowski I, Nillegoda NB, Piróg A, Ziętkiewicz S, Bukau B, Mogk A, Liberek K. Hsp70 displaces small heat shock proteins from aggregates to initiate protein refolding. The Embo Journal. PMID 28219929 DOI: 10.15252/embj.201593378  0.52
2017 Mogk A, Bukau B. Role of sHsps in organizing cytosolic protein aggregation and disaggregation. Cell Stress & Chaperones. PMID 28120291 DOI: 10.1007/s12192-017-0762-4  0.52
2016 Ungelenk S, Moayed F, Ho CT, Grousl T, Scharf A, Mashaghi A, Tans S, Mayer MP, Mogk A, Bukau B. Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding. Nature Communications. 7: 13673. PMID 27901028 DOI: 10.1038/ncomms13673  0.52
2016 Goerke S, Milde KS, Bukowiecki R, Kunz P, Klika KD, Wiglenda T, Mogk A, Wanker EE, Bukau B, Ladd ME, Bachert P, Zaiss M. Aggregation-induced changes in the chemical exchange saturation transfer (CEST) signals of proteins. Nmr in Biomedicine. PMID 27859838 DOI: 10.1002/nbm.3665  0.52
2016 Kummer E, Szlachcic A, Franke KB, Ungelenk S, Bukau B, Mogk A. Bacterial and yeast AAA+ disaggregases ClpB and Hsp104 operate through conserved mechanism involving cooperation with Hsp70. Journal of Molecular Biology. PMID 27616763 DOI: 10.1016/j.jmb.2016.09.003  0.52
2016 Schibich D, Gloge F, Pöhner I, Björkholm P, Wade RC, von Heijne G, Bukau B, Kramer G. Global profiling of SRP interaction with nascent polypeptides. Nature. PMID 27487212 DOI: 10.1038/nature19070  1
2016 Yonashiro R, Tahara EB, Bengtson MH, Khokhrina M, Lorenz H, Chen KC, Kigoshi-Tansho Y, Savas JN, Yates JR, Kay SA, Craig EA, Mogk A, Bukau B, Joazeiro CA. The Rqc2/Tae2 subunit of the ribosome-associated quality control (RQC) complex marks ribosome-stalled nascent polypeptide chains for aggregation. Elife. 5. PMID 26943317 DOI: 10.7554/eLife.11794  0.52
2016 Nilsson OB, Müller-Lucks A, Kramer G, Bukau B, von Heijne G. Trigger factor reduces the force exerted on the nascent chain by a cotranslationally folding protein. Journal of Molecular Biology. PMID 26906929 DOI: 10.1016/j.jmb.2016.02.014  1
2016 Nissley DA, Sharma AK, Ahmed N, Friedrich UA, Kramer G, Bukau B, O'Brien EP. Accurate prediction of cellular co-translational folding indicates proteins can switch from post- to co-translational folding. Nature Communications. 7: 10341. PMID 26887592 DOI: 10.1038/ncomms10341  1
2015 Sharma AK, Bukau B, O'Brien EP. The physical origins of codon positions that strongly influence cotranslational folding: A framework for controlling nascent-protein folding. Journal of the American Chemical Society. PMID 26716464 DOI: 10.1021/jacs.5b08145  1
2015 Khmelinskii A, Meurer M, Ho CT, Besenbeck B, Füller J, Lemberg MK, Bukau B, Mogk A, Knop M. Incomplete proteasomal degradation of green fluorescent proteins in the context of tandem fluorescent protein timers. Molecular Biology of the Cell. PMID 26609072 DOI: 10.1091/mbc.E15-07-0525  1
2015 Cherkasov V, Grousl T, Theer P, Vainshtein Y, Gläßer C, Mongis C, Kramer G, Stoecklin G, Knop M, Mogk A, Bukau B. Systemic control of protein synthesis through sequestration of translation and ribosome biogenesis factors during severe heat stress. Febs Letters. PMID 26484595 DOI: 10.1016/j.febslet.2015.10.010  1
2015 Shieh YW, Minguez P, Bork P, Auburger JJ, Guilbride DL, Kramer G, Bukau B. Operon structure and cotranslational subunit association direct protein assembly in bacteria. Science (New York, N.Y.). 350: 678-80. PMID 26405228 DOI: 10.1126/science.aac8171  1
2015 Kityk R, Vogel M, Schlecht R, Bukau B, Mayer MP. Pathways of allosteric regulation in Hsp70 chaperones. Nature Communications. 6: 8308. PMID 26383706 DOI: 10.1038/ncomms9308  1
2015 Gao X, Carroni M, Nussbaum-Krammer C, Mogk A, Nillegoda NB, Szlachcic A, Guilbride DL, Saibil HR, Mayer MP, Bukau B. Human Hsp70 Disaggregase Reverses Parkinson's-Linked α-Synuclein Amyloid Fibrils. Molecular Cell. 59: 781-93. PMID 26300264 DOI: 10.1016/j.molcel.2015.07.012  1
2015 Nillegoda NB, Kirstein J, Szlachcic A, Berynskyy M, Stank A, Stengel F, Arnsburg K, Gao X, Scior A, Aebersold R, Guilbride DL, Wade RC, Morimoto RI, Mayer MP, Bukau B. Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation. Nature. 524: 247-51. PMID 26245380 DOI: 10.1038/nature14884  1
2015 Mogk A, Kummer E, Bukau B. Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregation. Frontiers in Molecular Biosciences. 2: 22. PMID 26042222 DOI: 10.3389/fmolb.2015.00022  0.52
2015 Goerke S, Zaiss M, Kunz P, Klika KD, Windschuh JD, Mogk A, Bukau B, Ladd ME, Bachert P. Signature of protein unfolding in chemical exchange saturation transfer imaging. Nmr in Biomedicine. 28: 906-13. PMID 26010522 DOI: 10.1002/nbm.3317  1
2015 Kramer G, Guilbride DL, Bukau B. Cell Biology. Finding nascent proteins the right home. Science (New York, N.Y.). 348: 182-3. PMID 25859030 DOI: 10.1126/science.aab1335  1
2015 Suresh HG, da Silveira Dos Santos AX, Kukulski W, Tyedmers J, Riezman H, Bukau B, Mogk A. Prolonged starvation drives reversible sequestration of lipid biosynthetic enzymes and organelle reorganization in Saccharomyces cerevisiae. Molecular Biology of the Cell. 26: 1601-15. PMID 25761633 DOI: 10.1091/mbc.E14-11-1559  1
2015 Miller SB, Mogk A, Bukau B. Spatially organized aggregation of misfolded proteins as cellular stress defense strategy. Journal of Molecular Biology. 427: 1564-74. PMID 25681695 DOI: 10.1016/j.jmb.2015.02.006  1
