Ruprecht-Karls-Universität Heidelberg


Publications by the Bukau Lab (present - 2011)

see publications 2010 - 2004
see publications 2003 - 1983
search pubmed for current publications by B. Bukau

 

2023

Günnigmann M., Koubek J., Kramer G., Bukau B. (2023). Selective ribosome profiling as a tool to study interactions of translating ribosomes in mammalian cells. Methods in Enzymology. Academic Press. ISSN 0076-6879. https://doi.org/10.1016/bs.mie.2022.09.006

 

Jawed, A., Ho, C. T., Grousl, T., Shrivastava, A., Ruppert, T., Bukau, B., & Mogk, A. (2023). Balanced activities of Hsp70 and the ubiquitin proteasome system underlie cellular protein homeostasis. Frontiers in molecular biosciences, 9, 1106477. https://doi.org/10.3389/fmolb.2022.1106477

 

2022

Cerullo, F., Filbeck, S., Patil, P. R., Hung, H. C., Xu, H., Vornberger, J., Hofer, F. W., Schmitt, J., Kramer, G., Bukau, B., Hofmann, K., Pfeffer, S., & Joazeiro, C. A. P. (2022). Bacterial ribosome collision sensing by a MutS DNA repair ATPase paralogue. Nature, 603(7901), 509–514.https://doi.org/10.1038/s41586-022-04487-6  

 

Reinle, K., Mogk, A., & Bukau, B. (2022). The Diverse Functions of Small Heat Shock Proteins in the Proteostasis Network. Journal of molecular biology, 434(1), 167157. https://doi.org/10.1016/j.jmb.2021.167157

 

Shrivastava, A., Sandhof, C. A., Reinle, K., Jawed, A., Ruger-Herreros, C., Schwarz, D., Creamer, D., Nussbaum-Krammer, C., Mogk, A., & Bukau, B. (2022). The cytoprotective sequestration activity of small heat shock proteins is evolutionarily conserved. The Journal of cell biology, 221(10), e202202149. https://doi.org/10.1083/jcb.202202149


2021

Sharma, A.K., Venezian, J., Shiber, A., Kramer, G., Bukau, B., O´Brien E.P. Combinations of slow-translating codon clusters can increase mRNA half-life in Saccharomyces cerevisiae. (2021) Proc. Nat. Acad. Sci., 118: e2026362118. https://doi.org/10.1073/pnas.2026362118.

Friedrich, U.A., Zedan, M., Hessling, B., Fenzl, K., Gillet. L., Barry, J., Knop, M., Kramer, G., Bukau, B. N α-terminal acetylation of proteins by NatA and NatB serves distinct physiological roles in Saccharomyces cerevisiae. (2021) Cell Rep. 34: 108711, https://doi.org/10.1016/j.celrep.2021.108711.

Bertolini, M., Fenzl, K., Kats, I., Wruck, F., Tippmann, F. Schmitt, J., Auburger, J.J., Tans, S., Bukau, B., Kramer, G. Interactions between nascent proteins translated by adjacent ribosomes drive homomer assembly. (2021) Science 371: 57-64, doi: https://doi.org/10.1126/science.abc7151.

Reinle, K., Mogk, A., Bukau, B. The diverse functions of small heat shock proteins in the proteostasis network. (2021) J. Mol. Biol. 14:167157. doi: 10.1016/j.jmb.2021.167157. Online ahead of print.

2020

Wentink, A.S., Nillegoda, N.B., Feufel, J., Ubartaite, G., Schneider, C.P., De Los Rios, P., Hennig, J., Barducci, A., Bukau, B. Molecular dissection of amyloid disaggregation by the human Hsp70 chaperone. (2020) Nature, https://doi.org/10.1038/s41586-020-2904-6.
PNAS Journal Club: "Insights into heat shock protein machinery could point to interventions for neurodegenerative disease" by Amy McDermott, 20 November 2020 (read more).

