Publikationen

2024

  • Kremer M., Schulze S., Eisenbruch N., Nagel F., Vogt R., Berndt L., Dörre B., Palm G.J., Hoppen J., Girbardt B., Albrecht D., Sievers S., Delcea M., Baumann U., Schnetz K., Lammers M. (2024) Bacteria employ lysine acetylation of transcriptional regulators to adapt gene expression to cellular metabolism. Nature Communications, 15:1674. doi.org/10.1038/s41467-024-46039-8.
  • Tölken L.A., Paulikat A.D., Jachmann L.H., Reder A., Salazar M.G., Palma Medina L.M., Michalik S., Völker U., Svensson M., Norrby-Teglund A., Hoff K.J., Lammers M., Siemens N. (2024) Reduced interleukin-18 secretion by human monocytic cells in response to infections with hyper-virulent Streptococcus pyogenes.Journal of Biomedical Science, 31:26. doi: 10.1186/s12929-024-01014-9

2023

  • Dutschei T., Beidler I., Bartosik D., Seeßelberg J.M., Teune M., Bäumgen M., Ferreira S.Q., Heldmann J., Nagel F., Krull J., Berndt L., Methling K., Hein M., Becher D., Langer P., Delcea M., Lalk M., Lammers M., Höhne M., Hehemann J.H., Schweder T., Bornscheuer U.T. (2023) Marine Bacteroidetes enzymatically digest xylans from terrestrial plants. Environ Microbiol., 25:1713-1727. doi: 10.1111/1462-2920.16390.

2022

  • Nagel F., Palm G.J., Geist N., McDonnell T.C.R., Susemihl A., Girbardt B., Mayerle J., Lerch M.M., Lammers M., Delcea M. (2022) Structural and Biophysical Insights into SPINK1 Bound to Human Cationic Trypsin. International Journal of Molecular Sciences, 23:3468. doi: 10.3390/ijms23073468.
  • Hasan M., Schulze S., Berndt L., Palm G.J., Braga D., Richter I., Last D., Lammers M., Lackner G. (2022) Diversification by CofC and Control by CofD Govern Biosynthesis and Evolution of Coenzyme F 420 and Its Derivative 3PG-F 420. mBio, 13:e0350121. doi: 10.1128/mbio.03501-21.
  • von Haugwitz G., Han X., Pfaff L., Li Q., Wei H., Gao J., Methling K., Ao Y., Brack Y., Mican J., Feiler C.G., Weiss M.S., Bednar D., Palm G.J., Lalk M., Lammers M., Damborsky J., Weber G., Liu W., Bornscheuer U.T., Wei R. (2022) Structural Insights into (Tere)phthalate-Ester Hydrolysis by a Carboxylesterase and Its Role in Promoting PET Depolymerization. ACS Catal., 12:15259-15270. doi: 10.1021/acscatal.2c03772.
  • Pfaff L., Gao J., Li Z., Jäckering A., Weber G., Mican J., Chen Y., Dong W., Han X., Feiler C.G., Ao Y.F., Badenhorst C.P.S., Bednar D., Palm G.J., Lammers M., Damborsky J., Strodel B., Liu W., Bornscheuer U.T., Wei R. (2022) Multiple Substrate Binding Mode-Guided Engineering of a Thermophilic PET Hydrolase. ACS Catal., 12:9790-9800. doi: 10.1021/acscatal.2c02275.
  • Blasl A.T., Schulze S., Qin C., Graf L.G., Vogt R., Lammers M. (2022) Post-translational lysine ac(et)ylation in health, ageing and disease. Biol Chem., 403: 151-194. doi: 10.1515/hsz-2021-0139.