2015 Miller SB, Ho CT, Winkler J, Khokhrina M, Neuner A, Mohamed MY, Guilbride DL, Richter K, Lisby M, Schiebel E, Mogk A, Bukau B. Compartment-specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition. The Embo Journal. 34: 778-97. PMID 25672362 DOI: 10.15252/embj.201489524  1
2014 Mogk A, Bukau B. Mitochondria tether protein trash to rejuvenate cellular environments. Cell. 159: 471-2. PMID 25417098 DOI: 10.1016/j.cell.2014.10.007  1
2014 Hsieh TY, Nillegoda NB, Tyedmers J, Bukau B, Mogk A, Kramer G. Monitoring protein misfolding by site-specific labeling of proteins in vivo. Plos One. 9: e99395. PMID 24915041 DOI: 10.1371/journal.pone.0099395  1
2014 Carroni M, Kummer E, Oguchi Y, Wendler P, Clare DK, Sinning I, Kopp J, Mogk A, Bukau B, Saibil HR. Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. Elife. 3: e02481. PMID 24843029 DOI: 10.7554/eLife.02481  1
2014 Gloge F, Becker AH, Kramer G, Bukau B. Co-translational mechanisms of protein maturation. Current Opinion in Structural Biology. 24: 24-33. PMID 24721450 DOI: 10.1016/j.sbi.2013.11.004  1
2013 Cherkasov V, Hofmann S, Druffel-Augustin S, Mogk A, Tyedmers J, Stoecklin G, Bukau B. Coordination of translational control and protein homeostasis during severe heat stress. Current Biology : Cb. 23: 2452-62. PMID 24291094 DOI: 10.1016/j.cub.2013.09.058  1
2013 Schlecht R, Scholz SR, Dahmen H, Wegener A, Sirrenberg C, Musil D, Bomke J, Eggenweiler HM, Mayer MP, Bukau B. Functional analysis of Hsp70 inhibitors. Plos One. 8: e78443. PMID 24265689 DOI: 10.1371/journal.pone.0078443  1
2013 Stoecklin G, Bukau B. Telling right from wrong in life - cellular quality control. Nature Reviews. Molecular Cell Biology. 14: 613-5. PMID 24199228 DOI: 10.1038/nrm3662  1
2013 Becker AH, Oh E, Weissman JS, Kramer G, Bukau B. Selective ribosome profiling as a tool for studying the interaction of chaperones and targeting factors with nascent polypeptide chains and ribosomes. Nature Protocols. 8: 2212-39. PMID 24136347 DOI: 10.1038/nprot.2013.133  1
2013 Mashaghi A, Kramer G, Bechtluft P, Zachmann-Brand B, Driessen AJ, Bukau B, Tans SJ. Reshaping of the conformational search of a protein by the chaperone trigger factor. Nature. 500: 98-101. PMID 23831649 DOI: 10.1038/nature12293  1
2013 Sandikci A, Gloge F, Martinez M, Mayer MP, Wade R, Bukau B, Kramer G. Dynamic enzyme docking to the ribosome coordinates N-terminal processing with polypeptide folding. Nature Structural & Molecular Biology. 20: 843-50. PMID 23770820 DOI: 10.1038/nsmb.2615  1
2013 Tariq M, Wegrzyn R, Anwar S, Bukau B, Paro R. Drosophila GAGA factor polyglutamine domains exhibit prion-like behavior. Bmc Genomics. 14: 374. PMID 23731888 DOI: 10.1186/1471-2164-14-374  1
2013 Kummer E, Oguchi Y, Seyffer F, Bukau B, Mogk A. Mechanism of Hsp104/ClpB inhibition by prion curing Guanidinium hydrochloride. Febs Letters. 587: 810-7. PMID 23416293 DOI: 10.1016/j.febslet.2013.02.011  1
2012 Oguchi Y, Kummer E, Seyffer F, Berynskyy M, Anstett B, Zahn R, Wade RC, Mogk A, Bukau B. A tightly regulated molecular toggle controls AAA+ disaggregase. Nature Structural & Molecular Biology. 19: 1338-46. PMID 23160353 DOI: 10.1038/nsmb.2441  1
2012 Seyffer F, Kummer E, Oguchi Y, Winkler J, Kumar M, Zahn R, Sourjik V, Bukau B, Mogk A. Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces. Nature Structural & Molecular Biology. 19: 1347-55. PMID 23160352 DOI: 10.1038/nsmb.2442  1
2012 Rampelt H, Kirstein-Miles J, Nillegoda NB, Chi K, Scholz SR, Morimoto RI, Bukau B. Metazoan Hsp70 machines use Hsp110 to power protein disaggregation. The Embo Journal. 31: 4221-35. PMID 22990239 DOI: 10.1038/emboj.2012.264  1
2012 Hoffmann A, Becker AH, Zachmann-Brand B, Deuerling E, Bukau B, Kramer G. Concerted action of the ribosome and the associated chaperone trigger factor confines nascent polypeptide folding. Molecular Cell. 48: 63-74. PMID 22921937 DOI: 10.1016/j.molcel.2012.07.018  1
2012 Hofmann S, Cherkasova V, Bankhead P, Bukau B, Stoecklin G. Translation suppression promotes stress granule formation and cell survival in response to cold shock. Molecular Biology of the Cell. 23: 3786-800. PMID 22875991 DOI: 10.1091/mbc.E12-04-0296  1
2012 Winkler J, Tyedmers J, Bukau B, Mogk A. Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. The Journal of Cell Biology. 198: 387-404. PMID 22869599 DOI: 10.1083/jcb.201201074  1
2012 Winkler J, Tyedmers J, Bukau B, Mogk A. Chaperone networks in protein disaggregation and prion propagation. Journal of Structural Biology. 179: 152-60. PMID 22580344 DOI: 10.1016/j.jsb.2012.05.002  1
2011 Oh E, Becker AH, Sandikci A, Huber D, Chaba R, Gloge F, Nichols RJ, Typas A, Gross CA, Kramer G, Weissman JS, Bukau B. Selective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivo. Cell. 147: 1295-308. PMID 22153074 DOI: 10.1016/j.cell.2011.10.044  1
2011 Specht S, Miller SB, Mogk A, Bukau B. Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae. The Journal of Cell Biology. 195: 617-29. PMID 22065637 DOI: 10.1083/jcb.201106037  1
2011 Rampelt H, Mayer MP, Bukau B. Nucleotide exchange factors for Hsp70 chaperones. Methods in Molecular Biology (Clifton, N.J.). 787: 83-91. PMID 21898229 DOI: 10.1007/978-1-61779-295-3_7  1
2011 Kohl C, Tessarz P, von der Malsburg K, Zahn R, Bukau B, Mogk A. Cooperative and independent activities of Sgt2 and Get5 in the targeting of tail-anchored proteins. Biological Chemistry. 392: 601-8. PMID 21619481 DOI: 10.1515/BC.2011.066  1
2011 Mogk A, Huber D, Bukau B. Integrating protein homeostasis strategies in prokaryotes. Cold Spring Harbor Perspectives in Biology. 3. PMID 21441580 DOI: 10.1101/cshperspect.a004366  1