Faust, O., Abayev-Avraham, M., Wentink, A.S., Maurer, M., Nillegoda, N.B., London, N., Bukau, B., Rosenzweig, R. Hsp40s employ class-specific regulation to drive Hsp70 functional diversity. (2020) Nature, https://doi.org/10.1038/s41586-020-2906-4.
PNAS Journal Club: "Insights into heat shock protein machinery could point to interventions for neurodegenerative disease" by Amy McDermott, 20 November 2020 (read more).

Ahmed, N., Friedrich, U.A., Sormanni, P., Ciryam, P., Altman, N.S., Bukau, B., Kramer, G., O'Brien, E.P. Pairs of amino acids at the P- and A-sites of the ribosome predictably and causally modulate translation-elongation rates. (2020) J. Mol. Biol. S0022-2836(20)30614-8. doi: 10.1016/j.jmb.2020.10.030. Online ahead of print. (Abstract).


Bohlen, J., Harbrecht, L., Blanco, S., Clemm von Hohenberg, K., Fenzl, K., Kramer, G., Bukau, B., Teleman, A.A. DENR promotes translation reinitiation via ribosome recycling to drive expression of oncogenes including ATF4. (2020) Nat. Commun. 11:4676. doi: 10.1038/s41467-020-18452-2. (Abstract).


Nachman, E., Wentink, A.S., Madiona, K., Bousset, L., Katsinelos, T., Allinson, K., Kampinga, H., McEwan, W.A., Jahn, T.R., Melki, R., Mogk, A., Bukau, B., Nussbaum-Krammer, C. Disassembly of Tau Fibrils by the Human Hsp70 Disaggregation Machinery Generates Small Seeding-Competent Species. (2020) J. Biol. Chem. jbc.RA120.013478. doi: 10.1074/jbc.RA120.013478. (Abstract).


Serlidaki, D., van Waarde, M.A.W.H., Rohland, L., Wentink, A.S., Dekker, S.L., Kamphuis, M.J., Boertien, J.M., Brunsting, J.F., Nillegoda, N.B., Bukau, B., Mayer M.P., Kampinga, H.H., Bergink, S. Functional diversity between HSP70 paralogs due to variable interactions with specific co-chaperones. (2020) J. Biol. Chem. 295:7301-7316. doi: 10.1074/jbc.RA119.012449. PMID: 32284329. (Abstract).


Bohlen, J., Fenzl, K., Kramer, G., Bukau, B., Teleman, A.A. Selective 40S footprinting reveals cap-tethered ribosome scanning in human cells. (2020) Mol. Cell S1097-2765(20)30390-7. doi: 10.1016/j.molcel.2020.06.005. (Abstract).


den Brave F, Cairo L.V., Jagadeesan, C., Ruger-Herreros, C., Mogk, A., Bukau, B., Jentsch, S. Chaperone-Mediated Protein Disaggregation Triggers Proteolytic Clearance of Intra-nuclear Protein Inclusions. (2020) Cell Rep. 31:107680. doi: 10.1016/j.celrep.2020.107680. PMID: 32492414. (Abstract).


Tittelmeier, J., Sandhof, C.A., Ries, H.M., Druffel-Augustin, S., Mogk, A., Bukau, B., Nussbaum-Krammer, C. The HSP110/HSP70 disaggregation system generates spreading-competent toxic alpha-synuclein species. (2020) EMBO J. 39:e103954. doi: 10.15252/embj.2019103954. (Abstract).


Avellaneda, M.J., Franke, K.B., Sunderlikova, V., Bukau, B., Mogk, A., Tans, S.J. Processive extrusion of polypeptide loops by a Hsp100 disaggregase. (2020) Nature, doi: 10.3390/ijms20246220. (Abstract).


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. (2019) Int. J. Mol.Sci. 20(24). pii: E6220. doi: 10.3390/ijms20246220. (Abstract).


