Contact
Allmandring 31
70569 Stuttgart
Germany
Room: 0.307
2022
- Royek, S., Bayer, M., Pfannstiel, J., Pleiss, J., Ingram, G., Stintzi, A., & Schaller, A. (2022). Processing of a plant peptide hormone precursor facilitated by post-translational tyrosine sulfation. Proc Natl Acad Sci USA, 119, e2201195119.
- Mack, A., Emperle, M., Schnee, P., Pleiss, J., Bashtrykov, P., & Jeltsch, A. (2022). Preferential self-interaction of DNA methyltransferase DNMT3A subunits containing the R882H cancer mutation leads to dominant changes of flanking sequence preferences. J Mol Biol, 434, 167482.
- Zhang, H., Pérez-García, P., Dierkes, R., Danso, D., Pleiss, J., Almeida, A., Höcker, B., Schmitz-Streit, R., Chow, J., Streit, W., Applegate, V., Schumacher, J., Chibani, C., Sternagel, S., Preuss, L., Weigert, S., Schmeisser, C., Hallam, S., & Smits, S. (2022). The Bacteroidetes Aequorivita sp. and Kaistella jeonii produce promiscuous esterases with PET-hydrolyzing activity. Front Microbiol, 12, 803896. https://doi.org/10.3389/fmicb.2021.803896
2021
- Orlando, M., Buchholz, P., Lotti, M., & Pleiss, J. (2021). The GH19 Engineering Database: sequence diversity, substrate scope, and evolution in glycoside hydrolase family 19. PLoS One, 16, e0256817. https://doi.org/10.1371/journal.pone.0256817
- Buchholz, P., van, L. B., Eenink, B., Bornberg-Bauer, E., & Pleiss, J. (2021). Ancestral sequences of a large promiscuous enzyme family correspond to bridges in sequence space in a network representation. J R Soc Interface, 18, 20210389. https://doi.org/10.1098/rsif.2021.0389
- Schatz, K., Franco-Moreno, J., Schäfer, M., Rose, A., Ferrario, V., Pleiss, J., Vazquez, P., Ertl, T., & Krone, M. (2021). Visual analysis of large-scale protein-ligand interaction data. Comput Graph Forum, 40, 394–408. https://doi.org/10.1111/cgf.14386
- Schatz, K., Friess, F., Schäfer, M., Buchholz, P., Pleiss, J., Ertl, T., & Krone, M. (2021). Analyzing the similarity of protein domains by clustering molecular surface maps. Comput Graph, 99, 114–127. https://doi.org/10.1016/j.cag.2021.06.007
- Carvalho, H., Ferrario, V., & Pleiss, J. (2021). The molecular mechanism of methanol inhibition in CALB-catalyzed alcoholysis: analyzing molecular dynamics simulations by a Markov state model. J Chem Theory Comput, 17, 6570–6582. https://doi.org/10.1021/acs.jctc.1c00559
- Pleiss, J. (2021). Standardized data, scalable documentation, sustainable storage – EnzymeML as a basis for FAIR data management in biocatalysis. ChemCatChem, 13, 3909–3913. https://doi.org/10.1002/cctc.202100822
- Stockinger, P., Borlinghaus, N., Sharma, M., Aberle, B., Grogan, G., Pleiss, J., & Nestl, B. (2021). Inverting the stereoselectivity of an NADH-dependent imine-reductase variant. ChemCatChem, 13, 5210–5215. https://doi.org/10.1002/cctc.202101057
- Faheem, M., Zhang, C., Morris, M., Pleiss, J., & Oelschlaeger, P. (2021). The role of synonymous mutations in the evolution of TEM β-lactamase genes. Antimicrob Agents Chemother, 65, e00018-21. https://doi.org/10.1128/AAC.00018-21
- Lohoff, C., Buchholz, P., Le, R.-H. M., & Pleiss, J. (2021). The Expansin Engineering Database: a navigation and classification tool for expansins and homologues. Proteins, 89, 149–162. https://doi.org/10.1002/prot.26001
2020
- Stockinger, P., Schelle, L., Schober, B., Buchholz, P., Pleiss, J., & Nestl, B. (2020). Engineering of thermostable β-hydroxyacid dehydrogenase for asymmetric reduction of imines. ChemBioChem, 21, 3511–3514.
- Mangiagalli, M., Carvalho, H., Natalello, A., Ferrario, V., Pennati, M., Barbiroli, A., Lotti, M., Pleiss, J., & Brocca, S. (2020). Diverse effects of aqueous polar co-solvents on Candida antarctica lipase B. Int J Biol Macromol, 150, 930–940. https://doi.org/10.1016/j.ijbiomac.2020.02.145
- Gygli, G., Xu, X., & Pleiss, J. (2020). Meta-analysis of viscosity of aqueous deep eutectic solvents and their components. Sci Rep, 10, 21395–21395. https://doi.org/10.1038/s41598-020-78101-y
- Bauer, T., Buchholz, P., & Pleiss, J. (2020). The modular structure of α/β-hydrolases. FEBS J, 287, 1035–1053. https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.15071
- Eisenkolb, I., Jensch, A., Eisenkolb, K., Kramer, A., Buchholz, P., Pleiss, J., Spiess, A., & Radde, N. (2020). Modeling of biocatalytic reactions: A workflow for model calibration, selection and validation using Bayesian statistics. AIChE J, 66, e16866. https://doi.org/10.1002/aic.16866
- Rifai, E., Ferrario, V., Pleiss, J., & Geerke, D. (2020). A combined linear interaction energy and alchemical solvation free energy approach for protein-binding anity computation. J Chem Theory Comput, 16, 1300–1310.
- Stockinger, P., Roth, S., Müller, M., & Pleiss, J. (2020). Systematic evaluation of imine-reducing enzymes: Common principles in imine reductases, β-hydroxyacid dehydrogenases, and short-chain dehydrogenases/reductases. ChemBioChem, 21, 2689–2695. https://doi.org/10.1002/cbic.202000213
- Malzacher, S., Range, J., Halupczok, C., Pleiss, J., & Rother, D. (2020). BioCatHub, a graphical user interface for standardized data acquisition in biocatalysis. Chem Ing Tech, 92, 1251–1251.
- Gräff, M., Buchholz, P., Le Roes-Hill, M., & Pleiss, J. (2020). Multicopper oxidases: modular structure, sequence space and evolutionary relationships. Proteins.