2011 Huber D, Rajagopalan N, Preissler S, Rocco MA, Merz F, Kramer G, Bukau B. SecA interacts with ribosomes in order to facilitate posttranslational translocation in bacteria. Molecular Cell. 41: 343-53. PMID 21292166 DOI: 10.1016/j.molcel.2010.12.028  1
2011 Schlecht R, Erbse AH, Bukau B, Mayer MP. Mechanics of Hsp70 chaperones enables differential interaction with client proteins. Nature Structural & Molecular Biology. 18: 345-51. PMID 21278757 DOI: 10.1038/nsmb.2006  1
2010 Buchberger A, Bukau B, Sommer T. Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms. Molecular Cell. 40: 238-52. PMID 20965419 DOI: 10.1016/j.molcel.2010.10.001  1
2010 Tyedmers J, Mogk A, Bukau B. Cellular strategies for controlling protein aggregation. Nature Reviews. Molecular Cell Biology. 11: 777-88. PMID 20944667 DOI: 10.1038/nrm2993  1
2010 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. The Journal of Biological Chemistry. 285: 12445-53. PMID 20177057 DOI: 10.1074/jbc.M109.096735  1
2010 Mogk A, Bukau B. Cell biology. When the beginning marks the end. Science (New York, N.Y.). 327: 966-7. PMID 20167776 DOI: 10.1126/science.1187274  1
2010 Hoffmann A, Bukau B, Kramer G. Structure and function of the molecular chaperone Trigger Factor. Biochimica Et Biophysica Acta. 1803: 650-61. PMID 20132842 DOI: 10.1016/j.bbamcr.2010.01.017  1
2010 Haslberger T, Bukau B, Mogk A. Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 88: 63-75. PMID 20130680 DOI: 10.1139/o09-118  1
2010 Winkler J, Seybert A, König L, Pruggnaller S, Haselmann U, Sourjik V, Weiss M, Frangakis AS, Mogk A, Bukau B. Quantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing. The Embo Journal. 29: 910-23. PMID 20094032 DOI: 10.1038/emboj.2009.412  1
2010 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. The Journal of Biological Chemistry. 285: 3227-34. PMID 19920147 DOI: 10.1074/jbc.M109.075804  1
2009 Hoffmann A, Bukau B. Trigger factor finds new jobs and contacts. Nature Structural & Molecular Biology. 16: 1006-8. PMID 19809489 DOI: 10.1038/nsmb1009-1006  1
2009 Schmidt R, Bukau B, Mogk A. Principles of general and regulatory proteolysis by AAA+ proteases in Escherichia coli. Research in Microbiology. 160: 629-36. PMID 19781640 DOI: 10.1016/j.resmic.2009.08.018  1
2009 Rutkowska A, Beerbaum M, Rajagopalan N, Fiaux J, Schmieder P, Kramer G, Oschkinat H, Bukau B. Large-scale purification of ribosome-nascent chain complexes for biochemical and structural studies. Febs Letters. 583: 2407-13. PMID 19560460 DOI: 10.1016/j.febslet.2009.06.041  1
2009 Kramer G, Boehringer D, Ban N, Bukau B. The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins. Nature Structural & Molecular Biology. 16: 589-97. PMID 19491936 DOI: 10.1038/nsmb.1614  1
2009 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. Molecular and Cellular Biology. 29: 3738-45. PMID 19398583 DOI: 10.1128/MCB.00201-09  1
2009 Schmidt R, Zahn R, Bukau B, Mogk A. ClpS is the recognition component for Escherichia coli substrates of the N-end rule degradation pathway. Molecular Microbiology. 72: 506-17. PMID 19317833 DOI: 10.1111/j.1365-2958.2009.06666.x  1
2009 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. The Journal of Biological Chemistry. 284: 13519-32. PMID 19237538 DOI: 10.1074/jbc.M809588200  1
2008 Rodriguez F, Arsène-Ploetze F, Rist W, Rüdiger 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. Molecular Cell. 32: 347-58. PMID 18995833 DOI: 10.1016/j.molcel.2008.09.016  1
2008 Andréasson 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. Proceedings of the National Academy of Sciences of the United States of America. 105: 16519-24. PMID 18948593 DOI: 10.1073/pnas.0804187105  1
2008 Huber D, Bukau B. DegP: a Protein "Death Star". Structure (London, England : 1993). 16: 989-90. PMID 18611371 DOI: 10.1016/j.str.2008.06.004  1
2008 Merz F, Boehringer D, Schaffitzel C, Preissler S, Hoffmann A, Maier T, Rutkowska A, Lozza J, Ban N, Bukau B, Deuerling E. Molecular mechanism and structure of Trigger Factor bound to the translating ribosome. The Embo Journal. 27: 1622-32. PMID 18497744 DOI: 10.1038/emboj.2008.89  1
2008 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. Nature Structural & Molecular Biology. 15: 641-50. PMID 18488042 DOI: 10.1038/nsmb.1425  1
2008 Sadlish H, Rampelt H, Shorter J, Wegrzyn RD, Andréasson C, Lindquist S, Bukau B. Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities. Plos One. 3: e1763. PMID 18335038 DOI: 10.1371/journal.pone.0001763  1
2008 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. Molecular Microbiology. 68: 87-97. PMID 18312264 DOI: 10.1111/j.1365-2958.2008.06135.x  1
2008 Bingel-Erlenmeyer R, Kohler R, Kramer G, Sandikci A, Antoli? S, Maier T, Schaffitzel C, Wiedmann B, Bukau B, Ban N. A peptide deformylase-ribosome complex reveals mechanism of nascent chain processing. Nature. 452: 108-11. PMID 18288106 DOI: 10.1038/nature06683  1
2008 Erbse AH, Wagner JN, Truscott KN, Spall SK, Kirstein J, Zeth K, Turgay K, Mogk A, Bukau B, Dougan DA. Conserved residues in the N-domain of the AAA+ chaperone ClpA regulate substrate recognition and unfolding. The Febs Journal. 275: 1400-10. PMID 18279386 DOI: 10.1111/j.1742-4658.2008.06304.x  1
2008 Andréasson C, Fiaux J, Rampelt H, Mayer MP, Bukau B. Hsp110 is a nucleotide-activated exchange factor for Hsp70. The Journal of Biological Chemistry. 283: 8877-84. PMID 18218635 DOI: 10.1074/jbc.M710063200  1
