| Year |
Citation |
Score |
| 2024 |
Zoltsman G, Dang TL, Kuchersky M, Faust O, Silva MS, Ilani T, Wentink AS, Bukau B, Rosenzweig R. A unique chaperoning mechanism in class A JDPs recognizes and stabilizes mutant p53. Molecular Cell. PMID 38508184 DOI: 10.1016/j.molcel.2024.02.018 |
0.386 |
|
| 2024 |
Minoia M, Quintana-Cordero J, Jetzinger K, Kotan IE, Turnbull KJ, Ciccarelli M, Masser AE, Liebers D, Gouarin E, Czech M, Hauryliuk V, Bukau B, Kramer G, Andréasson C. Chp1 is a dedicated chaperone at the ribosome that safeguards eEF1A biogenesis. Nature Communications. 15: 1382. PMID 38360885 DOI: 10.1038/s41467-024-45645-w |
0.424 |
|
| 2024 |
Ruger-Herreros C, Svoboda L, Mogk A, Bukau B. Role of J-domain Proteins in Yeast Physiology and Protein Quality Control. Journal of Molecular Biology. 168484. PMID 38331212 DOI: 10.1016/j.jmb.2024.168484 |
0.498 |
|
| 2023 |
Marszalek J, De Los Rios P, Cyr D, Mayer MP, Adupa V, Andréasson C, Blatch GL, Braun JEA, Brodsky JL, Bukau B, Chapple JP, Conz C, Dementin S, Genevaux P, Genest O, et al. J-domain proteins: From molecular mechanisms to diseases. Cell Stress & Chaperones. 29: 21-33. PMID 38320449 DOI: 10.1016/j.cstres.2023.12.002 |
0.365 |
|
| 2023 |
Jawed A, Ho CT, Grousl T, Shrivastava A, Ruppert T, Bukau B, Mogk A. Balanced activities of Hsp70 and the ubiquitin proteasome system underlie cellular protein homeostasis. Frontiers in Molecular Biosciences. 9: 1106477. PMID 36660429 DOI: 10.3389/fmolb.2022.1106477 |
0.458 |
|
| 2022 |
Shrivastava A, Sandhof CA, Reinle K, Jawed A, Ruger-Herreros C, Schwarz D, Creamer D, Nussbaum-Krammer C, Mogk A, Bukau B. The cytoprotective sequestration activity of small heat shock proteins is evolutionarily conserved. The Journal of Cell Biology. 221. PMID 36069810 DOI: 10.1083/jcb.202202149 |
0.454 |
|
| 2022 |
Beton JG, Monistrol J, Wentink A, Johnston EC, Roberts AJ, Bukau BG, Hoogenboom BW, Saibil HR. Cooperative amyloid fibre binding and disassembly by the Hsp70 disaggregase. The Embo Journal. e110410. PMID 35698800 DOI: 10.15252/embj.2021110410 |
0.348 |
|
| 2022 |
Cerullo F, Filbeck S, Patil PR, Hung HC, Xu H, Vornberger J, Hofer FW, Schmitt J, Kramer G, Bukau B, Hofmann K, Pfeffer S, Joazeiro CAP. Bacterial ribosome collision sensing by a MutS DNA repair ATPase paralogue. Nature. 603: 509-514. PMID 35264791 DOI: 10.1038/s41586-022-04487-6 |
0.324 |
|
| 2021 |
Reinle K, Mogk A, Bukau B. The diverse functions of small heat shock proteins in the proteostasis network. Journal of Molecular Biology. 167157. PMID 34271010 DOI: 10.1016/j.jmb.2021.167157 |
0.478 |
|
| 2021 |
Friedrich UA, Zedan M, Hessling B, Fenzl K, Gillet L, Barry J, Knop M, Kramer G, Bukau B. N-terminal acetylation of proteins by NatA and NatB serves distinct physiological roles in Saccharomyces cerevisiae. Cell Reports. 34: 108711. PMID 33535049 DOI: 10.1016/j.celrep.2021.108711 |
0.411 |
|
| 2021 |
Bertolini M, Fenzl K, Kats I, Wruck F, Tippmann F, Schmitt J, Auburger JJ, Tans S, Bukau B, Kramer G. Interactions between nascent proteins translated by adjacent ribosomes drive homomer assembly. Science (New York, N.Y.). 371: 57-64. PMID 33384371 DOI: 10.1126/science.abc7151 |
0.368 |
|
| 2020 |
Faust O, Abayev-Avraham M, Wentink AS, Maurer M, Nillegoda NB, London N, Bukau B, Rosenzweig R. HSP40 proteins use class-specific regulation to drive HSP70 functional diversity. Nature. PMID 33177718 DOI: 10.1038/s41586-020-2906-4 |
0.442 |
|
| 2020 |
Wentink AS, Nillegoda NB, Feufel J, Ubartaitė G, Schneider CP, De Los Rios P, Hennig J, Barducci A, Bukau B. Molecular dissection of amyloid disaggregation by human HSP70. Nature. PMID 33177717 DOI: 10.1038/s41586-020-2904-6 |
0.332 |
|
| 2020 |
Bohlen J, Harbrecht L, Blanco S, Clemm von Hohenberg K, Fenzl K, Kramer G, Bukau B, Teleman AA. DENR promotes translation reinitiation via ribosome recycling to drive expression of oncogenes including ATF4. Nature Communications. 11: 4676. PMID 32938922 DOI: 10.1038/S41467-020-18452-2 |
0.35 |
|
| 2020 |
Bohlen J, Fenzl K, Kramer G, Bukau B, Teleman AA. Selective 40S Footprinting Reveals Cap-Tethered Ribosome Scanning in Human Cells. Molecular Cell. PMID 32589966 DOI: 10.1016/J.Molcel.2020.06.005 |
0.301 |
|
| 2020 |