- Gygli, G., & Pleiss, J. (2020). Simulation Foundry: automated and F.A.I.R. molecular modelling. J Chem Inf Model, 60, 1922–1927. https://doi.org/10.1021/acs.jcim.0c00018
- Xu, X., Range, J., Gygli, G., & Pleiss, J. (2020). Analysis of thermophysical properties of deep eutectic solvents by data integration. J Chem Eng Data, 65, 1172–1179. https://doi.org/10.1021/acs.jced.9b00555
- Roth, S., Stockinger, P., Steff, J., Steimle, S., Sautner, V., Tittmann, K., Pleiss, J., & Müller, M. (2020). Crossing the border: From keto- to imine reduction in short-chain dehydrogenases/reductases. ChemBioChem, 21, 2615–2619.
2019
- Buchholz, P., Ohs, R., Spieß, A., & Pleiss, J. (2019). Progress curve analysis within BioCatNet: comparing kinetic models for enzyme-catalyzed self-ligation. Biotechnol J, 14, e1800183.
- Gräff, M., Buchholz, P., Stockinger, P., Bommarius, B., Bommarius, A., & Pleiss, J. (2019). The Short-chain Dehydrogenase/Reductase Engineering Database (SDRED): A classification and analysis system for a highly diverse enzyme family. Proteins, 87, 443–451.
- Gobeil, S., Ebert, M., Park, J., Gagné, D., Doucet, N., Berghuis, A., Pleiss, J., & Pelletier, J. (2019). The structural dynamics of engineered β-lactamases vary broadly on three timescales yet sustain native function. Sci Rep, 9, 6656–6656.
- Schatz, K., Krone, M., Pleiss, J., & Ertl, T. (2019). Interactive visualization of biomolecules’ dynamic and complex properties. Eur Phys J Special Topics, 227, 1725–1739.
- Fries, A., Mazzaferro, L., Grüning, B., Bisel, P., Stibal, K., Buchholz, P., Pleiss, J., Sprenger, G., & Müller, M. (2019). Alteration of the route to menaquinone towards isochorismate - derived metabolites. ChemBioChem, 20, 1672–1677.
- Baz, J., Held, C., Pleiss, J., & Hansen, N. (2019). Thermophysical properties of glyceline-water mixtures investigated by molecular modelling. Phys Chem Chem Phys, 21, 6467–6476. https://doi.org/10.1039/C9CP00036D
- Ferrario, V., & Pleiss, J. (2019). Molecular simulations of enzymes under non-natural conditions. Eur Phys J Special Topics, 227, 1631–1638.
- Demming, R., Hammer, S., Nestl, B., Gergel, S., Fademrecht, S., Pleiss, J., & Hauer, B. (2019). Asymmetric Enzymatic Hydration of Unactivated, Aliphatic Alkenes. Angew Chem Int Ed Engl, 58, 173–177.
- Buchholz, P., Ferrario, V., Pohl, M., Gardossi, L., & Pleiss, J. (2019). Navigating within thiamine diphosphate-dependent decarboxylases: Sequences, structures, functional positions, and binding sites. Proteins, 87, 774–785.
- Ferrario, V., Fischer, M., Zhu, Y., & Pleiss, J. (2019). Modelling of substrate access and substrate binding to cephalosporin acylases. Sci Rep, 9, 12402. https://doi.org/10.1038/s41598-019-48849-z
- Grüninger, M., Buchholz, P., Mordhorst, S., Strack, P., Müller, M., Hubrich, F., Pleiss, J., & Andexer, J. (2019). Chorismatases – the family is growing. Org Biomol Chem, 17, 2092–2098.
- Roddan, R., Gygli, G., Sula, A., Mendez-Sanchez, D., Pleiss, J., Ward, J., Keep, N., & Hailes, H. (2019). The acceptance and kinetic resolution of alpha-methyl substituted aldehydes by norcoclaurine synthases. ACS Catal, 9, 9640–9649. https://pubs.acs.org/doi/abs/10.1021/acscatal.9b02699
2018
- Ferrario, V., Hansen, N., & Pleiss, J. (2018). Interpretation of cytochrome P450 monooxygenase kinetics by modeling of thermodynamic activity. J Inorg Biochem, 183, 172–178. https://doi.org/10.1016/j.jinorgbio.2018.02.016
- Lotti, M., Pleiss, J., Valero, F., & Ferrer, P. (2018). Enzymatic production of biodiesel: strategies to overcome methanol inactivation. Biotechnol J, 13, e1700155. https://doi.org/10.1002/biot.201700155
- Lenz, M., Fademrecht, S., Sharma, M., Pleiss, J., Grogan, G., & Nestl, B. (2018). New imine-reducing enzymes from beta-hydroxyacid dehydrogenases by single amino acid substitutions. Protein Engineering, Design and Selection, 31, 109–120.
- Ferrario, V., & Pleiss, J. (2018). Simulation of protein diffusion: a sensitive probe of protein-solvent interactions. J Biomol Struct Dyn, 37, 1534–1544.
- Baierl, A., Theorell, A., Mackfeld, U., Marquardt, P., Hoffmann, F., Moers, S., Nöh, K., Buchholz, P., Pleiss, J., & Pohl, M. (2018). Towards a mechanistic understanding of factors controlling the stereoselectivity of transketolase. ChemCatChem, 10, 2601–2611.
- Pleiss, J. (2018). Thermodynamic activity-based progress curve analysis in enzyme kinetics. Trends Biotechnol, 36, 234–238.
- Buß, O., Buchholz, P., Gräff, M., Klausmann, P., Rudat, J., & Pleiss, J. (2018). The omega-Transaminase Engineering Database (oTAED): a navigation tool in protein sequence and structure space. Proteins, 86, 566–580.
- Martínez-Martínez, M., Coscolín, C., Santiago, G., Chow, J., Stogios, P., ..., Buchholz, P., Pleiss, J., ..., & Ferrer, M. (2018). Determinants and prediction of esterase substrate promiscuity patterns. ACS Chem Biol, 13, 225–234.
- Buchholz, P., Zeil, C., & Pleiss, J. (2018). The scale-free nature of protein sequence space. PLoS One, 13, e0200815.
2017
- Zhang, Q., Catti, L., Pleiss, J., & Tiefenbacher, K. (2017). Terpene cyclizations inside a supramolecular catalyst: Leaving-group-controlled product selectivity and mechanistic studies. J Am Chem Soc, 139, 11482–11492.
- Benson, S., & Pleiss, J. (2017). Self-assembly nanostructures of triglyceride-water interfaces determine functional conformations of Candida antarctica lipase B. Langmuir, 33, 3151–3159.