2008 Mogk A, Haslberger T, Tessarz P, Bukau B. Common and specific mechanisms of AAA+ proteins involved in protein quality control. Biochemical Society Transactions. 36: 120-5. PMID 18208398 DOI: 10.1042/BST0360120  1
2008 Rutkowska A, Mayer MP, Hoffmann A, Merz F, Zachmann-Brand B, Schaffitzel C, Ban N, Deuerling E, Bukau B. Dynamics of trigger factor interaction with translating ribosomes. The Journal of Biological Chemistry. 283: 4124-32. PMID 18045873 DOI: 10.1074/jbc.M708294200  1
2008 Mayer MP, Bukau B. Regulation of Hsp70 Chaperones by Co-chaperones Protein Folding Handbook. 2: 516-562. DOI: 10.1002/9783527619498.ch48  1
2008 Deuerling E, Rauch T, Patzelt H, Bukau B. The Role of Trigger Factor in Folding of Newly Synthesized Proteins Protein Folding Handbook. 2: 459-489. DOI: 10.1002/9783527619498.ch46  1
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 Biotechnology. 7: 32. PMID 17565681 DOI: 10.1186/1472-6750-7-32  1
2007 Mogk A, Schmidt R, Bukau B. The N-end rule pathway for regulated proteolysis: prokaryotic and eukaryotic strategies. Trends in Cell Biology. 17: 165-72. PMID 17306546 DOI: 10.1016/j.tcb.2007.02.001  1
2007 Haslberger T, Weibezahn J, Zahn R, Lee S, Tsai FT, Bukau B, Mogk A. M domains couple the ClpB threading motor with the DnaK chaperone activity. Molecular Cell. 25: 247-60. PMID 17244532 DOI: 10.1016/j.molcel.2006.11.008  1
2006 Vogel M, Mayer MP, Bukau B. Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker. The Journal of Biological Chemistry. 281: 38705-11. PMID 17052976 DOI: 10.1074/jbc.M609020200  1
2006 Merz F, Hoffmann A, Rutkowska A, Zachmann-Brand B, Bukau B, Deuerling E. The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity. The Journal of Biological Chemistry. 281: 31963-71. PMID 16926148 DOI: 10.1074/jbc.M605164200  1
2006 Pastore C, Adinolfi S, Huynen MA, 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 (London, England : 1993). 14: 857-67. PMID 16698547 DOI: 10.1016/j.str.2006.02.010  1
2006 Raviol H, Sadlish H, Rodriguez F, Mayer MP, Bukau B. Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. The Embo Journal. 25: 2510-8. PMID 16688211 DOI: 10.1038/sj.emboj.7601139  1
2006 Bukau B, Weissman J, Horwich A. Molecular chaperones and protein quality control. Cell. 125: 443-51. PMID 16678092 DOI: 10.1016/j.cell.2006.04.014  1
2006 Rist W, Graf C, Bukau B, Mayer MP. Amide hydrogen exchange reveals conformational changes in hsp70 chaperones important for allosteric regulation. The Journal of Biological Chemistry. 281: 16493-501. PMID 16613854 DOI: 10.1074/jbc.M600847200  1
2006 Kirstein J, Schlothauer T, Dougan DA, Lilie H, Tischendorf G, Mogk A, Bukau B, Turgay K. Adaptor protein controlled oligomerization activates the AAA+ protein ClpC. The Embo Journal. 25: 1481-91. PMID 16525504 DOI: 10.1038/sj.emboj.7601042  1
2006 Erbse A, Schmidt R, Bornemann T, Schneider-Mergener J, Mogk A, Zahn R, Dougan DA, Bukau B. ClpS is an essential component of the N-end rule pathway in Escherichia coli. Nature. 439: 753-6. PMID 16467841 DOI: 10.1038/nature04412  1
2006 Vogel M, Bukau B, Mayer MP. Allosteric regulation of Hsp70 chaperones by a proline switch. Molecular Cell. 21: 359-67. PMID 16455491 DOI: 10.1016/j.molcel.2005.12.017  1
2006 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. The Journal of Biological Chemistry. 281: 6539-45. PMID 16407311 DOI: 10.1074/jbc.M512345200  1
2006 Raviol H, Bukau B, Mayer MP. Human and yeast Hsp110 chaperones exhibit functional differences. Febs Letters. 580: 168-74. PMID 16364315 DOI: 10.1016/j.febslet.2005.11.069  1
2006 Andersson FI, Blakytny R, Kirstein J, Turgay K, Bukau B, Mogk A, Clarke AK. Cyanobacterial ClpC/HSP100 protein displays intrinsic chaperone activity. The Journal of Biological Chemistry. 281: 5468-75. PMID 16361263 DOI: 10.1074/jbc.M509661200  1
2005 Weibezahn J, Schlieker C, Tessarz P, Mogk A, Bukau B. Novel insights into the mechanism of chaperone-assisted protein disaggregation. Biological Chemistry. 386: 739-44. PMID 16201868 DOI: 10.1515/BC.2005.086  1
2005 Vorderwülbecke S, Kramer G, Merz F, Kurz TA, Rauch T, Zachmann-Brand B, Bukau B, Deuerling E. Low temperature of GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor DnaK. Febs Letters. 579: 181-7. PMID 16021693  1
2005 Bukau B. Ribosomes catch Hsp70s. Nature Structural & Molecular Biology. 12: 472-3. PMID 15933729 DOI: 10.1038/nsmb0605-472  1
2005 Mayer MP, Bukau B. Hsp70 chaperones: cellular functions and molecular mechanism. Cellular and Molecular Life Sciences : Cmls. 62: 670-84. PMID 15770419 DOI: 10.1007/s00018-004-4464-6  1
2004 Deuerling E, Bukau B. Chaperone-assisted folding of newly synthesized proteins in the cytosol. Critical Reviews in Biochemistry and Molecular Biology. 39: 261-77. PMID 15763705 DOI: 10.1080/10409230490892496  1
2004 Schlieker C, Tews I, Bukau B, Mogk A. Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides. Febs Letters. 578: 351-6. PMID 15589844 DOI: 10.1016/j.febslet.2004.11.051  1
2004 Weibezahn J, Tessarz P, Schlieker C, Zahn R, Maglica Z, Lee S, Zentgraf H, Weber-Ban EU, Dougan DA, Tsai FT, Mogk A, Bukau B. Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell. 119: 653-65. PMID 15550247 DOI: 10.1016/j.cell.2004.11.027  1
2004 Ferbitz L, Maier T, Patzelt H, Bukau B, Deuerling E, Ban N. Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins. Nature. 431: 590-6. PMID 15334087 DOI: 10.1038/nature02899  1