den Brave F, Cairo LV, Jagadeesan C, Ruger-Herreros C, Mogk A, Bukau B, Jentsch S. Chaperone-Mediated Protein Disaggregation Triggers Proteolytic Clearance of Intra-nuclear Protein Inclusions. Cell Reports. 31: 107680. PMID 32492414 DOI: 10.1016/J.Celrep.2020.107680 |
0.575 |
|
| 2020 |
Nachman E, Wentink AS, Madiona K, Bousset L, Katsinelos T, Allinson K, Kampinga H, McEwan WA, Jahn TR, Melki R, Mogk A, Bukau B, Nussbaum-Krammer C. Disassembly of Tau fibrils by the human Hsp70 disaggregation machinery generates small seeding-competent species. The Journal of Biological Chemistry. PMID 32467226 DOI: 10.1074/Jbc.Ra120.013478 |
0.41 |
|
| 2020 |
Tittelmeier J, Sandhof CA, Ries HM, Druffel-Augustin S, Mogk A, Bukau B, Nussbaum-Krammer C. The HSP110/HSP70 disaggregation system generates spreading-competent toxic α-synuclein species. The Embo Journal. e103954. PMID 32449565 DOI: 10.15252/Embj.2019103954 |
0.442 |
|
| 2020 |
Serlidaki D, van Waarde MAWH, Rohland L, Wentink AS, Dekker SL, Kamphuis MJ, Boertien JM, Brunsting JF, Nillegoda NB, Bukau B, Mayer MP, Kampinga HH, Bergink S. Functional diversity between HSP70 paralogs due to variable interactions with specific co-chaperones. The Journal of Biological Chemistry. PMID 32284329 DOI: 10.1074/Jbc.Ra119.012449 |
0.542 |
|
| 2020 |
Avellaneda MJ, Franke KB, Sunderlikova V, Bukau B, Mogk A, Tans SJ. Processive extrusion of polypeptide loops by a Hsp100 disaggregase. Nature. PMID 31996849 DOI: 10.1038/S41586-020-1964-Y |
0.485 |
|
| 2019 |
Castells-Ballester J, Rinis N, Kotan I, Gal L, Bausewein D, Kats I, Zatorska E, Kramer G, Bukau B, Schuldiner M, Strahl S. Translational Regulation of Pmt1 and Pmt2 by Bfr1 Affects Unfolded Protein O-Mannosylation. International Journal of Molecular Sciences. 20. PMID 31835530 DOI: 10.3390/Ijms20246220 |
0.449 |
|
| 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 |
0.537 |
|
| 2019 |
Rosenzweig R, Nillegoda NB, Mayer MP, Bukau B. The Hsp70 chaperone network. Nature Reviews. Molecular Cell Biology. PMID 31253954 DOI: 10.1038/S41580-019-0133-3 |
0.549 |
|
| 2019 |
Jamshad M, Knowles TJ, White SA, Ward DG, Mohammed F, Rahman KF, Wynne M, Hughes GW, Kramer G, Bukau B, Huber D. The C-terminal tail of the bacterial translocation ATPase SecA modulates its activity. Elife. 8. PMID 31246174 DOI: 10.7554/Elife.48385 |
0.524 |
|
| 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: 10.2210/Pdb6Qs4/Pdb |
0.44 |
|
| 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 |
0.489 |
|
| 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 |
0.581 |
|
| 2019 |
Wentink A, Nussbaum-Krammer C, Bukau B. Modulation of Amyloid States by Molecular Chaperones. Cold Spring Harbor Perspectives in Biology. PMID 30755450 DOI: 10.1101/Cshperspect.A033969 |
0.487 |
|
| 2018 |
Kramer G, Shiber A, Bukau B. Mechanisms of Cotranslational Maturation of Newly Synthesized Proteins. Annual Review of Biochemistry. PMID 30508494 DOI: 10.1146/Annurev-Biochem-013118-111717 |
0.481 |
|
| 2018 |
Shiber A, Döring K, Friedrich U, Klann K, Merker D, Zedan M, Tippmann F, Kramer G, Bukau B. Cotranslational assembly of protein complexes in eukaryotes revealed by ribosome profiling. Nature. PMID 30158700 DOI: 10.1038/S41586-018-0462-Y |
0.468 |
|
| 2018 |
Nillegoda NB, Wentink AS, Bukau B. Protein Disaggregation in Multicellular Organisms. Trends in Biochemical Sciences. PMID 29501325 DOI: 10.1016/J.Tibs.2018.02.003 |
0.547 |
|
| 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 |
0.595 |
|
| 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 |
0.56 |
|
| 2018 |
Rampelt H, Mayer MP, Bukau B. Nucleotide Exchange Factors for Hsp70 Chaperones. Methods in Molecular Biology (Clifton, N.J.). 1709: 179-188. PMID 29177659 DOI: 10.1007/978-1-4939-7477-1_13 |
0.342 |
|
| 2018 |
Ahmed N, Döring K, Kramer G, Bukau B, O'Brien EP. Evolutionarily-Encoded Translation Kinetics Coordinate Co-Translational SSB Chaperone Binding in Yeast Biophysical Journal. 114: 395a. DOI: 10.1016/J.Bpj.2017.11.2188 |
0.391 |
|
| 2017 |
Lee C, Franke KB, Kamal SM, Kim H, Lünsdorf H, Jäger J, Nimtz M, Trček J, Jänsch L, Bukau B, Mogk A, Römling U. Stand-alone ClpG disaggregase confers superior heat tolerance to bacteria. Proceedings of the National Academy of Sciences of the United States of America. PMID 29263094 DOI: 10.1073/Pnas.1712051115 |
0.475 |
|
| 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 |
0.425 |
|
| 2017 |