Ho, C.-T., Grousl, T., Shatz, O., Jawed, A., Rutger-Herreros, C., Semmelink, M., Zahn, R., Richter, K., Bukau, B., Mogk, A. Cellular sequestrases maintain basal Hsp70 capacity ensuring balanced proteostasis. (2019) Nature Commun. 10:4851. doi: 10.1038/s41467-019-12868-1. (Abstract).


Rusu, P., Shao, C., Neuerburg, A., Acikgöz, A.A., Wu, Y., Zou, P., Phapale, P., Shankar, T.S., Döring, K., Dettling, S., Körkel-Qu, H., Bekki, G., Costa, B., Guo, T., Friesen, O., Schlotter, M., Heikenwalder, M., Tschaharganeh. D.F., Bukau, B., Kramer, G., Angel, P., Herold-Mende, C., Radlwimmer, B., Liu, H.K. GPD1 Specifically Marks Dormant Glioma Stem Cells with a Distinct Metabolic Profile. (2019) Cell Stem Cells pii: S1934-5909(19)30268-1. doi: 10.1016/j.stem.2019.06.004. (Abstract).


Rosenzweig, R., Nillegoda, N.B., Mayer, M.P., Bukau, B. The Hsp70 chaperone network. (2019) Nat. Rev. Mol. Cell Biol. doi: 10.1038/s41580-019-0133-3 (Abstract).


Jamshad, M., Knowles, T.J., White, S.A., Ward, D.G., Mohammed, F., Rahman, K.F., Wynne, M., Hughes, G.W., Kramer, G., Bukau, B., Huber, D. The C-terminal tail of the bacterial translocation ATPase SecA modulates its activity. (2019) Elife pii: e48385. doi: 10.7554/eLife.48385 (Abstract).


Deville, C., Franke, K., Mogk, A., Bukau, B., Saibil, H.R. Two-Step Activation Mechanism of the ClpB Disaggregase for Sequential Substrate Threading by the Main ATPase Motor. (2019) Cell Rep. pii: e48385. doi: 10.7554/eLife.48385 (Abstract).


Maurer, M., Linder, D., Franke, K.B., Jäger, J., Taylor, G., Gloge, F., Gremer, S., Le Breton, L., Mayer, M.P., Weber-Ban, E., Carroni, M., Bukau, B., Mogk, A. Toxic Activation of an AAA+ Protease by the Antibacterial Drug Cyclomarin A. (2019) Cell Chem. Biol., pii: S2451-9456(19)30177-1. doi: 10.1016/j.chembiol.2019.05.008 (Abstract).


Mogk, A., Ruger-Herreros, C., Bukau, B. Cellular Functions and Mechanisms of Action of Small Heat Shock Proteins. (2019) Annu. Rev. Microbiol. doi: 10.1146/annurev-micro-020518-115515 (Abstract).


Wentink, A., Nussbaum-Krammer, C., Bukau, B. Modulation of Amyloid States by Molecular Chaperones. (2019) Cold Spring Harb Perspect Biol., pii: a033969. doi: 10.1101/cshperspect.a033969 (Abstract).


2018

Kramer, G., Shiber, A., Bukau, B. Mechanisms of Co-Translational Maturation of Newly Synthesized Proteins. (2018) Ann. Rev. Biochem., doi: 10.1146/annurev-biochem-013118-111717 (Abstract).


Shiber, A., Döring, K., Friedrich, U., Klann, K., Merker, D., Zedan, M., Tippmann, F., Kramer, G., Bukau, B. (2018) Co-translational assembly of protein complexes in eukaryotes revealed by ribosome profiling. Nature, doi: 10.1038/s41586-018-0462-y (Abstract).


Nillegoda, N.B., Wentink, A.S., Bukau, B. Protein Disaggregation in Multicellular Organisms. (2018) Trends Biochem. Sci. pii: S0968-0004(18)30024-0. doi: 10.1016/j.tibs.2018.02.003. (Abstract).