2004 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. Molecular Biology of the Cell. 15: 5130-44. PMID 15317846 DOI: 10.1091/mbc.E04-05-0405  1
2004 Erbse A, Mayer MP, Bukau B. Mechanism of substrate recognition by Hsp70 chaperones. Biochemical Society Transactions. 32: 617-21. PMID 15270690 DOI: 10.1042/BST0320617  1
2004 Schlieker C, Weibezahn J, Patzelt H, Tessarz P, Strub C, Zeth K, Erbse A, Schneider-Mergener J, Chin JW, Schultz PG, Bukau B, Mogk A. Substrate recognition by the AAA+ chaperone ClpB. Nature Structural & Molecular Biology. 11: 607-15. PMID 15208691 DOI: 10.1038/nsmb787  1
2004 Kramer G, Rutkowska A, Wegrzyn RD, Patzelt H, Kurz TA, Merz F, Rauch T, Vorderwülbecke S, Deuerling E, Bukau B. Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains. Journal of Bacteriology. 186: 3777-84. PMID 15175291 DOI: 10.1128/JB.186.12.3777-3784.2004  1
2004 Buskiewicz I, Deuerling E, Gu SQ, Jöckel J, Rodnina MV, Bukau B, Wintermeyer W. Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor. Proceedings of the National Academy of Sciences of the United States of America. 101: 7902-6. PMID 15148364 DOI: 10.1073/pnas.0402231101  1
2004 Schlieker C, Mogk A, Bukau B. A PDZ switch for a cellular stress response. Cell. 117: 417-9. PMID 15137934 DOI: 10.1016/S0092-8674(04)00453-2  1
2004 Brehmer D, Gässler C, Rist W, Mayer MP, Bukau B. Influence of GrpE on DnaK-substrate interactions. The Journal of Biological Chemistry. 279: 27957-64. PMID 15102842 DOI: 10.1074/jbc.M403558200  1
2004 Mogk A, Dougan D, Weibezahn J, Schlieker C, Turgay K, Bukau B. Broad yet high substrate specificity: the challenge of AAA+ proteins. Journal of Structural Biology. 146: 90-8. PMID 15037240 DOI: 10.1016/j.jsb.2003.10.009  1
2004 Vorderwülbecke S, Kramer G, Merz F, Kurz TA, 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 Letters. 559: 181-7. PMID 14960329 DOI: 10.1016/S0014-5793(04)00052-3  1
2004 Mogk A, Bukau B. Molecular chaperones: structure of a protein disaggregase. Current Biology : Cb. 14: R78-80. PMID 14738756 DOI: 10.1016/j.cub.2003.12.051  1
2004 Kramer G, Patzelt H, Rauch T, Kurz TA, Vorderwülbecke S, Bukau B, Deuerling E. Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli. The Journal of Biological Chemistry. 279: 14165-70. PMID 14729669 DOI: 10.1074/jbc.M313635200  1
2004 Weibezahn J, Bukau B, Mogk A. Unscrambling an egg: protein disaggregation by AAA+ proteins. Microbial Cell Factories. 3: 1. PMID 14728719 DOI: 10.1186/1475-2859-3-1  1
2004 Nikolay R, Wiederkehr T, Rist W, Kramer G, Mayer MP, Bukau B. Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity. The Journal of Biological Chemistry. 279: 2673-8. PMID 14610072 DOI: 10.1074/jbc.M311112200  1
2003 Mogk A, Deuerling E, Vorderwülbecke S, Vierling E, Bukau B. Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation. Molecular Microbiology. 50: 585-95. PMID 14617181 DOI: 10.1046/j.1365-2958.2003.03710.x  1
2003 Strub C, Schlieker C, Bukau B, Mogk A. Poly-L-lysine enhances the protein disaggregation activity of ClpB. Febs Letters. 553: 125-30. PMID 14550559 DOI: 10.1016/S0014-5793(03)00985-2  1
2003 Dougan DA, Weber-Ban E, Bukau B. Targeted delivery of an ssrA-tagged substrate by the adaptor protein SspB to its cognate AAA+ protein ClpX. Molecular Cell. 12: 373-80. PMID 14536077 DOI: 10.1016/j.molcel.2003.08.012  1
2003 Rist W, Jørgensen TJ, Roepstorff P, Bukau B, Mayer MP. Mapping temperature-induced conformational changes in the Escherichia coli heat shock transcription factor sigma 32 by amide hydrogen exchange. The Journal of Biological Chemistry. 278: 51415-21. PMID 14504287 DOI: 10.1074/jbc.M307160200  1
2003 Hengge R, Bukau B. Proteolysis in prokaryotes: protein quality control and regulatory principles. Molecular Microbiology. 49: 1451-62. PMID 12950913 DOI: 10.1046/j.1365-2958.2003.03693.x  1
2003 Weibezahn J, Schlieker C, Bukau B, Mogk A. Characterization of a trap mutant of the AAA+ chaperone ClpB. The Journal of Biological Chemistry. 278: 32608-17. PMID 12805357 DOI: 10.1074/jbc.M303653200  1
2003 Mogk A, Schlieker C, Friedrich KL, Schönfeld HJ, Vierling E, Bukau B. Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK. The Journal of Biological Chemistry. 278: 31033-42. PMID 12788951 DOI: 10.1074/jbc.M303587200  1
2003 Mogk A, Schlieker C, Strub C, Rist W, Weibezahn J, Bukau B. Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity. The Journal of Biological Chemistry. 278: 17615-24. PMID 12624113 DOI: 10.1074/jbc.M209686200  1
2003 Deuerling E, Patzelt H, Vorderwülbecke S, Rauch T, Kramer G, Schaffitzel E, Mogk A, Schulze-Specking A, Langen H, Bukau B. Trigger Factor and DnaK possess overlapping substrate pools and binding specificities. Molecular Microbiology. 47: 1317-28. PMID 12603737 DOI: 10.1046/j.1365-2958.2003.03370.x  1
2003 Schlothauer T, Mogk A, Dougan DA, Bukau B, Turgay K. MecA, an adaptor protein necessary for ClpC chaperone activity. Proceedings of the National Academy of Sciences of the United States of America. 100: 2306-11. PMID 12598648 DOI: 10.1073/pnas.0535717100  1
2003 Erbse A, Dougan DA, Bukau B. A folding machine for many but a master of none. Nature Structural Biology. 10: 84-6. PMID 12555083 DOI: 10.1038/nsb0203-84  1
2002 Mayer MP, Nikolay R, Bukau B. Aha, another regulator for hsp90 chaperones. Molecular Cell. 10: 1255-6. PMID 12503997 DOI: 10.1016/S1097-2765(02)00793-1  1
2002 Dougan DA, Mogk A, Bukau B. Protein folding and degradation in bacteria: to degrade or not to degrade? That is the question. Cellular and Molecular Life Sciences : Cmls. 59: 1607-16. PMID 12475170  1