- Krone, M., Friess, F., Scharnowski, K., Reina, G., Fademrecht, S., Kulschewski, T., Pleiss, J., & Ertl, T. (2017). Molecular Surface Maps. IEEE Trans Vis Comput Graph, 23, 701–710.
- Buchholz, P., Fademrecht, S., & Pleiss, J. (2017). Percolation in protein sequence space. PLoS One, 12, e0189646.
- Schmid, J., Steiner, L., Fademrecht, S., Pleiss, J., Otte, K., & Hauer, B. (2017). Biocatalytic study of novel oleate hydratases. J Mol Catal B: Enzym, 133, S243–S249.
- Pleiss, J. (2017). Thermodynamic activity–based interpretation of enzyme kinetics. Trends Biotechnol, 35, 379–382.
2016
- Zeil, C., Widmann, M., Fademrecht, S., Vogel, C., & Pleiss, J. (2016). Microdiversity of TEM β-lactamases: a network analysis of sequence-function relationships and exploration of sequence space. Antimicrob Agents Chemother, 60, 2709–2717.
- Bock, S., Buchholz, P., Vogel, C., Holzapfel, A., Pleiss, J., Wiechert, W., Pohl, M., & Rother, D. (2016). Exploring the Sequence-Function Space of ThDP-Dependent Enzymes. Chemie Ingenieur Technik, 88, 1246.
- Benson, S., & Pleiss, J. (2016). Computational modeling of a biocatalyst at a hydrophobic substrate interface. In R. M. Nagel WE, Kröner DH (Ed.), High Performance Computing in Science and Engineering ´15. Springer International Publishing.
- Kulschewski, T., & Pleiss, J. (2016). Binding of solvent molecules to a protein surface in binary mixtures follows a competitive Langmuir model. Langmuir, 32, 8960–8968.
- Notonier, S., Gricman, L., Pleiss, J., & Hauer, B. (2016). Semi-rational protein engineering of CYP153A M.aq.-CPR BM3 for efficient terminal hydroxylation of short to long chain fatty acids. ChemBioChem, 17, 1550–1557.
- Eichler, A., Gricman, L., Herter, S., Kelly, P., Turner, N., Pleiss, J., & Flitsch, S. (2016). Enantioselective benzylic hydroxylation catalysed by P450 monooxygenases: characterisation of a P450cam mutant library and molecular modelling. ChemBioChem, 17, 426–432.
- Jozwik, I., Kiss, F., Gricman, L., Abdulmughni, A., Brill, E., Zapp, J., Pleiss, J., Bernhardt, R., & Thunnissen, A. (2016). Structural basis of steroid binding and oxidation by the cytochrome P450 CYP109E1 from Bacillus megaterium. FEBS J, 283, 4128–4148.
- Widmann, M., & Pleiss, J. (2016). Sequence, structure, function: what we learn from analyzing protein families. In S. A (Ed.), Understanding enzymes. pan Standord Publishing.
- Pleiss, J., & Zeil, C. (2016). Reply to The Curious Case of TEM-116. Antimicrob Agents Chemother, 60, 7001–7001.
- Schäfer, I., Lasko, G., Do, T., Pleiss, J., Weber, U., & Schmauder, S. (2016). Peptide–zinc oxide interaction: Finite element simulation using cohesive zone models based on molecular dynamics simulation. In S. I. Schmauder S (Ed.), Multiscale Materials Modeling. De Gruyter.
- Gricman, L., Weissenborn, M., Hoffmann, S., Borlinghaus, N., Hauer, B., & Pleiss, J. (2016). Redox Partner Interaction Sites in Cytochrome P450 Monooxygenases: In Silico Analysis and Experimental Validation. ChemistrySelect, 6, 1243–1251.
- Buchholz, P., Vogel, C., Reusch, W., Pohl, M., Rother, D., Spieß, A., & Pleiss, J. (2016). BioCatNet: a database system for the integration of enzyme sequences and biocatalytic experiments. ChemBioChem, 17, 2093–2098.
- Hoffmann, S., Weissenborn, M., Gricman, L., Notonier, S., Pleiss, J., & Hauer, B. (2016). The Impact of Linker Length on P450 Fusion Constructs: Activity, Stability and Coupling. ChemCatChem, 8, 1591–1597.
- Fademrecht, S., Scheller, P., Nestl, B., Hauer, B., & Pleiss, J. (2016). Identification of imine reductase-specific sequence motifs. Proteins, 84, 600–610.
2015
- Gricman, L., Vogel, C., & Pleiss, J. (2015). Identification of universal selectivity-determining positions in cytochrome P450 monooxygenases by systematic sequence-based literature mining. Proteins, 83, 1593-1603.
- Prins, A., Kleinsmidt, L., Khan, N., Kirby, B., Kudanga, T., Vollmer, J., Pleiss, J., Burton, S., & Le, R.-H. M. (2015). The effect of mutations near the T1 copper site on the biochemical characteristics of the small laccase from Streptomyces coelicolor A3(2). Enzyme Microb Technol, 68, 23–32.
- Taudt, A., Arnold, A., & Pleiss, J. (2015). Simulation of protein association - Kinetic pathways towards crystal contacts. Phys Rev E, 91, 033311.
- Lotti, M., Pleiss, J., Valero, F., & Ferrer, P. (2015). Effects of methanol on lipases: molecular, kinetic and process issues in the production of biodiesel. Biotechnol J, 10, 22–30.
- Sasso, F., Kulschewski, T., Secundo, F., Lotti, M., & Pleiss, J. (2015). The effect of thermodynamic properties of solvent mixtures explains the difference between methanol and ethanol in C.antarctica lipase B catalyzed alcoholysis. J Biotechnol, 214, 1–8.
2014
- Widmann, M., & Pleiss, J. (2014). Protein variants form a system of networks: microdiversity of IMP metallo-beta-lactamases. PLoS ONE, 9, e101813.
- Westphal, R., Vogel, C., Schmitz, C., Pleiss, J., Müller, M., Pohl, M., & Rother, D. (2014). A Tailor-Made Chimeric Thiamine Diphosphate Dependent Enzyme for the Direct Asymmetric Synthesis of (S)-Benzoins. Angew. Chem. Int. Ed., 53, 9376–9379.
- Scharnowski, K., Krone, M., Reina, G., Kulschewski, T., Pleiss, J., & Ertl, T. (2014). Comparative Visualization of Molecular Surfaces Using Deformable Models. Comput Graph Forum, 3, 191–200.
