Kontakt
Allmandring 31
70569 Stuttgart
Germany
Raum: 0.307
2024
- Pleiss, J.: Modeling Enzyme Kinetics: Current Challenges and Future Perspectives for Biocatalysis. Biochemistry. 63, 2533–2541 (2024). https://doi.org/10.1021/acs.biochem.4c00501.
- Windels, A., Franceus, J., Pleiss, J., Desmet, T.: CANDy: Automated analysis of domain architectures in carbohydrate-active enzymes. PLOS ONE. 19, 1–16 (2024). https://doi.org/10.1371/journal.pone.0306410.
- Carvalho, H.F., Mestrom, L., Hanefeld, U., Pleiss, J.: Beyond the Chemical Step: The Role of Substrate Access in Acyltransferase from Mycobacterium smegmatis. ACS Catal. 14, 10077--10088 (2024). https://doi.org/10.1021/acscatal.4c00812.
- Pleiss, J.: FAIR Data and Software: Improving Efficiency and Quality of Biocatalytic Science. ACS Catal. 14, 2709--2718 (2024). https://doi.org/10.1021/acscatal.3c06337.
- Behr, A.S., Surkamp, J., Abbaspour, E., Häußler, M., Lütz, S., Pleiss, J., Kockmann, N., Rosenthal, K.: Fluent Integration of Laboratory Data into Biocatalytic Process Simulation Using EnzymeML, DWSIM, and Ontologies. Processes. 12, 597 (2024). https://doi.org/10.3390/pr12030597.
- Schnee, P., Pleiss, J., Jeltsch, A.: Approaching the catalytic mechanism of protein lysine methyltransferases by biochemical and simulation techniques. Critical Reviews in Biochemistry and Molecular Biology. 59, 20–68 (2024). https://doi.org/10.1080/10409238.2024.2318547.
- Neubauer, F., Bredl, P., Xu, M., Patel, K., Pleiss, J., Uekermann, B.: MetaConfigurator: A User-Friendly Tool for Editing Structured Data Files. Datenbank-Spektrum. 24, 161–169 (2024). https://doi.org/10.1007/s13222-024-00472-7.
- Fademrecht, S., Pleiss, J.: Enzyme Modeling: From the Sequence to the Substrate Complex. In: Introduction to Enzyme Technology. pp. 39--59. Springer International Publishing, Cham (2024). https://doi.org/10.1007/978-3-031-42999-6_3.
- Weirich, S., Kusevic, D., Schnee, P., Reiter, J., Pleiss, J., Jeltsch, A.: Discovery of NSD2 non-histone substrates and design of a super-substrate. Communications Biology. 7, 707-- (2024). https://doi.org/10.1038/s42003-024-06395-z.
- Flemisch, B., Hermann, S., Herschel, M., Pflüger, D., Pleiss, J., Range, J., Roy, S., Takamoto, M., Uekermann, B.: Research Data Management in Simulation Science: Infrastructure, Tools, and Applications. Datenbank-Spektrum. 24, 97–105 (2024). https://doi.org/10.1007/s13222-024-00475-4.
2023
- Giess, T., Itzigehl, S., Range, J., Schömig, R., Bruckner, J.R., Pleiss, J.: FAIR and scalable management of small-angle X-ray scattering data. Journal of Applied Crystallography. 56, 565–575 (2023). https://doi.org/10.1107/S1600576723001577.
- Lauterbach, S., Dienhart, H., Range, J., Malzacher, S., Spöring, J.-D., Rother, D., Pinto, M.F., Martins, P., Lagerman, C.E., Bommarius, A.S., Høst, A.V., Woodley, J.M., Ngubane, S., Kudanga, T., Bergmann, F.T., Rohwer, J.M., Iglezakis, D., Weidemann, A., Wittig, U., Kettner, C., Swainston, N., Schnell, S., Pleiss, J.: EnzymeML: seamless data flow and modeling of enzymatic data. Nature Methods. 20, 400--402 (2023). https://doi.org/10.1038/s41592-022-01763-1.
