- Bioinformatics and molecular modeling of proteins
- Enzyme design for biocatalysis
- J. Pleiss. “Thermodynamic activity-based interpretation of enzyme kinetics”. In: Trends Biotechnology 35.5 (2017), pp. 379–382.
- P. C. F. Buchholz, C. Vogel, W. Reusch, M. Pohl, D. Rother, A. C. Spieß, and J. Pleiss. “BioCatNet: a database system for the integration of enzyme sequences and biocatalytic experiments”. In: ChemBioChem 17.21 (2016), pp. 2093–2098.
- S. Fademrecht, P. N. Scheller, B. M. Nestl, B. Hauer, and J. Pleiss. “Identification of imine reductase-specific sequence motifs”. In: Proteins 84.5 (2016), pp. 600–610.
- T. Kulschewski and J. Pleiss. “Binding of solvent molecules to a protein surface in binary mixtures follows a competitive Langmuir model”. In: Langmuir 32.35 (2016), pp. 8960–8968.
- A. Taudt, A. Arnold, and J. Pleiss. “Simulation of protein association - Kinetic pathways towards crystal contacts”. In: Physical Review E 91.3 (2015), p. 033311.
- C. Vogel and J. Pleiss. “The modular structure of ThDP-dependent enzymes”. In: Proteins 82.10 (2014), pp. 2523–2537.
- T. Kulschewski, F. Sasso, F. Secundo, M. Lotti, and J. Pleiss. “Molecular mechanism of deactivation of C. antarctica lipase B by methanol”. In: Journal of Biotechnology 168.4 (2013), pp. 462–469.
- A. Seifert, S. Vomund, K. Grohmann, S. Kriening, V. B. Urlacher, S. Laschat, and J. Pleiss. “Rational design of a minimal and highly enriched CYP102A1 mutant library with improved regio-, stereo- and chemoselectivity”. In: ChemBioChem 10.5 (2009), pp. 853–861.
- P. Ölschlaeger, S. L. Mayo, and J. Pleiss. “Impact of remote mutations on metallo-betalactamase substrate specificity: implications for the evolution of antibiotic resistance”. In: Protein Science 14.3 (2005), pp. 765–774.
- J. Pleiss, M. Fischer, and R. D. Schmid. “Anatomy of lipase binding sites: the scissile fatty acid binding site”. In: Chemistry and Physics of Lipids 93.1 (1998), pp. 67–80.
- since 2001 Akademischer Oberrat, Institute of Biochemistry and Technical Biochemistry, University of Stuttgart
- 1995–2001 Akademischer Rat, Institute of Biochemistry and Technical Biochemistry, University of Stuttgart
- 1994 Research scientist, Institute of Organic Chemistry, University of Stuttgart
- 1991–1993 Product Line Manager, Biostructure S.A., Strasbourg
- 1990 Postdoctoral fellow, Max-Planck-Institute of Biology, Tübingen
Academic Studies and Degrees
- 2006 Apl.Professor (Bioinformatics and computational biology)
- 2001 Habilitation, Faculty of Earth and Life Sciences, University of Stuttgart
- 1990 Dr.rer.nat., University of Tübingen
- 1987–1990 Doctoral thesis at Max-Planck-Institute of Biology, Tübingen
- 1986 Diploma in Physics, University of Tübingen
- 1982–1986 Study of Physics, University of Tübingen
- 1980–1982 Study of Physics, University of Stuttgart
- 2003 Offer for a full professorship in bioinformatics at the Technical University of Graz
- 2003 Merit medal “Science and Technology” of the Socialist Republic of Vietnam
- Coordinator of a BMBF-funded German-Vietnamese Research and Training Program in bioinformatics and biotechnology (1998–2006) and member of BMBF delegations (2003, 2005)
- PI of DFG SFB 716 “Particle Simulation” (since 2007) and Member of the Executive Committee (2011–2014)
- PI of the DFG FOR 1296 “Diversity of Asymmetric Thiamine Catalysis” (since 2010)
- Steering committee of the annual “European Summer School on Industrial Biotechnology” (since 2015)
- Organizing committee of the CECAM workshop 1023 “Biological molecules under non-natural conditions” (2014) and 1598 “Proteins in realistic environments: simulation meets experiment” (2018)
- Evaluator for EU, DFG, BMBF, DAAD, NWO, STW, ANR, FWF
- Evaluation panel EU-NEST-Pathfinder (2005)
- Selected Patents (with co-inventors)
- Method for the biocatalytic cyclization of terpenes and cyclase employable therein, US2016340666 (2016)
- Modified Cytochrome P450 monooxygenases, CY1107811 (2013)
- Method for the biocatalytic cyclization of terpenes and cyclase mutants which can be used in said method, EP2640835 (2013)
- Cytochrome P450 monooxygenases and their use for oxidizing organic compounds, US7960155 (2011)
- Modified lipolytic enzymes and their use EP1130100 (2001)
- Cyto-chrome P450 monooxygenase for oxidizing organic compounds, useful especially for converting indole to indigo, has wide substrate range, DE19955605 (2001)