2002 Patzelt H, Kramer G, Rauch T, Schönfeld HJ, Bukau B, Deuerling E. Three-state equilibrium of Escherichia coli trigger factor. Biological Chemistry. 383: 1611-9. PMID 12452438 DOI: 10.1515/BC.2002.182  1
2002 Zeth K, Ravelli RB, Paal K, Cusack S, Bukau B, Dougan DA. Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA Nature Structural Biology. 9: 906-911. PMID 12426582 DOI: 10.1038/nsb869  1
2002 Dougan DA, Mogk A, Zeth K, Turgay K, Bukau B. AAA+ proteins and substrate recognition, it all depends on their partner in crime Febs Letters. 529: 6-10. PMID 12354604 DOI: 10.1016/S0014-5793(02)03179-4  1
2002 Kramer G, Rauch T, Rist W, Vorderwülbecke S, Palzelt H, Schulze-Specking A, Ban N, Deuerling E, Bukau B. L23 protein functions as a chaperone docking site on the ribosome Nature. 419: 171-174. PMID 12226666 DOI: 10.1038/nature01047  1
2002 Kluck CJ, Patzelt H, Genevaux P, Brehmer D, Rist W, Schneider-Mergener J, Bukau B, Mayer MP. Structure-function analysis of HscC, the Escherichia coli member of a novel subfamily of specialized Hsp70 chaperones Journal of Biological Chemistry. 277: 41060-41069. PMID 12183460 DOI: 10.1074/jbc.M206520200  1
2002 Mayer MP, Tomoyasu T, Bukau B. Molecular mechanism of Hsp70 chaperones Tanpakushitsu Kakusan Koso. Protein, Nucleic Acid, Enzyme. 47: 1189-1195. PMID 12166065  1
2002 Schlieker C, Bukau B, Mogk A. Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: implications for their applicability in biotechnology. Journal of Biotechnology. 96: 13-21. PMID 12142139 DOI: 10.1016/S0168-1656(02)00033-0  1
2002 Zeth K, Dougan DA, Cusack S, Bukau B, Ravelli RB. Crystallization and preliminary X-ray analysis of the Escherichia coli adaptor protein ClpS, free and in complex with the N-terminal domain of ClpA Acta Crystallographica Section D: Biological Crystallography. 58: 1207-1210. PMID 12077445 DOI: 10.1107/S0907444902006960  1
2002 Dougan DA, Reid BG, Horwich AL, Bukau B. ClpS, a substrate modulator of the ClpAP machine. Molecular Cell. 9: 673-83. PMID 11931773 DOI: 10.1016/S1097-2765(02)00485-9  1
2002 Wiederkehr T, Bukau B, Buchberger A. Protein turnover: A CHIP programmed for proteolysis Current Biology. 12: R26-R28. PMID 11790321 DOI: 10.1016/S0960-9822(01)00644-3  1
2001 Mayer MP, Brehmer D, Gässler CS, Bukau B. Hsp70 chaperone machines Advances in Protein Chemistry. 59: 1-44. PMID 11868269 DOI: 10.1016/S0065-3233(01)59001-4  1
2001 Patzelt H, Rüdiger S, Brehmer D, Kramer G, Vorderwülbecke S, Schaffitzel E, Waitz A, Hesterkamp T, Dong L, Schneider-Mergener J, Bukau B, Deuerling E. Binding specificity of Escherichia coli trigger factor Proceedings of the National Academy of Sciences of the United States of America. 98: 14244-14249. PMID 11724963 DOI: 10.1073/pnas.261432298  1
2001 Schaffitzel E, Rüdiger S, Bukau B, Deuerling E. Functional dissection of trigger factor and DnaK: Interactions with nascent polypeptides and thermally denatured proteins Biological Chemistry. 382: 1235-1243. PMID 11592405 DOI: 10.1515/BC.2001.154  1
2001 Tomoyasu T, Arsène F, Ogura T, Bukau B. The C terminus of σ32 is not essential for degradation by FtsH Journal of Bacteriology. 183: 5911-5917. PMID 11566990 DOI: 10.1128/JB.183.20.5911-5917.2001  1
2001 Gässler CS, Wiederkehr T, Brehmer D, Bukau B, Mayer MP. Bag-1M Accelerates Nucleotide Release for Human Hsc70 and Hsp70 and Can Act Concentration-dependent as Positive and Negative Cofactor Journal of Biological Chemistry. 276: 32538-32544. PMID 11441021 DOI: 10.1074/jbc.M105328200  1
2001 Brehmer D, Rüdiger S, Gässler CS, Klostermeier D, Packschies L, Reinstein J, Mayer MP, Bukau B. Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange Nature Structural Biology. 8: 427-432. PMID 11323718 DOI: 10.1038/87588  1
2001 Tomoyasu T, Mogk A, Langen H, Goloubinoff P, Bukau B. Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol Molecular Microbiology. 40: 397-413. PMID 11309122 DOI: 10.1046/j.1365-2958.2001.02383.x  1
2001 Rüdiger S, Schneider-Mergener J, Bukau B. Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone Embo Journal. 20: 1042-1050. PMID 11230128 DOI: 10.1093/emboj/20.5.1042  1
2000 Rüdiger S, Mayer MP, Schneider-Mergener J, Bukau B. Modulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic arch Journal of Molecular Biology. 304: 245-251. PMID 11090270 DOI: 10.1006/jmbi.2000.4193  1
2000 Mayer MP, Rudiger S, Bukau B. Molecular basis for interactions of the DnaK chaperone with substrates Biological Chemistry. 381: 877-885. PMID 11076019  1
2000 Mayer MP, Schröder H, Rüdiger S, Paal K, Laufen T, Bukau B. Multistep mechanism of substrate binding determines chaperone activity of Hsp70 Nature Structural Biology. 7: 586-593. PMID 10876246 DOI: 10.1038/76819  1
2000 Diamant S, Peres Ben-Zvi A, Bukau B, Goloubinoff P. Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery Journal of Biological Chemistry. 275: 21107-21113. PMID 10801805 DOI: 10.1074/jbc.M001293200  1
2000 Arsène F, Tomoyasu T, Bukau B. The heat shock response of Escherichia coli International Journal of Food Microbiology. 55: 3-9. PMID 10791710 DOI: 10.1016/S0168-1605(00)00206-3  1
2000 Bukau B, Deuerling E, Pfund C, Craig EA. Getting newly synthesized proteins into shape Cell. 101: 119-122. PMID 10786831 DOI: 10.1016/S0092-8674(00)80806-5  1