- Benson, S., & Pleiss, J. (2014). Molecular dynamics simulations of self-emulsifying drug delivery systems (SEDDS): influence of excipients on droplet nanostructure and drug localization. Langmuir, 30, 8471–8480.
- Scheller, P., Fademrecht, S., Hofelzer, S., Pleiss, J., Leipold, F., Turner, N., Nestl, B., & Hauer, B. (2014). Enzyme Toolbox: Novel Enantiocomplementary Imine Reductases. ChemBioChem, 15, 2201–2204.
- Benson, S., & Pleiss, J. (2014). Solvent Flux Method (SFM): A case study of water access to Candida antarctica lipase B. J Chem Theory Comput, 10, 5206–5214.
- Pleiss, J. (2014). Systematic analysis of large enzyme families: identification of specificity- and selectivity-determining hotspots. ChemCatChem, 6, 944–950.
- Gricman, L., Vogel, C., & Pleiss, J. (2014). Conservation analysis of class-specific positions in cytochrome P450 monooxygenases: functional and structural relevance. Proteins, 82, 491–504.
- Westphal, R., Jansen, S., Vogel, C., Pleiss, J., Müller, M., Rother, D., & Pohl, M. (2014). MenD from Bacillus subtilis: A Potent Catalyst for the Enantiocomplementary Asymmetric Synthesis of Functionalized α-Hydroxy Ketones. ChemCatChem, 6, 1082–1088.
- Schäfer, I., Lasko, G., Do, T., Pleiss, J., Weber, U., & Schmauder, S. (2014). Peptide - zinc oxide interaction: finite element simulation using cohesive zone models based on molecular dynamics simulation. Comp Mater Sci, 95, 320–327.
- Bogazkaya, A., von, B. C., Kriening, S., Busch, A., Seifert, A., Pleiss, J., Laschat, S., & Urlacher, V. (2014). Selective allylic hydroxylation of acyclic terpenoids by CYP154E1 from Thermobifida fusca YX. Beilstein J. Org. Chem, 10, 1347–1353.
- Baier, J., Blumenstein, N., Preusker, J., Jeurgens, L., Welzel, U., Do, T., Pleiss, J., & Bill, J. (2014). The influence of ZnO-binding 12-mer peptides on bio-inspired ZnO formation. Cryst Eng Comm, 16, 5301–5307.
- Vogel, C., & Pleiss, J. (2014). The modular structure of ThDP-dependent enzymes. Proteins, 82, 2523–2537.
2013
- Krone, M., Reina, G., Schulz, C., Kulschewski, T., Pleiss, J., & Ertl, T. (2013). Interactive Extraction and Tracking of Biomolecular Surface Features. Comput Graph Forum, 32, 331–340.
- Benson, S., & Pleiss, J. (2013). Incomplete mixing versus clathrate-like structures: a molecular view on hydrophobicity in methanol-water mixtures. J Mol Model, 19, 3427–3436.
- Roduner, E., Kaim, W., Sarkar, B., Urlacher, V., Pleiss, J., Gläser, R., Einicke, W., Sprenger, G., & Beifuss, U. (2013). Selective catalytic oxidation of CH bonds with molecular oxygen. ChemCatChem, 5, 82–112.
- Hailes, H., Rother, D., Müller, M., Westphal, R., Ward, J., Pleiss, J., Vogel, C., & Pohl, M. (2013). Engineering stereoselectivity of ThDP-dependent enzymes. FEBS J, 280, 6374–6394.
- Kulschewski, T., & Pleiss, J. (2013). A molecular dynamics study of liquid aliphatic alcohols: simulation of density and self-diffusion coefficient using a modified OPLS force field. Mol Simulat, 39, 754–767.
- Westphal, R., Waltzer, S., Mackfeld, U., Widmann, M., Pleiss, J., Beigi, M., Müller, M., Rother, D., & Pohl, M. (2013). (S)-Selective MenD variants from Escherichia coli provide access to new functionalized chiral 2-hydroxy ketones. Chem Commun, 49, 2061–2063.
- Kulschewski, T., Sasso, F., Secundo, F., Lotti, M., & Pleiss, J. (2013). Molecular mechanism of deactivation of C. antarctica lipase B by methanol. J Biotechnol, 168, 462–469.
- Westphal, R., Hahn, D., Mackfeld, U., Waltzer, S., Beigi, M., Widmann, M., Vogel, C., Pleiss, J., Müller, M., & Pohl, M. (2013). Tailoring (S)-selectivity of MenD from Escherichia coli. ChemCatChem, 13, 3587–3594.
2012
- Fademrecht, S., Juhl, P., Sirim, D., & Pleiss, J. (2012). The triterpene cyclase protein family: a systematic analysis. Proteins, 80, 2009–2019.
- Kulschewski, T., & Pleiss, J. (2012). Simulation of enzymes in organic solvents. In S. Lutz & U. Bornscheuer (Eds.), Protein engineering handbook, vol.3. Wiley-VCH.
- Gruber, C., & Pleiss, J. (2012). Lipase B from Candida antarctica binds to hydrophobic substrate-water interfaces via hydrophobic anchors surrounding the active site entrance. J Mol Catal B, 84, 48–54.
- Seifert, A., & Pleiss, J. (2012). Identification of selectivity determinants in CYP monooxygenases by modelling and systematic analysis of sequence and structure. Curr Drug Metab, 13, 197–202.
- Siedenburg, G., Jendrossek, D., Breuer, M., Juhl, B., Pleiss, J., Seitz, M., Klebensberger, J., & Hauer, B. (2012). Activation-independent cyclization of monoterpenoids. Appl Environ Microbiol, 78, 1055–1062.
- Pickel, B., Pfannstiel, J., Steudle, A., Lehmann, A., Gerken, U., Pleiss, J., & Schaller, A. (2012). A model of dirigent proteins derived from structural and functional similarities with alleneoxide cyclase and lipocalins. FEBS J, 279, 1980–1993.
- Baier, J., Naumburg, T., Blumenstein, N., Jeurgens, L., Welzel, U., Do, T., Pleiss, J., & Bill, J. (2012). Bio-inspired mineralization of zinc oxide in presence of ZnO-binding peptides. Biointerface Res Appl Chem, 2, 380–391.
- Widmann, M., Pleiss, J., & Oelschlaeger, P. (2012). Systematic analysis of metallo-b-lactamases using an automated database. Antimicrob Agents Ch, 56, 3481–3491.
- Pleiss, J. (2012). Rational design of enzymes. In K. Drauz, H. Gröger, & O. May (Eds.), Enzyme catalysis in organic synthesis. Wiley-VCH.