Kirstein J, Arnsburg K, Scior A, Szlachcic A, Guilbride DL, Morimoto RI, Bukau B, Nillegoda NB. In vivo properties of the disaggregase function of J-proteins and Hsc70 in Caenorhabditis elegans stress and aging. Aging Cell. PMID 29024389 DOI: 10.1111/Acel.12686 |
0.542 |
|
| 2017 |
Acosta-Sampson L, Döring K, Lin Y, Yu VY, Bukau B, Kramer G, Cate JHD. Role for Ribosome-Associated Complex and Stress-Seventy subfamily B (RAC-Ssb) in integral membrane protein translation. The Journal of Biological Chemistry. PMID 28972146 DOI: 10.1074/Jbc.M117.813857 |
0.485 |
|
| 2017 |
Zemva J, Fink CA, Fleming TH, Schmidt L, Loft A, Herzig S, Knieß RA, Mayer M, Bukau B, Nawroth PP, Tyedmers J. Hormesis enables cells to handle accumulating toxic metabolites during increased energy flux. Redox Biology. 13: 674-686. PMID 28826004 DOI: 10.1016/J.Redox.2017.08.007 |
0.363 |
|
| 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 |
0.502 |
|
| 2017 |
Döring K, Ahmed N, Riemer T, Suresh HG, Vainshtein Y, Habich M, Riemer J, Mayer MP, O'Brien EP, Kramer G, Bukau B. Profiling Ssb-Nascent Chain Interactions Reveals Principles of Hsp70-Assisted Folding. Cell. 170: 298-311.e20. PMID 28708998 DOI: 10.1016/J.Cell.2017.06.038 |
0.518 |
|
| 2017 |
Bascos NAD, Mayer MP, Bukau B, Landry SJ. The Hsp40 J-domain modulates Hsp70 conformation and ATPase activity with a semi-elliptical spring. Protein Science : a Publication of the Protein Society. PMID 28685898 DOI: 10.1002/Pro.3223 |
0.464 |
|
| 2017 |
Garcia VM, Nillegoda NB, Bukau B, Morano KA. Substrate binding by the yeast Hsp110 nucleotide exchange factor and molecular chaperone, Sse1, is not obligate for its biological activities. Molecular Biology of the Cell. PMID 28539411 DOI: 10.1091/Mbc.E17-01-0070 |
0.534 |
|
| 2017 |
Nillegoda NB, Stank A, Malinverni D, Alberts N, Szlachcic A, Barducci A, De Los Rios P, Wade RC, Bukau B. Evolution of an intricate J-protein network driving protein disaggregation in eukaryotes. Elife. 6. PMID 28504929 DOI: 10.7554/Elife.24560 |
0.536 |
|
| 2017 |
Carra S, Alberti S, Arrigo PA, Benesch JL, Benjamin IJ, Boelens W, Bartelt-Kirbach B, Brundel BJ, Buchner J, Bukau B, Carver JA, Ecroyd H, Emanuelsson C, Finet S, Golenhofen N, et al. The growing world of small heat shock proteins: from structure to functions. Cell Stress & Chaperones. PMID 28364346 DOI: 10.1007/S12192-017-0787-8 |
0.509 |
|
| 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 |
0.412 |
|
| 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 |
0.56 |
|
| 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 |
0.587 |
|
| 2017 |
Carroni M, Franke KB, Maurer M, Jäger J, Hantke I, Gloge F, Linder D, Gremer S, Turgay K, Bukau B, Mogk A. Author response: Regulatory coiled-coil domains promote head-to-head assemblies of AAA+ chaperones essential for tunable activity control Elife. DOI: 10.7554/Elife.30120.036 |
0.33 |
|
| 2017 |
Nillegoda NB, Stank A, Malinverni D, Alberts N, Szlachcic A, Barducci A, Rios PDL, Wade RC, Bukau B. Author response: Evolution of an intricate J-protein network driving protein disaggregation in eukaryotes Elife. DOI: 10.7554/Elife.24560.020 |
0.431 |
|
| 2017 |
Wentink A, Nillegoda N, Ho C, Mogk A, Bukau B. A versatile chaperone network coping with protein aggregates and amyloids Febs Journal. 284: 17-18. DOI: 10.1111/Febs.14170 |
0.413 |
|
| 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 |
0.543 |
|
| 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 |
0.45 |
|
| 2016 |
Huber D, Jamshad M, Hanmer R, Schibich D, Döring K, Marcomini I, Kramer G, Bukau B. SecA cotranslationally interacts with nascent substrate proteins in vivo. Journal of Bacteriology. PMID 27795329 DOI: 10.1128/Jb.00622-16 |
0.462 |
|
| 2016 |
Mashaghi A, Bezrukavnikov S, Minde DP, Wentink AS, Kityk R, Zachmann-Brand B, Mayer MP, Kramer G, Bukau B, Tans SJ. Alternative modes of client binding enable functional plasticity of Hsp70. Nature. PMID 27783598 DOI: 10.1038/Nature20137 |
0.556 |
|
| 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 |
0.517 |
|
| 2016 |
Lange S, Franks WT, Rajagopalan N, Döring K, Geiger MA, Linden A, van Rossum BJ, Kramer G, Bukau B, Oschkinat H. Structural analysis of a signal peptide inside the ribosome tunnel by DNP MAS NMR. Science Advances. 2: e1600379. PMID 27551685 DOI: 10.1126/Sciadv.1600379 |
0.399 |
|
| 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 |