2021

  • Neumann-Staubitz P., Lammers M., Neumann H. (2021) Genetic Code Expansion tools to study lysine acylation. Advanced Biology, e2100926. doi: 10.1002/adbi.202100926.
  • Okada A.K., Ambroso M.R., Isas J.M., Sarandeses E.V., Lee J., Melo A.A., Pandey P., Merken D., Berndt L., Lammers M., Daumke O., Chang K., Haworth I.S., Langen R. (2021) Lysine Acetylation Regulates the Interaction between Proteins and Membranes. Nature Communications, 12:6466. doi: 10.1038/s41467-021-26657-2.
  • Graf L.G., Vogt R., Blasl A.T., Qin C., Schulze S., Zühlke D., Sievers S., Lammers M. (2021)  Assays to study enzymatic and non-enzymatic protein lysine acetylation in vitro. Current Protocols, 1, e277. doi: 10.1002/cpz1.277.
  • Lammers, M. (2021) Post-translational Lysine Ac(et)ylation in Bacteria: A Biochemical, Structural, and Synthetic Biological Perspective. Front. Microbiol., doi: 10.3389/fmicb.2021.757179.
  • Schuiten E.D., Badenhorst C.P.S., Palm G.J., Berndt L., Lammers M., Mican J., Bednar D., Damborsky J., Bornscheuer U.T. (2021) Promiscuous Dehalogenase Activity of the Epoxide Hydrolase CorEH from Corynebacterium sp. C12 ACS Catal., 11:6113−6120. doi: 10.1021/acscatal.1c00851.
  • Müller H., Godehard S.P., Palm G.J., Berndt L., Badenhorst C.P.S., Becker A.K., Lammers M., Bornscheuer U.T. (2021) Discovery and Design of Family VIII Carboxylesterases as Highly Efficient Acyltransferases. Angew Chem Int Ed Engl., 60:2013-2017. doi: 10.1002/anie.202014169.

2020

  • Hermanns T., Woiwode I., Guerreiro R.F.M., Vogt R., Lammers M. and Hofmann K. (2020) An evolutionary approach to systematic discovery of novel deubiquitinases, applied to Legionella. Life Sci. Alliance. doi: 10.26508/lsa.202000838.
  • Müller H., Becker A.K., Palm G.J., Berndt L., Badenhorst C.P.S., Godehard S.P., Reisky L., Lammers M., Bornscheuer U. (2020) Sequence-Based Prediction of Promiscuous Acyltransferase Activity in Hydrolases. Angew. Chem. Int. Ed., 59:11607–11612. doi: 10.1002/anie.202003635.
  • Negrete-Hurtado A., Overhoff M., Bera S.,De Bruyckere E., Schätzmüller K., Qin C., Lammers M., Kondylis V. Neundorf I. And Kononenko N. (2020) Autophagy lipidation machinery regulates axonal microtubule dynamics but is dispensable for survival of mammalian neurons. Nature Communications, 11:1535. doi: 10.1038/s41467-020-15287-9.
  • Schulze S. and Lammers M. (2020) The development of genome editing tools as powerful techniques with versatile applications in biotechnology and medicine: CRISPR/Cas9, ZnF and TALE nucleases, RNA interference, and Cre/loxP.ChemTexts, doi: 10.1007/s40828-020-00126-7.

2019

  • Chen G., Luo Y., Warncke K., Sun Y., Yu D., Fu H., Behera M., Ramalingam S., Doetsch P., Duong D., Lammers M., Curran W. and Deng X. (2019) Acetylation regulates ribonucleotide reductase activity and cancer cell growth. Nature Communications, 10:3213. doi: 10.1038/s41467-019-11214-9.
  • Lammers M., Vogt R., Kremer M., Berndt L. (2019) Lysinacetylierung — eine kleine Modifikation mit großer Wirkung Biospektrum, 25:389-393. doi: 10.1007/s12268-019-1067-1
  • Seenivasan R., Hermanns T., Blyszcz T., Lammers M., Praefcke G.J.K. and Hofmann K. (2019) Mechanism and chain-specificity of RNF216/TRIAD3, the ubiquitin ligase mutated in Gordon-Holmes Syndrome. Hum Mol Genet., 28:2862-2873. doi: 10.1093/hmg/ddz098
  • Hansen B.K., Gupta R., Baldus L., Lyon D., Narita T., Lammers M., Choudhary C. and Weinert B.T. (2019) Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation. Nature Communications, 10:1055. doi: 10.1038/s41467-019-09024-0.

2018

  • Kremer M, Kuhlmann N, Lechner M, Baldus L, Lammers M. (2018) Comment on 'YcgC represents a new protein deacetylase family in prokaryotes'. Elife, 7. pii: e37798. doi: 10.7554/eLife.37798.
  • Gupta R., Somyajit K., Narita T., Maskey E., Stanlie A., Kremer M., Typas D, Lammers M., Mailand N., Nussenzweig A., Lukas J. and Choudhary C. (2018) DNA Repair Network Analysis Reveals Shieldin as a Key Regulator of NHEJ and PARP Inhibitor Sensitivity. Cell, 73:972-988. doi: 10.1016/j.cell.2018.03.050
  •  Lammers M. (2018) Expression and Purification of Site-Specifically Lysine-Acetylated  and Natively-Folded Proteins for Biophysical Investigations. Methods Mol. Biol., 1728:169-190. doi: 10.1007/978-1-4939-7574-7_11.