- Widmann, M., Pleiss, J., & Samland, A. (2012). Computational tools for rational protein engineering of aldolases. Comput Struct Biotechnol J, 2, e201209016–e201209016.
- Ferrario, V., Braiuca, P., Tessaro, P., Knapic, L., Gruber, C., Pleiss, J., Ebert, C., Eichhorn, E., & Gardossi, L. (2012). Elucidating the structural and conformational factors responsible for the activity and substrate specificity of alkanesulfonate monooxygenase. J Biomol Struct Dyn, 30, 74–88.
- Gruber, C., & Pleiss, J. (2012). Molecular modeling of lipase binding to a substrate-water interface. Methods Mol Biol, 861, 313–327.
- Hutt, M., Kulschewski, T., & Pleiss, J. (2012). Molecular modelling of the mass density of single proteins. J Biomol Struct Dyn, 30, 318–327.
- Vogel, C., Widmann, M., Pohl, M., & Pleiss, J. (2012). A standard numbering scheme for thiamine diphosphate-dependent decarboxylases. BMC Biochemistry, 13, 24–24.
2011
- Rother, D., Kolter, G., Gerhards, T., Berthold, C., Gauchenova, E., Knoll, M., Pleiss, J., Müller, M., Schneider, G., & Pohl, M. (2011). S-selective mixed carboligation by structure-based design of the pyruvate decarboxylase from Acetobacter pasteurianus. ChemCatChem, 3, 1587–1596.
- Habeych, D., Juhl, P., Pleiss, J., Vanegas, D., Eggink, G., & Boeriu, C. (2011). Biocatalytic synthesis of polyesters from sugar-based building blocks using immobilized Candida antarctica lipase B. J Mol Catal B - Enzym, 71, 1–9.
- Steudle, A., & Pleiss, J. (2011). Modelling of lysozyme binding to a cation exchange surface at atomic detail: the role of flexibility. Biophys.J., 100, 3016–3024.
- Pleiss, J. (2011). Protein design in metabolic engineering and synthetic biology. Curr.Opin.Biotech., 22, 1–7.
- Seifert, A., Antonovici, M., Hauer, B., & Pleiss, J. (2011). An efficient route to selective bio-oxidation catalysts: an iterative approach comprising modeling, diversification, and screening, based on CYP102A1. ChemBioChem, 12, 1346–1351.
- Krone, M., Falk, M., Rehm, S., Pleiss, J., & Ertl, T. (2011). Interactive exploration of protein cavities. Comput Graph Forum, 30, 673–682.
- Weber, E., Seifert, A., Antonovici, M., Geinitz, C., Pleiss, J., & Urlacher, V. (2011). Screening of a minimal enriched P450 BM3 mutant library for hydroxylation of cyclic and acyclic alkanes. Chem.Commun., 47, 944–946.
- Sirim, D., Wagner, F., Wang, L., Schmid, R., & Pleiss, J. (2011). The Laccase Engineering Database: a classification and analysis system for laccases and related multicopper oxidases. Database, bar006.
- Gruber, C., & Pleiss, J. (2011). Systematic benchmarking of large molecular dynamics simulations employing GROMACS on massive multiprocessing facilities. J.Comput.Chem., 32, 600–606.
2010
- Widmann, M., Juhl, P., & Pleiss, J. (2010). Structural classification by the Lipase Engineering Database: a case study of Candida antarctica lipase A. BMC Genomics, 11, 123.
- Juhl, P., Doderer, K., Hollmann, F., Thum, O., & Pleiss, J. (2010). Engineering of Candida antarctica lipase B forhydrolysis of bulky carboxylic acid esters. J Biotechnol, 150, 474–480.
- Thai, K., & Pleiss, J. (2010). SHV Lactamase Engineering Database: a reconciliation tool for SHV β-lactamases in public databases. BMC Genomics, 11, 563–563.
- Rehm, S., Trodler, P., & Pleiss, J. (2010). Solvent-induced lid opening in lipases: A molecular dynamics study. Protein Sci., 19, 2122–2130.
- Widmann, M., Radloff, R., & Pleiss, J. (2010). The Thiamine diphosphate dependent Enzyme Engineering Database: A tool for the systematic analysis of sequence and structure relations. BMC Biochemistry, 11, 9–9.
- Liu, D., Trodler, P., Eiben, S., Koschorrek, K., Mueller, M., Pleiss, J., Maurer, S., Branneby, C., & Schmid, R. (2010). Rational Design of Pseudozyma antarctica Lipase B Yielding a General Esterification Catalyst. Chem. Bio. Chem., 11, 789–795.
- Trodler, P., Eiben, S., Koschorreck, K., Müller, M., Pleiss, J., Maurer, S., Branneby, C., & Schmid, R. (2010). Rational design of Pseudozyma antarctica lipase B yielding a general esterification catalyst. ChemBioChem, 11, 789–795.
- Widmann, M., Trodler, P., & Pleiss, J. (2010). The isoelectric region of proteins: a systematic analysis. PLoS One, 5, e10546–e10546.
- Weber, E., Sirim, D., Schreiber, T., Bejoy, T., Pleiss, J., Hunger, M., Gläser, R., & Urlacher, V. (2010). Immobilization of P450 BM-3 monooxygenase on mesoporous molecular sieves with differentpore diameters. J Mol Catal B, 64, 29–37.
- Gatti-Lafranconi, P., Natalello, A., Rehm, S., Doglia, S., Pleiss, J., & Lotti, M. (2010). Evolution of stability in a cold-active enzyme elicits specificity relaxation and highlights substrate-related effects on temperature adaptation. J Mol Biol, 395, 155–166.
- Sirim, D., Widmann, M., Wagner, F., & Pleiss, J. (2010). Prediction and analysis of the modular structure of cytochrome P450 monooxygenases. BMC Struct Biol, 10, 34–34.
2009
- Knoll, M., Hamm, T., Wagner, F., Martinez, V., & Pleiss, J. (2009). The PHA Depolymerase Engineering Database: A systematic analysis tool for the diverse family of polyhydroxyalkanoate (PHA) depolymerases. BMC Bioinformatics, 10, 89.
- Seifert, A., & Pleiss, J. (2009). Identification of selectivity-determining residues in cytochrome P450 monooxygenases: a systematic analysis of the substrate recognition site 5. Proteins, 74, 1028–1035.