- Khella, M.S., Schnee, P., Weirich, S., Bui, T., Bröhm, A., Bashtrykov, P., Pleiss, J., Jeltsch, A.: The T1150A cancer mutant of the protein lysine dimethyltransferase NSD2 can introduce H3K36 trimethylation. Journal of Biological Chemistry. 299, 104796-- (2023). https://doi.org/10.1016/j.jbc.2023.104796.
2022
- Range, J., Halupczok, C., Lohmann, J., Swainston, N., Kettner, C., Bergmann, F.T., Weidemann, A., Wittig, U., Schnell, S., Pleiss, J.: EnzymeML—a data exchange format for biocatalysis and enzymology. The FEBS Journal. 289, 5864--5874 (2022). https://doi.org/10.1111/febs.16318.
- Mack, A., Emperle, M., Schnee, P., Adam, S., Pleiss, J., Bashtrykov, P., Jeltsch, A.: Preferential Self-interaction of DNA Methyltransferase DNMT3A Subunits Containing the R882H Cancer Mutation Leads to Dominant Changes of Flanking Sequence Preferences. JOURNAL OF MOLECULAR BIOLOGY. 434, (2022). https://doi.org/10.1016/j.jmb.2022.167482.
- Gültig, M., Range, J.P., Schmitz, B., Pleiss, J.: Integration of Simulated and Experimentally Determined Thermophysical Properties of Aqueous Mixtures by ThermoML. Journal of Chemical & Engineering Data. 67, 3340–3350 (2022). https://doi.org/10.1021/acs.jced.2c00391.
- 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.: The Bacteroidetes Aequorivita sp. and Kaistella jeonii produce promiscuous esterases with PET-hydrolyzing activity. Front Microbiol. 12, 803896 (2022). https://doi.org/10.3389/fmicb.2021.803896.
- Royek, S., Bayer, M., Pfannstiel, J., Pleiss, J., Ingram, G., Stintzi, A., Schaller, A.: Processing of a plant peptide hormone precursor facilitated by post-translational tyrosine sulfation. Proc Natl Acad Sci USA. 119, e2201195119 (2022).
- Buchholz, P.C.F., Feuerriegel, G., Zhang, H., Perez-Garcia, P., Nover, L.-L., Chow, J., Streit, W.R., Pleiss, J.: Plastics degradation by hydrolytic enzymes: The plastics-active enzymes database—PAZy. Proteins: Structure, Function, and Bioinformatics. 90, 1443–1456 (2022). https://doi.org/10.1002/prot.26325.
- Chow, J., Pleiss, J., Streit, W.R.: PAZy — mikrobielle Enzyme für den Abbau künstlicher Polymere. BIOspektrum. 28, 451--452 (2022). https://doi.org/10.1007/s12268-022-1752-3.
- Schnee, P., Choudalakis, M., Weirich, S., Khella, M.S., Carvalho, H., Pleiss, J., Jeltsch, A.: Mechanistic basis of the increased methylation activity of the SETD2 protein lysine methyltransferase towards a designed super-substrate peptide. Communications Chemistry. 5, 139-- (2022). https://doi.org/10.1038/s42004-022-00753-w.
2021
- Orlando, M., Buchholz, P., Lotti, M., Pleiss, J.: The GH19 Engineering Database: sequence diversity, substrate scope, and evolution in glycoside hydrolase family 19. PLoS One. 16, e0256817 (2021). https://doi.org/10.1371/journal.pone.0256817.
- Buchholz, P., van, L.B., Eenink, B., Bornberg-Bauer, E., Pleiss, J.: Ancestral sequences of a large promiscuous enzyme family correspond to bridges in sequence space in a network representation. J R Soc Interface. 18, 20210389 (2021). https://doi.org/10.1098/rsif.2021.0389.
- Carvalho, H., Ferrario, V., Pleiss, J.: 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 (2021). https://doi.org/10.1021/acs.jctc.1c00559.