0.462 |
|
| 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 |
0.457 |
|
| 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 |
0.384 |
|
| 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 |
0.457 |
|
| 2016 |
Yonashiro R, Tahara EB, Bengtson MH, Khokhrina M, Lorenz H, Chen K, Kigoshi-Tansho Y, Savas JN, Yates JR, Kay SA, Craig EA, Mogk A, Bukau B, Joazeiro CA. Author response: The Rqc2/Tae2 subunit of the ribosome-associated quality control (RQC) complex marks ribosome-stalled nascent polypeptide chains for aggregation Elife. DOI: 10.7554/Elife.11794.015 |
0.324 |
|
| 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 |
0.469 |
|
| 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 |
0.446 |
|
| 2015 |
Nillegoda NB, Bukau B. Metazoan Hsp70-based protein disaggregases: emergence and mechanisms. Frontiers in Molecular Biosciences. 2: 57. PMID 26501065 DOI: 10.3389/Fmolb.2015.00057 |
0.576 |
|
| 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 |
0.494 |
|
| 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 |
0.438 |
|
| 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 |
0.512 |
|
| 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 |
0.398 |
|
| 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 |
0.582 |
|
| 2015 |
Kramer G, Bukau B. 18 The busy life of nascent chains: mechanisms of folding of newly synthesized proteins. Journal of Biomolecular Structure & Dynamics. 33: 10. PMID 26103229 DOI: 10.1080/07391102.2015.1032558 |
0.398 |
|
| 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 |
0.538 |
|
| 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 |
0.461 |
|
| 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 |
0.423 |
|
| 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 |
0.32 |
|
| 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 |
0.538 |
|
| 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 |
0.515 |
|
| 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 |
0.474 |
|
| 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 |
0.416 |
|
| 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 |
0.505 |
|
| 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 |
0.445 |
|
| 2014 |
Carroni M, Kummer E, Oguchi Y, Wendler P, Clare DK, Sinning I, Kopp J, Mogk A, Bukau B, Saibil HR. Author response: Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation Elife. DOI: 10.7554/Elife.02481.022 |
0.469 |
|
| 2014 |
Bukau B. Mechanisms of protein folding and quality control in bacteria New Biotechnology. 31: S45. DOI: 10.1016/j.nbt.2014.05.1713 |
0.308 |
|
| 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 |
0.476 |
|
| 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 |
0.449 |
|
| 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 |
0.302 |
|
| 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 |
0.324 |
|
| 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 |
0.513 |
|
| 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 |
0.348 |
|
| 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 |
0.412 |
|
| 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 |
0.516 |
|
| 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 |
0.412 |
|
| 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 |
0.523 |
|
| 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 |
0.52 |
|
| 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 |
0.439 |
|
| 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 |
0.439 |
|
| 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 |
0.496 |
|
| 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 |
0.501 |
|
| 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 |
0.446 |
|
| 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 |
0.562 |
|
| 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 |
0.44 |
|
| 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 |
0.541 |
|
| 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 |
0.494 |
|
| 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 |
0.46 |
|
| 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 |
0.52 |
|
| 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 |
0.501 |
|
| 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 |
0.512 |
|
| 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 |
0.513 |
|
| 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 |