- Seifert, A., Vomund, S., Grohmann, K., Kriening, S., Urlacher, V., Laschat, S., & Pleiss, J. (2009). Rational design of a minimal and highly enrichedCYP102A1 mutant library with improved regio-, stereo- and chemoselectivity. ChemBioChem, 10, 853–861.
- Bös, F., & Pleiss, J. (2009). Multiple molecular dynamics simulations of TEMbeta-lactamase: Dynamics and water binding of the Omega-loop. Biophys J, 97, 2550–2558.
- Juhl, P., Trodler, P., Tyagi, S., & Pleiss, J. (2009). Modelling substrate specificity and enantioselectivity for lipases and esterases by substrate-imprinted docking. BMC Struct Biol, 9, 39.
- Thai, Q., Bös, F., & Pleiss, J. (2009). The Lactamase Engineering Database: a critical survey of TEM sequences in public databases. BMC Genomics, 10, 390.
- Branco, R., Graber, M., Denis, V., & Pleiss, J. (2009). Molecular mechanism of the hydration of Candida antarctica lipase B in gas phase: water adsorption isotherms and molecular dynamics simulations. ChemBioChem, 10, 2913–2919.
- Trodler, P., Schmid, R., & Pleiss, J. (2009). Modeling of solvent-dependent conformational transitions in Burkholderia cepacia lipase. BMC Struct Biol, 9, 38.
- Sirim, D., Wagner, F., Lisitsa, A., & Pleiss, J. (2009). The Cytochrome P450 Engineering Database: integration of biochemical properties. BMC Biochemistry, 10, 27.
- Chen, B., Huang, Y., Pleiss, J., & Lin, Z. (2009). Morphing activity between structurally similar enzymes: from heme-free bromoperoxidase to lipase. Biochemistry, 48, 11496–11504.
- Dietrich, M., Schmid, R., Pleiss, J., & Urlacher, V. (2009). Altering the regioselectivity of the subterminal fatty acid hydroxylase P450 BM-3 towards gamma- and delta-positions. J Biotechnol, 139, 115–117.
2008
- Trodler, P., & Pleiss, J. (2008). Modeling structure and flexibility of Candida antarctica lipase B in organic solvents. BMC Struct Biol, 8, 9.
- Widmann, M., Clairo, M., Dippon, J., & Pleiss, J. (2008). Analysis of the distribution of functionally relevant rare codons. BMC Genomics, 9, 207.
- Trodler, P., Nieveler, J., Rusnak, M., Schmid, R., & Pleiss, J. (2008). Rational design of a new one-step purification strategy for Candida antarctica lipase B by ion-exchange chromatography. J Chromatogr A, 1179, 161–167.
- Gocke, D., Walter, L., Gauchenova, E., Kolter, G., Knoll, M., Berthold, C., Schneider, G., Pleiss, J., Müller, M., & Pohl, M. (2008). Rational protein design of ThDP-dependent enzymes: engineering stereoselectivity. ChemBioChem, 9, 406–412.
- Bös, F., & Pleiss, J. (2008). Conserved water molecules stabilize the omega-loop in class A beta-lactamases. Antimicrob Agents Chemother, 52, 1072–1079.
- Branco, R., Seifert, A., Budde, M., Urlacher, V., Ramos, M., & Pleiss, J. (2008). Anchoring effects in a wide binding pocket: The molecular basis of regioselectivity in engineered cytochrome P450 monooxygenase from B. megaterium. Proteins, 73, 597–607.
- Messerschmidt, S., Kolbe, A., Müller, D., Knoll, M., Pleiss, J., & Kontermann, R. (2008). Novel single-chain Fv′ formats for the generation of immunoliposomes by site-directed coupling. Bioconjugate Chem., 19, 362–369.
- Dietrich, M., Eiben, S., Asta, C., Pleiss, J., & Urlacher, V. (2008). Cloning, expression and characterisation of CYP102A7, a self-sufficient P450 from Bacillus licheniformis. Appl Microbiol Biotechnol, 79, 931–940.
- Knoll, M., & Pleiss, J. (2008). The Medium-Chain Dehydrogenase/Reductase Engineering Database: A systematic analysis of a diverse protein family to understand sequence-structure-function relationship. Protein Sci, 17, 1689–1697.
- Bidmon, K., Grottel, S., Bös, F., Pleiss, J., & Ertl, T. (2008). Visual abstractions of solvent pathlines near protein cavities. Comput Graph Forum, 27, 935–942.
2007
- Pleiss, J. (2007). Human Cytochrome P450 Monooxygenases – a General Model of Substrate Specificity and Regioselectivity. In V. B. U. Rolf D. Schmid (Ed.), Modern Biooxidation:Enzymes, Reactions and Applications. Wiley-VCH.
- Klein, K., Tatzel, S., Raimundo, S., Saussele, T., Hustert, E., Pleiss, J., Eichelbaum, M., & Zanger, U. (2007). A natural variant of the heme-bindingsignature (R441C) resulting in complete loss of the function of CYP2D6. Drug Metab Dispos, 35, 1247–1250.
- Oelschlaeger, P., & Pleiss, J. (2007). Hydroxyl groups in the betabeta sandwich of metallo-beta-lactamases favor enzyme activity: Tyr218 and Ser262 pull down the lid. J Mol Biol, 366, 316–329.
- Fischer, M., Knoll, M., Sirim, D., Wagner, F., Funke, S., & Pleiss, J. (2007). The Cytochrome P450 Engineering Database: a navigation and prediction tool for the cytochrome P450 protein family. Bioinformatics, 23, 2015–2017.
2006
- Fischer, M., Thai, Q., Grieb, M., & Pleiss, J. (2006). DWARF - a data warehouse system for analyzing protein families. BMC Bioinformatics, 7, 495–495.
- Knoll, M., Müller, M., Pleiss, J., & Pohl, M. (2006). Factors mediating activity, selectivity, and substrate specificity for the thiamin diphosphate-dependent enzymes benzaldehyde lyase and benzoylformate decarboxylase. Chembiochem, 7, 1928–1934.
- Tyagi, S., & Pleiss, J. (2006). Biochemical profiling in silico - Predicting substrate specificities of large enzyme families. J Biotechnol, 124, 108–116.
- Pleiss, J. (2006). The promise of synthetic biology. Appl Microbiol Biotechnol, 73, 735–739.
- Seifert, A., Tatzel, S., Schmid, R., & Pleiss, J. (2006). Multiple molecular dynamics simulations of human P450 monooxygenase CYP2C9: the molecular basis of substrate binding and regioselectivity toward warfarin. Proteins, 64, 147–155.