1999 Buchberger A, Gässler CS, Büttner M, McMacken R, Bukau B. Functional defects of the DnaK756 mutant chaperone of Escherichia coli indicate distinct roles for amino- and carboxyl-terminal residues in substrate and co-chaperone interaction and interdomain communication Journal of Biological Chemistry. 274: 38017-38026. PMID 10608870 DOI: 10.1074/jbc.274.53.38017  1
1999 Mogk A, Tomoyasu T, Goloubinoff P, Rüdiger S, Röder D, Langen H, Bukau B. Identification of thermolabile Escherichia coli proteins: Prevention and reversion of aggregation by DnaK and ClpB Embo Journal. 18: 6934-6949. PMID 10601016  1
1999 Goloubinoff P, Mogk A, Ben Zvi AP, Tomoyasu T, Bukau B. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network Proceedings of the National Academy of Sciences of the United States of America. 96: 13732-13737. PMID 10570141 DOI: 10.1073/pnas.96.24.13732  1
1999 Knoblauch NTM, Rüdiger S, Schönfeld HJ, Driessen AJM, Schneider-Mergener J, Bukau B. Substrate specificity of the SecB chaperone Journal of Biological Chemistry. 274: 34219-34225. PMID 10567394 DOI: 10.1074/jbc.274.48.34219  1
1999 Deuerling E, Schulze-Specking A, Tomoyasu T, Mogk A, Bukau B. Trigger factor and DnaK cooperate in folding of newly synthesized proteins Nature. 400: 693-696. PMID 10458167 DOI: 10.1038/23301  1
1999 Mayer MP, Laufen T, Paal K, McCarty JS, Bukau B. Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy Journal of Molecular Biology. 289: 1131-1144. PMID 10369787 DOI: 10.1006/jmbi.1999.2844  1
1999 Arsène F, Tomoyasu T, Mogk A, Schirra C, Schulze-Specking A, Bukau B. Role of region C in regulation of the heat shock gene-specific sigma factor of Escherichia coli, σ32 Journal of Bacteriology. 181: 3552-3561. PMID 10348869  1
1999 Brix J, Rüdiger S, Bukau B, Schneider-Mergener J, Pfanner N. Distribution of binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70 in a presequence-carrying preprotein and a non- cleavable preprotein Journal of Biological Chemistry. 274: 16522-16530. PMID 10347216 DOI: 10.1074/jbc.274.23.16522  1
1999 Mayer MP, Bukau B. Molecular chaperones: The busy life of Hsp90 Current Biology. 9: R322-R325. PMID 10322107 DOI: 10.1016/S0960-9822(99)80203-6  1
1999 Laufen T, Mayer MP, Beisel C, Klostermeier D, Mogk A, Reinstein J, Bukau B. Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones. Proceedings of the National Academy of Sciences of the United States of America. 96: 5452-7. PMID 10318904 DOI: 10.1073/pnas.96.10.5452  1
1999 Mogk A, Bukau B, Lutz R, Schumann W. Construction and analysis of hybrid Escherichia coli-Bacillus subtilis dnaK genes Journal of Bacteriology. 181: 1971-1974. PMID 10074100  1
1998 Gässler CS, Buchberger A, Laufen T, Mayer MP, Schröder H, Valencia A, Bukau B. Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone Proceedings of the National Academy of Sciences of the United States of America. 95: 15229-15234. PMID 9860951 DOI: 10.1073/pnas.95.26.15229  1
1998 Tatsuta T, Tomoyasu T, Bukau B, Kitagawa M, Mori H, Karata K, Ogura T. Heat shock regulation in the ftsH null mutant of Escherichia coli: Dissection of stability and activity control mechanisms of σ32 in vivo Molecular Microbiology. 30: 583-593. PMID 9822823 DOI: 10.1046/j.1365-2958.1998.01091.x  1
1998 Tomoyasu T, Ogura T, Tatsuta T, Bukau B. Levels of DnaK and DnaJ provide tight control of heat shock gene expression and protein repair in Escherichia coli Molecular Microbiology. 30: 567-581. PMID 9822822 DOI: 10.1046/j.1365-2958.1998.01090.x  1
1998 Hesterkamp T, Bukau B. Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E.coli Embo Journal. 17: 4818-4828. PMID 9707441 DOI: 10.1093/emboj/17.16.4818  1
1998 Mayer MP, Bukau B. Hsp70 chaperone systems: Diversity of cellular functions and mechanism of action Biological Chemistry. 379: 261-268. PMID 9563820  1
1998 Bukau B, Horwich AL. The Hsp70 and Hsp60 chaperone machines. Cell. 92: 351-66. PMID 9476895 DOI: 10.1016/S0092-8674(00)80928-9  1
1997 Terada K, Kanazawa M, Bukau B, Mori M. The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding Journal of Cell Biology. 139: 1089-1095. PMID 9382858 DOI: 10.1083/jcb.139.5.1089  1
1997 Hesterkamp T, Deuerling E, Bukau B. The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes Journal of Biological Chemistry. 272: 21865-21871. PMID 9268318 DOI: 10.1074/jbc.272.35.21865  1
1997 Shotland Y, Koby S, Teff D, Mansur N, Oren DA, Tatematsu K, Tomoyasu T, Kessel M, Bukau B, Ogura T, Oppenheim AB. Proteolysis of the phage λ CII regulatory protein by FtsH (HfIB) of Escherichia coli Molecular Microbiology. 24: 1303-1310. PMID 9218777  1
1997 Rüdiger S, Buchberger A, Bukau B. Interaction of Hsp70 chaperones with substrates Nature Structural Biology. 4: 342-349. PMID 9145101  1
1997 Packschies L, Theyssen H, Buchberger A, Bukau B, Goody RS, Reinstein J. GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism Biochemistry. 36: 3417-3422. PMID 9131990 DOI: 10.1021/bi962835l  1
1997 Rüdiger S, Germeroth L, Schneider-Mergener J, Bukau B. Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries Embo Journal. 16: 1501-1507. PMID 9130695 DOI: 10.1093/emboj/16.7.1501  1
1996 Langer T, Buchner J, Bukau B. Chaperone function on Crete: A meeting report Cell Stress and Chaperones. 1: 5-12. PMID 9222582  1
1996 Theyssen H, Schuster HP, Packschies L, Bukau B, Reinstein J. The second step of ATP binding to DnaK induces peptide release Journal of Molecular Biology. 263: 657-670. PMID 8947566 DOI: 10.1006/jmbi.1996.0606  1