0.511 |
|
| 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 |
0.488 |
|
| 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 |
0.443 |
|
| 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 |
0.493 |
|
| 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 |
0.471 |
|
| 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 |
0.455 |
|
| 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 |
0.428 |
|
| 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 |
0.352 |
|
| 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 |
0.479 |
|
| 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 |
0.503 |
|
| 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 |
0.355 |
|
| 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 |
0.389 |
|
| 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 |
0.464 |
|
| 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 |
0.515 |
|
| 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 |
0.363 |
|
| 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 |
0.407 |
|
| 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 |
0.537 |
|
| 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 |
0.45 |
|
| 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 |
0.548 |
|
| 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 |
0.439 |
|
| 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 |
0.458 |
|
| 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 |
0.468 |
|
| 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 |
0.608 |
|
| 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 |
0.431 |
|
| 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 |
0.354 |
|
| 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 |
0.528 |
|
| 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 |
0.362 |
|
| 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 |
0.436 |
|
| 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 |
0.46 |
|
| 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 |
0.408 |
|
| 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 |
0.386 |
|
| 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 |
0.549 |
|
| 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 |
0.454 |
|
| 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 |
0.467 |
|
| 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 |
0.56 |
|
| 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 |
0.373 |
|
| 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 |
0.396 |
|
| 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 |
0.401 |
|
| 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 |
0.546 |
|
| 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 |
0.581 |
|
| 2006 |
Bukau B, Craig EA, Morimoto RI, Horwich AL. Stress-Induced Expression of Heat Shock Proteins and Action of the Heat Shock Protein Effectors Reviews in Cell Biology and Molecular Medicine. 463-516. DOI: 10.1002/3527600906.Mcb.200500068 |
0.462 |
|
| 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 |
0.778 |
|
| 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 |
0.4 |
|
| 2005 |
Bukau B. Ribosomes catch Hsp70s. Nature Structural & Molecular Biology. 12: 472-3. PMID 15933729 DOI: 10.1038/Nsmb0605-472 |
0.414 |
|
| 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 |
0.569 |
|
| 2005 |
Kirstein J, Schlothauer T, Dougan DA, Tischendorf G, Mogk A, Bukau B, Turgay K. Functional characterization of an adaptor for a Hsp100 protein Gbm Annual Spring Meeting Mosbach 2005. 2005. DOI: 10.1240/sav_gbm_2005_m_001005 |
0.404 |
|
| 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 |
0.527 |
|
| 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 |
0.74 |
|
| 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 |
0.771 |
|
| 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 |
0.511 |
|
| 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 |
0.457 |
|
| 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 |
0.556 |
|
| 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 |
0.747 |
|
| 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 |
0.42 |
|
| 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 |
0.351 |
|
| 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 |
0.73 |
|
| 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 |
0.417 |
|
| 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 |
0.763 |
|
