Publikationen

Publikationen AK Synthetische und Strukturelle Biochemie

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. bioRxiv doi: doi.org/10.1101/2020.07.01.182683

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 Engl. Angew. Chem. Int. Ed. 2020, 59, 11607–11612 doi.org/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. Nat Communications, 11 doi.org/10.1038/s41467-020-15287-9

 

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

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.,pii: ddz098. doi: 10.1093/hmg/ddz098. [Epub ahead of print]

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.

 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.

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.

 

2016

Knyphausen, P., de Boor, S. Scislowski, L., Extra, A., Baldus, L., Kuhlmann, N., Schacherl, M., Baumann, U., Neundorf, I., and Lammers, M. (2016) Mechanistic insights into lysine-deacetylation of natively folded substrate proteins by sirtuins. J. Biol. Chem., 291:14677-14694.

Knyphausen, P., Lang, F., Baldus, L., Extra, A. and Lammers, M. (2016) Insights into K-Ras 4B regulation by post-translational lysine acetylation. Biological Chemistry,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.

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.

 

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.

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. PNAS112:E3679–E3688.

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.

 

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