1996 Buchberger A, Schröder H, Hesterkamp T, Schönfeld HJ, Bukau B. Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding Journal of Molecular Biology. 261: 328-333. PMID 8780775 DOI: 10.1006/jmbi.1996.0465  1
1996 Hesterkamp T, Bukau B. The Escherichia coli trigger factor Febs Letters. 389: 32-34. PMID 8682200 DOI: 10.1016/0014-5793(96)00582-0  1
1996 Hesterkamp T, Bukau B. Identification of the prolyl isomerase domain of Escherichia coli trigger factor Febs Letters. 385: 67-71. PMID 8641469 DOI: 10.1016/0014-5793(96)00351-1  1
1996 Hesterkamp T, Hauser S, Lütcke H, Bukau B. Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains. Proceedings of the National Academy of Sciences of the United States of America. 93: 4437-41. PMID 8633085 DOI: 10.1073/pnas.93.9.4437  1
1996 McCarty JS, Rüdiger S, Schönfeld HJ, Schneider-Mergener J, Nakahigashi K, Yura T, Bukau B. Regulatory region C of the E. coli heat shock transcription factor, σ32, constitutes a DnaK binding site and is conserved among eubacteria Journal of Molecular Biology. 256: 829-837. PMID 8601834 DOI: 10.1006/jmbi.1996.0129  1
1996 Gamer J, Multhaup G, Tomoyasu T, McCarty JS, Rüdiger S, Schönfeld HJ, Schirra C, Bujard H, Bukau B. A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor σ32 Embo Journal. 15: 607-617. PMID 8599944  1
1996 Bukau B, Hesterkamp T, Luirink J. Growing up in a dangerous environment: A network of multiple targeting and folding pathways for nascent polypeptides in the cytosol Trends in Cell Biology. 6: 480-486. DOI: 10.1016/0962-8924(96)84946-4  1
1995 Schonfeld HJ, Schmidt D, Schroder H, Bukau B. The DnaK chaperone system of Escherichia coli: Quaternary structures and interactions of the DnaK and GrpE components Journal of Biological Chemistry. 270: 2183-2189. PMID 7836448 DOI: 10.1074/jbc.270.5.2183  1
1995 Tomoyasu T, Gamer J, Bukau B, Kanemori M, Mori H, Rutman AJ, Oppenheim AB, Yura T, Yamanaka K, Niki H. Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32. The Embo Journal. 14: 2551-60. PMID 7781608  1
1995 McCarty JS, Buchberger A, Reinstein J, Bukau B. The role of ATP in the functional cycle of the DnaK chaperone system Journal of Molecular Biology. 249: 126-137. PMID 7776367 DOI: 10.1006/jmbi.1995.0284  1
1995 Levy EJ, McCarty J, Bukau B, Chirico WJ. Conserved ATPase and luciferase refolding activities between bacteria and yeast Hsp70 chaperones and modulators Febs Letters. 368: 435-440. PMID 7635193 DOI: 10.1016/0014-5793(95)00704-D  1
1995 Buchberger A, Theyssen H, Schroder H, McCarty JS, Virgallita G, Milkereit P, Reinstein J, Bukau B. Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication Journal of Biological Chemistry. 270: 16903-16910. PMID 7622507 DOI: 10.1074/jbc.270.28.16903  1
1994 Szabo A, Langer T, Schröder H, Flanagan J, Bukau B, Hartl FU. The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system - DnaK, DnaJ, and GrpE Proceedings of the National Academy of Sciences of the United States of America. 91: 10345-10349. PMID 7937953 DOI: 10.1073/pnas.91.22.10345  1
1994 Buchberger A, Valencia A, McMacken R, Sander C, Bukau B. The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171 Embo Journal. 13: 1687-1695. PMID 7908876  1
1994 Buchberger A, Schröder H, Büttner M, Valencia A, Bukau B. A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE Nature Structural Biology. 1: 95-101. PMID 7656024  1
1993 Bukau B, Reilly P, McCarty J, Walker GC. Immunogold localization of the DnaK heat shock protein in Escherichia coli cells. Journal of General Microbiology. 139: 95-9. PMID 8450312  1
1993 Bukau B. Regulation of the Escherichia coli heat-shock response Molecular Microbiology. 9: 671-680. PMID 7901731  1
1993 Schroder H, Langer T, Hartl FU, Bukau B. DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage Embo Journal. 12: 4137-4144. PMID 7900997  1
1992 Gamer J, Bujard H, Bukau B. Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor σ32 Cell. 69: 833-842. PMID 1534276 DOI: 10.1016/0092-8674(92)90294-M  1
1992 Bukau B. A module of the DnaJ heat shock proteins found in malaria parasites Trends in Biochemical Sciences. 17: 129. DOI: 10.1016/0968-0004(92)90319-5  1
1990 Bukau B, Walker GC. Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone. The Embo Journal. 9: 4027-36. PMID 2249663  1
1989 Bukau B, Walker GC. Delta dnaK52 mutants of Escherichia coli have defects in chromosome segregation and plasmid maintenance at normal growth temperatures. Journal of Bacteriology. 171: 6030-8. PMID 2681151  1
1989 Bukau B, Walker GC. Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism. Journal of Bacteriology. 171: 2337-46. PMID 2651398  1
1986 Case CC, Bukau B, Granett S, Villarejo MR, Boos W. Contrasting mechanisms of envZ control of mal and pho regulon genes in Escherichia coli. Journal of Bacteriology. 166: 706-12. PMID 3011737  1
1986 Bukau B, Ehrmann M, Boos W. Osmoregulation of the maltose regulon in Escherichia coli. Journal of Bacteriology. 166: 884-91. PMID 2423504  1
1985 Bukau B, Brass JM, Boos W. Ca2+-induced permeabilization of the Escherichia coli outer membrane: comparison of transformation and reconstitution of binding-protein-dependent transport. Journal of Bacteriology. 163: 61-8. PMID 3891741  1
1983 Brass JM, Ehmann U, Bukau B. Reconstitution of maltose transport in Escherichia coli: conditions affecting import of maltose-binding protein into the periplasm of calcium-treated cells Journal of Bacteriology. 155: 97-106. PMID 6345515  1
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