- Schatz, K., Franco-Moreno, J., Schäfer, M., Rose, A., Ferrario, V., Pleiss, J., Vazquez, P., Ertl, T., Krone, M.: Visual analysis of large-scale protein-ligand interaction data. Comput Graph Forum. 40, 394–408 (2021). https://doi.org/10.1111/cgf.14386.
- Schatz, K., Friess, F., Schäfer, M., Buchholz, P., Pleiss, J., Ertl, T., Krone, M.: Analyzing the similarity of protein domains by clustering molecular surface maps. Comput Graph. 99, 114–127 (2021). https://doi.org/10.1016/j.cag.2021.06.007.
- Pleiss, J.: Standardized data, scalable documentation, sustainable storage – EnzymeML as a basis for FAIR data management in biocatalysis. ChemCatChem. 13, 3909–3913 (2021). https://doi.org/10.1002/cctc.202100822.
- Stockinger, P., Borlinghaus, N., Sharma, M., Aberle, B., Grogan, G., Pleiss, J., Nestl, B.: Inverting the stereoselectivity of an NADH-dependent imine-reductase variant. ChemCatChem. 13, 5210–5215 (2021). https://doi.org/10.1002/cctc.202101057.
- Faheem, M., Zhang, C., Morris, M., Pleiss, J., Oelschlaeger, P.: The role of synonymous mutations in the evolution of TEM β-lactamase genes. Antimicrob Agents Chemother. 65, e00018-21 (2021). https://doi.org/10.1128/AAC.00018-21.
- Lohoff, C., Buchholz, P., Le, R.-H.M., Pleiss, J.: The Expansin Engineering Database: a navigation and classification tool for expansins and homologues. Proteins. 89, 149–162 (2021). https://doi.org/10.1002/prot.26001.
2020
- Stockinger, P., Schelle, L., Schober, B., Buchholz, P., Pleiss, J., Nestl, B.: Engineering of thermostable β-hydroxyacid dehydrogenase for asymmetric reduction of imines. ChemBioChem. 21, 3511–3514 (2020).
- Mangiagalli, M., Carvalho, H., Natalello, A., Ferrario, V., Pennati, M., Barbiroli, A., Lotti, M., Pleiss, J., Brocca, S.: Diverse effects of aqueous polar co-solvents on Candida antarctica lipase B. Int J Biol Macromol. 150, 930–940 (2020). https://doi.org/10.1016/j.ijbiomac.2020.02.145.
- Rifai, E., Ferrario, V., Pleiss, J., Geerke, D.: A combined linear interaction energy and alchemical solvation free energy approach for protein-binding anity computation. J Chem Theory Comput. 16, 1300–1310 (2020).
- Bauer, T., Buchholz, P., Pleiss, J.: The modular structure of α/β-hydrolases. FEBS J. 287, 1035–1053 (2020). 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.: Modeling of biocatalytic reactions: A workflow for model calibration, selection and validation using Bayesian statistics. AIChE J. 66, e16866 (2020). https://doi.org/10.1002/aic.16866.
- Xu, X., Range, J., Gygli, G., Pleiss, J.: Analysis of thermophysical properties of deep eutectic solvents by data integration. J Chem Eng Data. 65, 1172–1179 (2020). https://doi.org/10.1021/acs.jced.9b00555.
- Gygli, G., Xu, X., Pleiss, J.: Meta-analysis of viscosity of aqueous deep eutectic solvents and their components. Sci Rep. 10, 21395–21395 (2020). https://doi.org/10.1038/s41598-020-78101-y.
- Gygli, G., Pleiss, J.: Simulation Foundry: automated and F.A.I.R. molecular modelling. J Chem Inf Model. 60, 1922–1927 (2020). https://doi.org/10.1021/acs.jcim.0c00018.
- Gräff, M., Buchholz, P., Le Roes-Hill, M., Pleiss, J.: Multicopper oxidases: modular structure, sequence space and evolutionary relationships. Proteins. (2020).
