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The Department's buildings are currently open for wet laboratory work only. We have carried out a comprehensive COVID-19 risk assessment process and have introduced a number of new measures to ensure the safety of our staff, including reduced building occupancy, strict social distancing, 'family'-based working, and increased cleaning and hygiene regimes. All staff who can work remotely will do so for the foreseeable future. Please continue to contact us by email until further notice.

Department of Biochemistry


Philipp Knyphausen

Joined the lab: April 2016
Background and Current Projects: I studied Biology at the University of Münster and received my M.Sc. in 2012. After a research internship in the group of Nathan Lawson at the UMass Medical School in Worcester during the summer of 2011, I did my Master thesis in the lab of Andy Oates at the MPI-CBG in Dresden where I was working on genetic oscillators and transcription factor stability. During my PhD in the group of Michael Lammers at University of Cologne I studied post-translational lysine-acetylation and the enzymes regulating this protein modification. I joined the Hollfelder group in April 2016 and my project focuses on proteases for therapeutic applications.
Interests: I enjoy producing music on my computer and to go running.

Selected publications
[3] Knyphausen, P., de Boor, S., Kuhlmann, N., Scislowski, L., Extra, A., Baldus, L., Schacherl, M., Baumann, U., Neundorf, I., and Lammers, M. (2016). Insights into lysine-deacetylation of natively folded substrate proteins by sirtuins. J. Biol. Chem. read online
[2] 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. (* equal contribution) read online
[1] de Boor, S.*, Knyphausen, P.*, Kuhlmann, N., Wroblowski, S., Brenig, J., Scislowski, L., Baldus, L., Nolte, H., Krüger, M., and Lammers, M. (2015). Small GTP-binding protein Ran is regulated by posttranslational lysine acetylation. Proc. Natl. Acad. Sci. U.S.A. 112, E3679-3688. (* equal contribution) read online


Philipp Knyphausen 

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