2005
- Riepe, F., Tatzel, S., Sippell, W., Pleiss, J., & Krone, N. (2005). Congenital adrenal hyperplasia: the molecular basis of 21-hydroxylase deficiency in H-2(aw18) mice. Endocrinology, 146, 2563–2574.
- Koschorreck, M., Fischer, M., Barth, S., & Pleiss, J. (2005). How to find soluble proteins: a comprehensive analysis of alpha/beta hydrolases for recombinant expression in E. coli. BMC Genomics, 6, 1–10.
- Oelschlaeger, P., Mayo, S., & Pleiss, J. (2005). Impact of remote mutations on metallo-beta-lactamase substrate specificity: implications for the evolution of antibiotic resistance. Protein Sci, 14, 765–774.
- Bornscheuer, U., Henke, E., & Pleiss, J. (2005). Enzymatic methods. In A. Christoffers, J.; Baro (Ed.), Quaternary Stereocenters (pp. 315–327). Wiley-VCH.
2004
- Tejo, B., Salleh, A., & Pleiss, J. (2004). Structure and dynamics of Candida rugosa lipase: the role of organic solvent. J Mol Model, 10, 358–366.
- Barth, S., Fischer, M., Schmid, R., & Pleiss, J. (2004). The database of epoxide hydrolases andhaloalkane dehalogenases: one structure, manyfunctions. Bioinformatics, 20, 2845–2847.
- Strohmeier, M., Hrmova, M., Fischer, M., Harvey, A., Fincher, G., & Pleiss, J. (2004). Molecular modeling of family GH16 glycoside hydrolases: potential roles for xyloglucan transglucosylases/hydrolases in cell wall modification in the poaceae. Protein Sci, 13, 3200–3213.
- Schmid, R., Pleiss, J., & Urlacher, V. (2004). Biokatalyse: Selektivoxidation von C-H-Bindungen mit O2. Nachr Chem, 52, 767–772.
- Currle-Linde, N., Boes, F., Lindner, P., Pleiss, J., & Resch, M. (2004). A Management System for Complex Parameter Studies and Experiments in Grid Computing. In T. Gonzales (Ed.), Proceedings of the 16th IASTED International Conference on PDCS - International Conference on Parallel and Distributed Computing and Systems (pp. 34–39). Acta press.
- Richter, T., Muerdter, T., Heinkele, G., Pleiss, J., Tatzel, S., Schwab, M., Eichelbaum, U., & Zanger, M. (2004). Potent mechanism-based inhibition of human CYP2B6 by clopidogrel and ticlopidine. J Pharmacol Exp Ther, 303, 189–197.
- Barth, S., Fischer, M., Schmid, R., & Pleiss, J. (2004). Sequence and structure of epoxide hydrolases: a systematic analysis. Proteins, 55, 846–855.
2003
- Oelschlaeger, P., Schmid, R., & Pleiss, J. (2003). Insight into the mechanism of the IMP-1 metallo-beta-lactamase by molecular dynamics simulations. Protein Eng, 16, 341–350.
- Henke, E., Bornscheuer, U., Schmid, R., & Pleiss, J. (2003). A molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases. ChemBioChem, 4, 485–493.
- Oelschlaeger, P., Schmid, R., & Pleiss, J. (2003). Modeling domino effects in enzymes: molecular basis of the substrate specificity of the bacterial metallo-beta-lactamases IMP-1 and IMP-6. Biochemistry, 42, 8945–8956.
- Fischer, M., & Pleiss, J. (2003). The Lipase Engineering Database: a navigation and analysis tool for protein families. Nucleic Acids Res, 31, 319–321.
- Lich, N., Barth, F., Pleiss, J., & Hai, T. (2003). Homology modelling of alpha-amylase from Saccharomycopsis fibuligera with maltohexaose substrate. Vietnam Journal of Biotechnology, 1, 149–159.
2002
- Bathelt, C., Schmid, R., & Pleiss, J. (2002). Regioselectivity of CYP2B6: homology modeling, molecular dynamics simulation, docking. J Mol Model, 8, 327–335.
- Kusharyoto, W., Pleiss, J., Bachmann, T., & Schmid, R. (2002). Mapping of a hapten-binding site: molecular modeling and site-directed mutagenesis study of an anti-atrazine antibody. Protein Eng, 15, 233–241.
- Gentner, C., Schmid, R., & Pleiss, J. (2002). Primary alcohols in a ring structure: quantifying enantioselectivity of Pseudomonas cepacia lipase by an in silico assay. Colloids Surf B Biointerfaces, 26, 57–66.
- Henke, E., Pleiss, J., & Bornscheuer, U. (2002). Activity of lipases and esterases towards tertiary alcohols: insights into structure-function relationships. Angew Chem Int Ed, 41, 3211–3213.
- Schmitt, J., Brocca, S., Schmid, R., & Pleiss, J. (2002). Blocking the tunnel: engineering of Candida rugosa lipase mutants with short chain length specificity. Protein Eng, 15, 595–601.
2001
- Kahlow, U., Schmid, R., & Pleiss, J. (2001). A model of the pressure dependence of the enantioselectivity of Candida rugosa lipase towards (±)-menthol. Protein Sci, 10, 1942–1952.
- Schulz, T., Schmid, R., & Pleiss, J. (2001). Structural basis of stereoselectivity in Candida rugosa lipase-catalyzed hydrolysis of secondary alcohols. J Mol Model, 7, 265–270.
- Schwaneberg, U., Fischer, M., Schmitt, J., Pleiss, J., Lutz-Wahl, S., & Schmid, R. (2001). Rational evolution of a medium chain-specific cytochrome P-450 BM-3 variant. Biochim Biophys Acta, 1545, 114–121.
- Bachmann, T., Pleiss, J., Villatte, F., & Schmid, R. (2001). Bioresponse-Linked Analysis Based on Acetylcholinesterase Inhibition. In H. B (Ed.), Bioresponse-Linked Instrumental Analysis. B.G. Teubner.
2000
- Bornscheuer, U., Pleiss, J., Schmidt-Dannert, C., & Schmid, R. (2000). Lipases from Rhizopus species: genetics, structure and applications. In L. Alberghina (Ed.), Protein engineering in industrial biotechnology (pp. 115–134). CRC Press.
- Otto, R., Scheib, H., Bornscheuer, U., Pleiss, J., Syldatk, C., & Schmid, R. (2000). Substrate specificity of lipase B from Candida antarctica in the synthesis of arylaliphatic glycolipids. J Mol Catal B Enzym, 8, 201–211.