| 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 |
0.497 |
|
| 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 |
0.537 |
|
| 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 |
0.538 |
|
| 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 |
0.584 |
|
| 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 |
0.447 |
|
| 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 |
0.537 |
|
| 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 |
0.735 |
|
| 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 |
0.506 |
|
| 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 |
0.407 |
|
| 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 |
0.783 |
|
| 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 |
0.785 |
|
| 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 |
0.731 |
|
| 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 |
0.56 |
|
| 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 |
0.58 |
|
| 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 |
0.302 |
|
| 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 |
0.348 |
|
| 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 DOI: 10.1007/Pl00012487 |
0.568 |
|
| 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 |
0.438 |
|
| 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 |
0.476 |
|
| 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 |
0.554 |
|
| 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 |
0.478 |
|
| 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 |
0.564 |
|
| 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 |
0.779 |
|
| 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 |
0.34 |
|
| 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 |
0.536 |
|
| 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 |
0.496 |
|
| 2002 |
Deuerling E, Kramer G, Rauch T, Rist W, Vorderw??lbecke S, Ban N, Bukau B. Cytosolic proteins at birth: linking translation and chaperone assisted protein folding Gbm Annual Fall Meeting Halle 2002. 2002. DOI: 10.1240/sav_gbm_2002_h_000042 |
0.426 |
|
| 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 |
0.543 |
|
| 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 |
0.413 |
|
| 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 |
0.56 |
|
| 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 |
0.438 |
|
| 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 |
0.379 |
|
| 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 |
0.546 |
|
| 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 |
0.543 |
|
| 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 |
0.509 |
|
| 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 |
0.43 |
|
| 2000 |
Mayer MP, Rudiger S, Bukau B. Molecular basis for interactions of the DnaK chaperone with substrates Biological Chemistry. 381: 877-885. PMID 11076019 DOI: 10.1515/Bc.2000.109 |
0.474 |
|
| 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 |
0.45 |
|
| 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 |
0.545 |
|
| 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 |
0.469 |
|
| 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 |
0.471 |
|
| 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 |
0.445 |
|
| 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 DOI: 10.1093/Emboj/18.24.6934 |
0.562 |
|
| 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 |
0.553 |
|
| 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 |
0.482 |
|
| 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 |
0.559 |
|
| 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 |
0.463 |
|
| 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 DOI: 10.1128/Jb.181.11.3552-3561.1999 |
0.392 |
|
| 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 |
0.364 |
|
| 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 |
0.462 |
|
| 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 |
0.497 |
|
| 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 DOI: 10.1128/Jb.181.6.1971-1974.1999 |
0.396 |
|
| 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 |
0.465 |
|
| 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 |
0.409 |
|
| 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 |
0.438 |
|
| 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 |
0.57 |
|
| 1998 |
Mayer MP, Bukau B. Hsp70 chaperone systems: Diversity of cellular functions and mechanism of action Biological Chemistry. 379: 261-268. PMID 9563820 |