- Stockinger, P., Roth, S., Müller, M., Pleiss, J.: Systematic evaluation of imine-reducing enzymes: Common principles in imine reductases, β-hydroxyacid dehydrogenases, and short-chain dehydrogenases/reductases. ChemBioChem. 21, 2689–2695 (2020). https://doi.org/10.1002/cbic.202000213.
- Malzacher, S., Range, J., Halupczok, C., Pleiss, J., Rother, D.: BioCatHub, a graphical user interface for standardized data acquisition in biocatalysis. Chem Ing Tech. 92, 1251–1251 (2020). https://doi.org/10.1002/cite.202055297.
- Roth, S., Stockinger, P., Steff, J., Steimle, S., Sautner, V., Tittmann, K., Pleiss, J., Müller, M.: Crossing the border: From keto- to imine reduction in short-chain dehydrogenases/reductases. ChemBioChem. 21, 2615–2619 (2020).
2019
- Buchholz, P., Ohs, R., Spieß, A., Pleiss, J.: Progress curve analysis within BioCatNet: comparing kinetic models for enzyme-catalyzed self-ligation. Biotechnol J. 14, e1800183 (2019).
- Gräff, M., Buchholz, P., Stockinger, P., Bommarius, B., Bommarius, A., Pleiss, J.: The Short-chain Dehydrogenase/Reductase Engineering Database (SDRED): A classification and analysis system for a highly diverse enzyme family. Proteins. 87, 443–451 (2019).
- Gobeil, S., Ebert, M., Park, J., Gagné, D., Doucet, N., Berghuis, A., Pleiss, J., Pelletier, J.: The structural dynamics of engineered β-lactamases vary broadly on three timescales yet sustain native function. Sci Rep. 9, 6656–6656 (2019).
- Fries, A., Mazzaferro, L., Grüning, B., Bisel, P., Stibal, K., Buchholz, P., Pleiss, J., Sprenger, G., Müller, M.: Alteration of the route to menaquinone towards isochorismate - derived metabolites. ChemBioChem. 20, 1672–1677 (2019).
- Schatz, K., Krone, M., Pleiss, J., Ertl, T.: Interactive visualization of biomolecules’ dynamic and complex properties. Eur Phys J Special Topics. 227, 1725–1739 (2019).
- Baz, J., Held, C., Pleiss, J., Hansen, N.: Thermophysical properties of glyceline-water mixtures investigated by molecular modelling. Phys Chem Chem Phys. 21, 6467–6476 (2019). https://doi.org/10.1039/C9CP00036D.
- Ferrario, V., Pleiss, J.: Molecular simulations of enzymes under non-natural conditions. Eur Phys J Special Topics. 227, 1631–1638 (2019).
- Buchholz, P., Ferrario, V., Pohl, M., Gardossi, L., Pleiss, J.: Navigating within thiamine diphosphate-dependent decarboxylases: Sequences, structures, functional positions, and binding sites. Proteins. 87, 774–785 (2019).
- Ferrario, V., Fischer, M., Zhu, Y., Pleiss, J.: Modelling of substrate access and substrate binding to cephalosporin acylases. Sci Rep. 9, 12402 (2019). https://doi.org/10.1038/s41598-019-48849-z.
- Demming, R., Hammer, S., Nestl, B., Gergel, S., Fademrecht, S., Pleiss, J., Hauer, B.: Asymmetric Enzymatic Hydration of Unactivated, Aliphatic Alkenes. Angew Chem Int Ed Engl. 58, 173–177 (2019).
- Grüninger, M., Buchholz, P., Mordhorst, S., Strack, P., Müller, M., Hubrich, F., Pleiss, J., Andexer, J.: Chorismatases – the family is growing. Org Biomol Chem. 17, 2092–2098 (2019).
- Roddan, R., Gygli, G., Sula, A., Mendez-Sanchez, D., Pleiss, J., Ward, J., Keep, N., Hailes, H.: The acceptance and kinetic resolution of alpha-methyl substituted aldehydes by norcoclaurine synthases. ACS Catal. 9, 9640–9649 (2019). https://pubs.acs.org/doi/abs/10.1021/acscatal.9b02699.