Grousl, T., Ungelenk, S., Miller, S., Ho, C.T., Khokhrina, M., Mayer, M.P., Bukau, B., Mogk, A. A prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins. (2018) J. Cell Biol. pii: jcb.201708116. doi: 10.1083/jcb.201708116. (Abstract).


Mogk, A., Bukau, B., Kampinga, H.H. Cellular Handling of Protein Aggregates by Disaggregation Machines. (2018) Mol. Cell 69(2):214-226. doi: 10.1016/j.molcel.2018.01.004. (Abstract).


Lee, C., Franke, K.B., Kamal, S.M., Kim, H., Lünsdorf, H., Jäger, J., Nimtz, M., Trcek, J., Jänsch, L., Bukau, B., Mogk, A., Römling, U. Stand-alone ClpG disaggregase confers superior heat tolerance to bacteria. (2018) Proc. Natl. Acad. Sci. USA 115:E273-E282. doi: 10.1073/pnas.1712051115. (Abstract).


Rampelt, H., Mayer, M.P., Bukau, B. Nucleotide Exchange Factors for Hsp70 Chaperones. (2018) Meth. Mol. Biol. 1709:179-188. doi: 10.1007/978-1-4939-7477-1_13. (Abstract).


2017

Carroni, M., Franke, K.B., 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. (2017) Elife pii: e30120. doi: 10.7554/eLife.30120. (Abstract).


Kirstein, J., Arnsburg, K., Scior, A., Szlachcic, A., Guilbride, D.L., Morimoto, R.I., Bukau, B., Nillegoda, N.B. In vivo properties of the disaggregase function of J-proteins and Hsc70 in Caenorhabditis elegans stress and aging. (2017) Aging Cell doi: 10.1111/acel.12686. (Abstract).


Acosta-Sampson, L., Döring, K., Lin, Y., Yu, V.Y., Bukau, B., Kramer, G., Cate, J.H.D. Role for Ribosome-Associated Complex and Stress-Seventy subfamily B (RAC-Ssb) in integral membrane protein translation. (2017) J. Biol. Chem. pii: jbc.M117.813857. doi: 10.1074/jbc.M117.813857. (Abstract).


Deville, C., Carroni, M., Franke, K.B., Topf, M., Bukau, B., Mogk, A., Saibil, H.R. Structural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase. (2017) Sci Adv. 3:e1701726. doi: 10.1126/sciadv.1701726. (Abstract).


Zemva, J., Fink, C.A., Fleming, T.H., Schmidt, L., Loft, A., Herzig, S., Knieß, R.A., Mayer, M., Bukau, B., Nawroth, P.P., Tyedmers, J. Hormesis enables cells to handle accumulating toxic metabolites during increased energy flux. (2017) Redox Biol. 13:674-686. doi: 10.1016/j.redox.2017.08.007. (Abstract).


Döring, K., Ahmed, N., Riemer, T., Suresh, H.G., Vainshtein, Y., Habich, M., Riemer, J., Mayer, M.P., O'Brien, E.P., Kramer, G., Bukau, B. Profiling Ssb-nascent chain interactions reveals principles of Hsp70-assisted folding. (2017) Cell 170:298-311.e20. doi: 10.1016/j.cell.2017.06.038. (Abstract).


Bascos, N.A.D., Mayer, M.P., Bukau, B., Landry, S.J. The Hsp40 J-domain modulates Hsp70 conformation and ATPase activity with a semi-elliptical spring. (2017) Protein Sci. doi: 10.1002/pro.3223 (Epub ahead of print). (Abstract).


Garcia, V.M., Nillegoda, N.B., Bukau, B., Morano, K.A. Substrate binding by the yeast Hsp110 nucleotide exchange factor and molecular chaperone, Sse1, is not obligate for its biological activities. (2017) Mol. Biol. Cell pii: mbc.E17-01-0070. doi: 10.1091/mbc.E17-01-0070. Epub ahead of print. (Abstract).