- Pleiss, J., Fischer, M., Peiker, M., Thiele, C., & Schmid, R. (2000). Lipase Engineering Database: understanding and exploiting sequence-structure-function relationships. J Mol Catal B: Enzym, 10, 491–508.
- Kovac, A., Scheib, H., Pleiss, J., Schmid, R., & Paltauf, F. (2000). Molecular basis of lipase stereoselectivity. Eur J Lipid Sci Tech, 102, 61–77.
- Pleiss, J., Fischer, M., Scheib, H., Schulz, T., & Schmid, R. (2000). Modelling structure-function relationship of lipase binding sites-a case study of specificity and selectivity. In G. Kokotos (Ed.), Lipases and LipidsStructure, function and biotechnological applications (pp. 21–39). Crete University Press.
- Pleiss, J. (2000). In silico-Assays: Computergestuetzte Modellierung der Stereoselektivität von Lipasen. Transkript, 9, 38–40.
- Pleiss, J., Scheib, H., & Schmid, R. (2000). The his gap motif in microbial lipases: a determinant of stereoselectivity toward triacylglycerols and analogs. Biochimie, 82, 1043–1052.
- Hwang, B., Scheib, H., Pleiss, J., Kim, B., & Schmid, R. (2000). Computer-aided molecular modeling of the enantioselectivity of Pseudomonas cepacia lipase toward g- and d-lactones. J Mol Catal B Enzym, 10, 223–231.
- Schulz, T., Pleiss, J., & Schmid, R. (2000). Stereoselectivity of Pseudomonas cepacia lipase towards secondary alcohols: a quantitative model. Protein Sci, 9, 1053–1062.
1999
- Scheib, H., Pleiss, J., Kovac, A., Paltauf, F., & Schmid, R. (1999). Stereoselectivity of Mucorales lipases toward triradylglycerols--a simple solution to a complex problem. Protein Sci, 8, 215–221.
- Pleiss, J., & Schmid, R. (1999). Bioinformatics and the internet. Chemistry International, 21, 33–36.
- Pleiss, J., Mionetto, N., & Schmid, R. (1999). Probing the acyl binding site of acetylcholinesterase by protein engineering. J Mol Catal B: Enzym, 6, 287–296.
1998
- Schmidt-Dannert, C., Pleiss, J., & Schmid, R. (1998). A toolbox of recombinant lipases for industrial applications. Ann N Y Acad Sci, 864, 14–22.
- Scheib, H., Pleiss, J., Stadler, P., Kovac, A., Potthoff, A., Haalck, L., Spener, F., Paltauf, F., & Schmid, R. (1998). Rational design of Rhizopus oryzae lipase with modified stereoselectivity toward triradylglycerols. Protein Eng, 11, 675–682.
- Hülser, D., Eckert, R., Irmer, U., Krisciukaitis, A., Mindermann, A., Pleiss, J., Rehkopf, B., Sharovskaya, J., & Traub, O. (1998). Intercellular communication via gap junction channels. Bioelectrochem Bioenerg, 45, 55–65.
- Pleiss, J., Fischer, M., & Schmid, R. (1998). Anatomy of lipase binding sites: the scissile fatty acid binding site. Chem Phys Lipids, 93, 67–80.
- Mindermann, A., Pleiss, J., & Hülser, D. (1998). Molecular Modeling of Gap Junction Pores. In R. Werner (Ed.), Gap Junctions. Proceedings of the 8th International Gap Junction Conference, Key Largo, Florida (pp. 67–71). IOS Press.
- Drees, R., Pleiss, J., Schmid, R., & Roller, D. (1998). Integrating molecular modeling tools and virtual reality engines: an architecture for a highly immersive molecular modeling (HIMM) environment. Proceedings of CGI, 391–392.
- Otto, R., Bornscheuer, U., Scheib, H., Pleiss, J., Syldatk, C., & Schmid, R. (1998). Lipase-catalyzed esterification of unusual substrates: synthesis of glucuronic acid and ascorbic acid. Biotechnol Lett, 20, 1091–1094.
1997
- Pleiss, J., Mionetto, N., & Schmid, R. (1997). Protein engineering of rat brain acetylcholinesterase: a point mutation enhances sensitivityto pesticides. Protein Eng, 10, 66–66.
- Holzwarth, H.-C., Pleiss, J., & Schmid, R. (1997). Computer-aided modelling of stereoselective triglyceride hydrolysis catalyzed by Rhizopus oryzae lipase. J Mol Catal B Enzym, 3, 73–82.
- Weber, H., Zuegg, J., Faber, J., & Pleiss, J. (1997). Molecular reasons for lipase-sensitivity against acetaldehyde. J Mol Catal B: Enzym, 3, 131–138.
- Haalck, L., Paltauf, F., Pleiss, J., Schmid, R., Spener, F., & Stadler, P. (1997). Stereoselectivity of lipase from Rhizopus oryzae toward triacylglycerols and anlogs: computer aided modelling and experimental validation. Methods Enzymol, 284, 353–376.
1996
- Drees, R., Pleiss, J., & Schmid, R. (1996). Highly immersive molecular modeling (HIMM): an architecture for the integration of molecular modelling and virtual reality. In R. Hofestädt, M. Löffler, & D. Schomburg (Eds.), Computer science and biology : proceedings of the German Conference on Bioinformatics (GCB 96) (pp. 190–192). Universität Leipzig.
1994
- Pleiss, J. (1994). Molecular basis of specificity and stereoselectivity of microbial lipases toward triacylglycerols. In U. T. Bornscheuer (Ed.), Enzymes in Lipid Modification (pp. 85–99). Wiley-VCH.
- Pleiss, J. (1994). Quantitative modelling of lipase enantioselectivity. In A. Svendsen (Ed.), Enzyme functionality: Design, engineering, and screening. Marcel Dekker.
1992
- Pleiss, J., & Jähnig, F. (1992). Conformational transition of an alpha-helix studied by molecular dynamics. Eur Biophys J, 21, 63–70.
1991
- Pleiss, J., & Jähnig, F. (1991). Collective vibrations of an alpha-helix. A molecular dynamics study. Biophys J, 59, 795–804.
1989
- Roditi, I., Schwarz, H., Pearson, T., Beecroft, R., Liu, M., Richardson, J., Bühring, H., Pleiss, J., Bülow, R., & et, al. (1989). Procyclin gene expression and loss of the variant surface glycoprotein during differentiation of Trypanosoma brucei. J Cell Biol, 108, 737–746.