0.316 |
|
| 1998 |
Rüdiger S, Bukau B. Gebrauchsanweisung für die einfachen Dinge: Proteine: Standardmethoden der Molekular-und Zellbiologie. Präparation, Gelelektrophorese, Membrantransfer und Immundetektion. Von W.A. Eckert und J. Kartenbeck. Springer, Heidelberg, 1997. 275 S., Spiralband, 7 Nachrichten Aus Chemie, Technik Und Laboratorium. 46: 246-246. DOI: 10.1002/Nadc.19980460224 |
0.346 |
|
| 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 |
0.522 |
|
| 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 |
0.396 |
|
| 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 DOI: 10.1046/J.1365-2958.1997.4231796.X |
0.461 |
|
| 1997 |
Rüdiger S, Buchberger A, Bukau B. Interaction of Hsp70 chaperones with substrates Nature Structural Biology. 4: 342-349. PMID 9145101 DOI: 10.1038/Nsb0597-342 |
0.44 |
|
| 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 |
0.382 |
|
| 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 |
0.453 |
|
| 1997 |
Bukau B, Schmid FX, Skerra A, Breitenbach U, Darlison MG, Hammar F. Biochemie und Molekulargenetik 1996 Nachrichten Aus Chemie, Technik Und Laboratorium. 45: 166-178. DOI: 10.1002/Nadc.19970450210 |
0.372 |
|
| 1996 |
Langer T, Buchner J, Bukau B. Chaperone function on Crete: A meeting report Cell Stress and Chaperones. 1: 5-12. PMID 9222582 DOI: 10.1379/1466-1268(1996)001<0005:Cfocam>2.3.Co;2 |
0.406 |
|
| 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 |
0.327 |
|
| 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 |
0.523 |
|
| 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 |
0.519 |
|
| 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 |
0.508 |
|
| 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 |
0.472 |
|
| 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 |
0.421 |
|
| 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 DOI: 10.1002/J.1460-2075.1996.Tb00393.X |
0.421 |
|
| 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 |
0.449 |
|
| 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 |
0.451 |
|
| 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 DOI: 10.1002/J.1460-2075.1995.Tb07253.X |
0.452 |
|
| 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 |
0.425 |
|
| 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 |
0.507 |
|
| 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 |
0.432 |
|
| 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 |
0.524 |
|
| 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 |
0.409 |
|
| 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 DOI: 10.1038/Nsb0294-95 |
0.541 |
|
| 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. The Embo Journal. 13: 1687-1695. DOI: 10.1002/J.1460-2075.1994.Tb06433.X |
0.505 |
|
| 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 DOI: 10.1099/00221287-139-1-95 |
0.566 |
|
| 1993 |
Bukau B. Regulation of the Escherichia coli heat-shock response Molecular Microbiology. 9: 671-680. PMID 7901731 DOI: 10.1111/J.1365-2958.1993.Tb01727.X |
0.443 |
|
| 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 DOI: 10.1002/J.1460-2075.1993.Tb06097.X |
0.521 |
|
| 1993 |
Schröder H, Langer T, Hartl F, Bukau B. DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. The Embo Journal. 12: 4137-4144. DOI: 10.1002/j.1460-2075.1993.tb06097.x |
0.324 |
|
| 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 |
0.416 |
|
| 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 |
0.481 |
|
| 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 DOI: 10.1002/J.1460-2075.1990.Tb07624.X |
0.556 |
|
| 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 DOI: 10.1128/Jb.171.11.6030-6038.1989 |
0.523 |
|
| 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 DOI: 10.1128/Jb.171.5.2337-2346.1989 |
0.522 |
|
| 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 DOI: 10.1128/Jb.166.3.706-712.1986 |
0.543 |
|
| 1986 |
Bukau B, Ehrmann M, Boos W. Osmoregulation of the maltose regulon in Escherichia coli. Journal of Bacteriology. 166: 884-91. PMID 2423504 DOI: 10.1128/Jb.166.3.884-891.1986 |
0.707 |
|
| 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 DOI: 10.1128/Jb.163.1.61-68.1985 |
0.561 |
|
| 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 DOI: 10.1128/Jb.155.1.97-106.1983 |
0.453 |
|
| Show low-probability matches. |