Nillegoda, N.B., Stank, A., Malinverni, D., Alberts, N., Szlachcic, A., Barducci, A., De Los Rios, P., Wade, R.C., Bukau, B. Evolution of an intricate J-protein network driving protein disaggregation in eukaryotes. (2017) Elife doi: 10.7554/eLife.24560. (Abstract).


Carra, S., Alberti, S., Arrigo, P.A., , Benesch, J.L., Benjamin, I.J., Boelens, W., Bartelt-Kirbach, B., Brundel, B.J., Buchner, J., Bukau, B., Carver, J.A., Ecroyd, H., Emanuelsson, C., Finet, S., Golenhofen, N., Goloubinoff, P., Gusev, N., Haslbeck, M., Hightower, L.E., Kampinga, H.H., Klevit, R.E., Liberek, K., Mchaourab, H.S., McMenimen, K.A., Poletti, A., Quinlan, R., Strelkov, S.V., Toth, M.E., Vierling, E., Tanguay, R.M. The growing world of small heat shock proteins: from structure to functions. (2017) Cell Stress & Chaperones doi: 10.1007/s12192-017-0787-8 (Abstract).


Franke, K.B., Bukau, B.,Mogk, A. Mutant analysis reveals allosteric regulation of ClpB disaggregase. (2017) Front. Mol. Biosci. doi: 10.3389/fmolb.2017.00006 (Abstract).

Zwirowski S, Klosowska A, Obuchowski I, Nillegoda NB, Piróg A, Zietkiewicz S, Bukau B, Mogk A, Liberek K. Hsp70 displaces small heat shock proteins from aggregates to initiate protein refolding. (2017) EMBO J. 36, 783-796. doi: 10.15252/embj.201593378. (Abstract).

Mogk, A. and Bukau, B. Role of sHsps in organizing cytosolic protein aggregation and disaggregation. (2017) Cell Stress & Chaperones doi: 10.1007/s12192-017-0762-4. [Epub ahead of print] (Abstract).


2016

Ungelenk, S., Moayed, F., Ho, C.T., Grousl, T., Scharf, A., Mashaghi, A., Tans, S., Mayer, M.P., Mogk, A., Bukau, B. Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding. (2016) Nat. Commun. 7, 13673 (Abstract).

Goerke, S., Milde, K.S., Bukowiecki, R., Kunz, P., Klika, K.D., Wiglenda, T., Mogk, A., Wanker, E.E., Bukau, B., Ladd, M.E., Bachert, P., Zaiss, M. Aggregation-induced changes in the chemical exchange saturation transfer (CEST) signals of proteins. (2016) NMR Biomed. doi: 10.1002/nbm.3665. (Abstract).


Mashaghi, A., Bezrukavnikov, S., Minde, D.P., Wentink, A.S., Kityk, R., Zachmann-Brand, B., Mayer, M.P., Kramer, G., Bukau, B., Tans, S.J. Alternative modes of client binding enable functional plasticity of Hsp70. (2016) Nature 539, 448-451 (Abstract).


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. (2016) J. Bacteriol. pii: JB.00622-16. Epub ahead of print. (Abstract).


Kummer, E., Szlachcic, A., Franke, K.B., Ungelenk, S., Bukau, B., Mogk, A. Bacterial and yeast AAA+ disaggregases ClpB and Hsp104 operate through conserved mechanism involving cooperation with Hsp70. (2016) J. Mol. Biol. 428, 4378-4391 (Abstract).


Lange, S., Franks, W.T., Rajagopalan, N., Döring, K., Geiger, M.A., Linden, A., van Rossum, B.J., Kramer, G., Bukau, B., Oschkinat, H. Structural analysis of a signal peptide inside the ribosome tunnel by DNP MAS NMR. (2016) Sci. Adv. 2, e1600379. doi: 10.1126/sciadv.1600379. eCollection 2016 Aug. (Abstract).