2017

  • Kuhlmann N, Chollet C, Baldus L, Neundorf I, Lammers M. (2017). Development of Substrate-Derived Sirtuin Inhibitors with Potential Anticancer Activity. ChemMedChem., 2:1703-1714. doi: 10.1002/cmdc.201700414
  • Yin G, Kistler S, George SD, Kuhlmann N, Garvey L, Huynh M, Bagni RK, Lammers M, Der CJ, Campbell SL (2017). A KRAS GTPase K104Q Mutant Retains Downstream Signaling by Offsetting Defects in Regulation. J. Biol. Chem., 292:4446-4456. doi: 10.1074/jbc.M116.762435

2016

  • Knyphausen, P., de Boor, S. Scislowski, L., Extra, A., Baldus, L., Kuhlmann, N., Schacherl, M., Baumann, U., Neundorf, I., Lammers, M. (2016) Mechanistic insights into lysine-deacetylation of natively folded substrate proteins by sirtuins. J. Biol. Chem., 291:14677-14694. doi: 10.1074/jbc.M116.726307.
  • Knyphausen, P., Lang, F., Baldus, L., Extra, A. and Lammers, M. (2016) Insights into K-Ras 4B regulation by post-translational lysine acetylation. Biol. Chem., 397:1071-85. Kuhlmann, N., Wroblowski, S., Scislowski, L., Lammers, M. (2016) RhoGDIa acetylation at K127 and K141 affects binding toward nonprenylated RhoA. Biochemistry, 2:304-312. doi: 10.1021/acs.biochem.5b01242.
  • Kuhlmann, N., Wroblowski, S., Knyphausen, P., de Boor, S., Brenig, J., Baldus, L., Scislowski, L., Meyer-Teschendorf, K., Zienert, A.Y., Praefcke, G.J.K., Nolte, H., Krüger, M., Schacherl, M., Baumann, U.  James, L.C., Chin, J.W., and Lammers, M. (2016) Structural and mechanistic insights into the regulation of the Rho-regulator RhoGDIa by lysine acetylation. J. Biol. Chem., 291:5484-5499. doi: 10.1074/jbc.M115.707091.

2015

  • Knyphausen, P., Kuhlmann, N., de Boor, S., and Lammers, M. (2015) Lysine acetylation as a fundamental regulator of Ran function: Implications for signaling of proteins of the Ras-superfamily. Small GTPases, 6:189-195. doi: 10.1080/21541248.2015.1103399.
  • de Boor, S., Knyphausen, P., Kuhlmann, N., Wroblowski, S., Brenig, J., Scislowski, L., Baldus, L., Nolte, H., Krüger, M.,  and Lammers, M. (2015) The small GTP-binding protein Ran is regulated by post-translational lysine acetylation. PNAS, 112:E3679–E3688. doi: 10.1073/pnas.1505995112.
  • Brenig, J., de Boor, S., Knyphausen, P., Kuhlmann, N., Wroblowski, S., Baldus, L., Scislowski, L., Artz, O., Trauschies, P., Baumann, U., Neundorf, I., and Lammers, M. (2015) Structural and biochemical basis of the inhibitory effect of liprin-a3 on mDia1 function. J. Biol. Chem., 290:14314–14327. doi: 10.1074/jbc.M114.621946.

Previous Years

  • Lammers, M., Neumann, H., Chin, J., and James, L. (2010). Acetylation regulates Cyclophilin A catalysis, immunosuppression and HIV isomerization. Nat. Chem. Biol., 6:331-337.
  • Price, A., Marzetta, F., Lammers, M., Ylinen, L., Schaller, T., Wilson, S., Towers, G., and James, L. (2009). Active site remodeling switches HIV specificity of antiretroviral TRIMCyp. Nat. Struct. Mol. Biol., 16:1036-1042.
  • Lammers, M., Meyer, S., Kühlmann, D., and Wittinghofer, A. (2008). Specificity of Interactions between mDia Isoforms and Rho Proteins. J. Biol. Chem., 283:35236-35246
  • Lammers, M., Rose, R., Scrima, A., and Wittinghofer, A. (2005). The regulation of mDia1 by autoinhibition and its release by Rho*GTP. EMBO J. ,24:4176-4187.
  • Rose, R.*, Weyand, M.*, Lammers, M.*, Ishizaki, T., Ahmadian, M.R., and Wittinghofer, A. (2005). Structural and mechanistic insights into the interaction between Rho and mammalian Dia. Nature ,435:513-518. *equal first authors