Schibich, D., Gloge, F., Pöhner, I., Björkholm, P., Wade, R.C., von Heijne, G., Bukau, B., Kramer, G. Global profiling of SRP interaction with nascent polypeptides. (2016) Nature 536, 219-223, doi: 10.1038/nature19070 (Abstract).

Yonashiro, R., Tahara, E.B., Bengtson, M.H., Khokhrina, M., Lorenz, H., Chen, K.C., Kigoshi-Tansho, Y., Savas, J.N., Yates, J.R., Kay, S.A., Craig, E.A., Mogk, A., Bukau, B., Joazeiro, C.A. The Rqc2/Tae2 subunit of the Ribosome-Associated Quality Control (RQC) complex marks ribosome-stalled nascent polypeptide chains for aggregation. (2016) Elife pii: e11794. doi: 10.7554/eLife.11794. (Abstract)


Nilsson, O.B., 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. (2016) J. Mol. Biol. 428, 1356-1364, pii: S0022-2836(16)00130-3. doi: 10.1016/j.jmb.2016.02.014. (Abstract)

Nissley, D.A., Sharma, A.K., Ahmed, N., Friedrich, U.A., Kramer, G., Bukau, B., O'Brien, E.P. Accurate prediction of cellular co-translational folding indicates proteins can switch from post- to co-translational folding. (2016) Nat. Commun. 7, 10341. doi: 10.1038/ncomms10341. (Abstract)

Sharma, A.K., Bukau, B., O'Brien, E.P. Physical Origins of Codon Positions That Strongly Influence Cotranslational Folding: A Framework for Controlling Nascent-Protein Folding. (2016) J. Am. Chem. Soc. 138, 11801195. doi: 10.1021/jacs.5b08145. (Abstract)

Khmelinskii, A., Meurer, M., Ho, C.T., Besenbeck, B., Füller, J., Lemberg, M.K., Bukau, B., Mogk, A., Knop, M. Incomplete proteasomal degradation of green fluorescent proteins in the context of tandem fluorescent protein timers. (2016) Mol. Biol. Cell 27, 360 - 370. (Abstract)

2015

Nillegoda, N.B., Bukau B. Metazoan Hsp70-based protein disaggregases: emergence and mechanisms. (2015) Front. Mol. Biosci. doi: 10.3389/fmolb.2015.00057. eCollection 2015. Review. (Abstract)

Tryggvesson, A., Ståhlberg, F.M., Töpel, M., Tanabe, N., Mogk, A., Clarke, A.K. Characterization of ClpS2, an essential adaptor protein for the cyanobacterium Synechococcus elongatus. (2015) FEBS Lett. doi: 589(24 Pt B):4039-4046. doi: 10.1016/j.febslet.2015.11.026. (Abstract)

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. (2015) FEBS Lett. 589, 3654-3664. doi: 10.1016/j.febslet.2015.10.010. (Abstract).

Shieh, Y.-W., Minguez, P., Bork, P., Auburger, J.J., Guilbride, D.L., Kramer, G., Bukau, B. Operon structure and cotranslational subunit association direct protein assembly in bacteria. (2015) Science 350, 678 - 680 (Abstract).

Kityk, R., Vogel, M., Schlecht, R., Bukau, B., Mayer, M.P. Pathways of allosteric regulation in Hsp70 chaperones. (2015) Nat. Commun. 6, 8308, doi: 10.1038/ncomms9308. (Abstract).

Gao, X., Carroni, M., Nussbaum-Krammer, C., Mogk, A., Nillegoda, N.B., Szlachcic, A., Guilbride, D.L., Saibil, H.R. Mayer, M.P., Bukau, B. Human Hsp70 Disaggregase Reverses Parkinson's-Linked α-Synuclein Amyloid Fibrils. (2015) Mol. Cell 59, 781-793. doi: 10.1016/j.molcel.2015.07.012 (Abstract).

Nillegoda, N.B., Kirstein, J., Szlachcic, A., Berynskyy, M., Stank, A., Stengel, F., Arnsburg, K., Gao, X., Scior, A., Aebersold, R., Guilbride, D.L., Wade, R.C., Morimoto, R.I., Mayer, M.P., Bukau, B. Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation. (2015) Nature 524, 247 - 251, doi:10.1038/nature14884 (read more).

Kramer, G., Bukau, B. 18 The busy life of nascent chains: mechanisms of folding of newly synthesized proteins. (2015) J. Biomol. Struct. Dyn. 33 Suppl 1:10. doi: 10.1080/07391102.2015.1032558 (Abstract).

Mogk, A., Kummer, E., Bukau, B. Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregation. (2015) Front. Mol. Biosci. 2, 22, doi: 10.3389/fmolb.2015.00022. eCollection 2015. (Abstract).

Goerke, S., Zaiss, M., Kunz, P., Klika, K.D., Windschuh, J.D., Mogk, A., Bukau, B., Ladd, M.E., Bachert, P. Signature of protein unfolding in chemical exchange saturation transfer imaging. (2015) NMR Biomed. 28, 906-913. (Abstract).

Garadi Suresh, H., Xavier da Silveira dos Santos, A., 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. (2015) Mol. Biol. Cell 26, 1601-1615 (Abstract).

Kramer, G., Guilbride, D.L., Bukau, B. Cell Biology. Finding nascent proteins the right home. (2015) Science 348, 182-183 (Summary | Full text | Reprint).

Miller, S.B., Ho, C.T., Winkler, J., Khokhrina, M., Neuner, A., Mohamed, M.Y., Guilbride, D.L., Richter, K., Lisby, M., Schiebel, E., Mogk, A., Bukau, B. Compartment-specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition. (2015) EMBO J. 34, 778-797. (Abstract)

Miller, S.B.M., Mogk, A., Bukau, B. Spatially organized aggregation of misfolded proteins as cellular stress defense strategy. (2015) J. Mol. Biol. 427, 1564-1574. (Abstract).

2014

Mogk, A., Bukau, B. Mitochondria tether protein trash to rejuvenate cellular environments. (2014) Cell 159: 471-472 (Article).

Hsieh T.Y., Nillegoda, N.B., Tyedmers, J., Bukau, B., Mogk, A., Kramer, G. Monitoring protein misfolding by site-specific labeling of proteins in vivo. (2014) Plos One 9(6):e99395 (Abstract).

Carroni, M., Kummer, E., Oguchi, Y., Wendler, P., Clare, D.K., Sinning, I., Kopp, J., Mogk, A., Bukau, B., Saibil, H.R. Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. (2014) Elife doi: 10.7554/eLife.02481 (Abstract).

Gloge, F., Becker, A.H., Kramer, G., Bukau, B. Co-translational mechanisms of protein maturation. (2014) Curr. Opin. Struct. Biol. 24, 24-33 (Abstract).

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. (2013) Curr. Biol. 23, 2452-2462 (Abstract).

Schlecht, R. Scholz, S.R., Dahmen, H., Wegener, A., Sirrenberg, C., Musil, D., Bomke, J., Eggenweiler, H.M., Mayer, M.P., Bukau, B. Functional analysis of hsp70 inhibitors. (2013) PLoS One 8(11), e78443 (Abstract). Correction.

Stoecklin, G., Bukau, B. Telling right from wrong in life - cellular quality control. (2013) Nat. Rev. Mol. Cell Biol. 14, 613-615 (Abstract).

Becker, A.H., Oh, E., Weissman, J. S., Kramer, G., Bukau, B. Selective ribosome profiling as a tool to study the interaction of chaperones and targeting factors with nascent polypeptide chains and ribosomes. (2013) Nature Protocols 8, 2212-2239 (Abstract).

Mashaghi, A., Kramer, G., Bechtluft, P., Zachmann-Brand, B., Driessen, A. J., Bukau, B., Tans, S. J. Reshaping of the conformational search of a protein by the chaperone trigger factor. (2013) Nature 500, 98-101 (Abstract).

Sandikci, A., Gloge, F., Martinez, M., Mayer, M.P., Wade, R., Bukau, B., Kramer, G. Dynamic enzyme docking to the ribosome coordinates N-terminal processing with polypeptide folding. (2013) Nat. Struct. Mol. Biol. 20, 843-850 (Abstract).

Tariq, M., Wegrzyn, R., Anwar, S., Bukau, B., Paro, R. Drosophila GAGA factor polyglutamine domains exhibit prion-like behavior. (2013) BMC Genomics 14, 374 (Abstract).

Kummer, E., Oguchi, Y., Seyffer, F., Bukau, B., Mogk, A. Mechanism of Hsp104/ClpB inhibition by prion curing Guanidinium hydrochloride. (2013) FEBS Lett. 587, 810-817 (Abstract).

2012

Oguchi, Y., Kummer, E., Seyffer, F., Berynskyy, M., Anstett, B., Zahn, R., Wade, R.C. Mogk, A., Bukau, B. A tightly regulated molecular toggle controls AAA+ disaggregase. (2012) Nat. Struct. Mol. Biol. 19, 1338-1346 (Abstract).

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. (2012) Nat. Struct. Mol. Biol. 19, 1347-1355 (Abstract).

Rampelt, H., Kirstein-Miles, J., Nillegoda, N.B., Chi, K., Scholz., S.R., Morimoto, R.I., Bukau, B. Metazoan Hsp70 machines use Hsp110 to power protein disaggregation. (2012) EMBO J. 31, 4221-4235 (Abstract).

Hoffmann, A., Becker, A.H., Zachmann-Brand, B., Deuerling, E., Bukau, B., Kramer, G. Concerted action of the ribosome and the associated chaperone trigger factor confines nascent polypeptide folding. (2012) Mol. Cell 48, 63-74 (Abstract).

Hofmann, S., Cherkasova, V., Bankhead, P., Bukau, B., Stoecklin, G. Translation suppression promotes stress granule formation and cell survival in response to cold shock. (2012) Mol. Biol. Cell 23, 3786-3800 (Abstract).

Winkler, J., Tyedmers, J., Bukau, B., Mogk, A. Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. (2012) J. Cell Biol. 198, 387-404 (Abstract).

Winkler, J., Tyedmers, J., Bukau, B., Mogk, A. Chaperone networks in protein disaggregation and prion propagation. (2012) J. Struct. Biol. 179, 152-160 (Abstract).

2011

Oh, E., Becker, A.H., Sandikci, A., Huber, D., Chaba, R., Gloge, F., Nichols, R.J., Typas, A., Gross, C.A., Kramer, G., Weissman, J.S., Bukau, B. Selective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivo. (2011) Cell 147, 1295-1308 (Abstract).

Specht, S., Miller, S.B.M., Mogk, A., Bukau, B. Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae. (2011) J. Cell Biol. 195, 617-629 (Abstract).

Rampelt, H., Mayer, M.P., Bukau, B. Nucleotide exchange factors for Hsp70 chaperones. In "Molecular chaperones: From protein quality control to physiological function", Series "Methods in Molecular Biology. S. Calderwood (Ed) ) (2011) 787, 83-91. (Abstract).

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. (2011) Biol. Chem. 392, 601-608. (Abstract).

Schlecht, R., Erbse, A., Bukau, B., Mayer, M.P. Mechanics of Hsp70 chaperones enables differential interaction with client proteins. (2011) Nat. Struct. Mol. Biol. 18, 345-351 (Abstract).

Huber, D., Rajagopalan, N., Preissler, S., Rocco, M.A., Merz, F., Kramer, G., Bukau, B. SecA interacts with ribosomes in order to facilitate posttranslational translocation in bacteria. (2011) Mol. Cell 41, 343-353 (Abstract).






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