2018
- Lotti, M., Pleiss, J., Valero, F., Ferrer, P.: Enzymatic production of biodiesel: strategies to overcome methanol inactivation. Biotechnol J. 13, e1700155 (2018). https://doi.org/10.1002/biot.201700155.
- Lenz, M., Fademrecht, S., Sharma, M., Pleiss, J., Grogan, G., Nestl, B.: New imine-reducing enzymes from beta-hydroxyacid dehydrogenases by single amino acid substitutions. Protein Engineering, Design and Selection. 31, 109–120 (2018).
- Ferrario, V., Pleiss, J.: Simulation of protein diffusion: a sensitive probe of protein-solvent interactions. J Biomol Struct Dyn. 37, 1534–1544 (2018).
- Ferrario, V., Hansen, N., Pleiss, J.: Interpretation of cytochrome P450 monooxygenase kinetics by modeling of thermodynamic activity. J Inorg Biochem. 183, 172–178 (2018). https://doi.org/10.1016/j.jinorgbio.2018.02.016.
- Baierl, A., Theorell, A., Mackfeld, U., Marquardt, P., Hoffmann, F., Moers, S., Nöh, K., Buchholz, P., Pleiss, J., Pohl, M.: Towards a mechanistic understanding of factors controlling the stereoselectivity of transketolase. ChemCatChem. 10, 2601–2611 (2018).
- Pleiss, J.: Thermodynamic activity-based progress curve analysis in enzyme kinetics. Trends Biotechnol. 36, 234–238 (2018).
- Buß, O., Buchholz, P., Gräff, M., Klausmann, P., Rudat, J., Pleiss, J.: The omega-Transaminase Engineering Database (oTAED): a navigation tool in protein sequence and structure space. Proteins. 86, 566–580 (2018).
- Martínez-Martínez, M., Coscolín, C., Santiago, G., Chow, J., Stogios, P., ..., Buchholz, P., Pleiss, J., ..., Ferrer, M.: Determinants and prediction of esterase substrate promiscuity patterns. ACS Chem Biol. 13, 225–234 (2018).
- Buchholz, P., Zeil, C., Pleiss, J.: The scale-free nature of protein sequence space. PLoS One. 13, e0200815 (2018).
2017
- Zhang, Q., Catti, L., Pleiss, J., Tiefenbacher, K.: Terpene cyclizations inside a supramolecular catalyst: Leaving-group-controlled product selectivity and mechanistic studies. J Am Chem Soc. 139, 11482–11492 (2017).
- Benson, S., Pleiss, J.: Self-assembly nanostructures of triglyceride-water interfaces determine functional conformations of Candida antarctica lipase B. Langmuir. 33, 3151–3159 (2017).
- Krone, M., Friess, F., Scharnowski, K., Reina, G., Fademrecht, S., Kulschewski, T., Pleiss, J., Ertl, T.: Molecular Surface Maps. IEEE Trans Vis Comput Graph. 23, 701–710 (2017).
- Buchholz, P., Fademrecht, S., Pleiss, J.: Percolation in protein sequence space. PLoS One. 12, e0189646 (2017).
- Schmid, J., Steiner, L., Fademrecht, S., Pleiss, J., Otte, K., Hauer, B.: Biocatalytic study of novel oleate hydratases. J Mol Catal B: Enzym. 133, S243–S249 (2017).
- Pleiss, J.: Thermodynamic activity–based interpretation of enzyme kinetics. Trends Biotechnol. 35, 379–382 (2017).
2016
- Zeil, C., Widmann, M., Fademrecht, S., Vogel, C., Pleiss, J.: Microdiversity of TEM β-lactamases: a network analysis of sequence-function relationships and exploration of sequence space. Antimicrob Agents Chemother. 60, 2709–2717 (2016).
- Bock, S., Buchholz, P., Vogel, C., Holzapfel, A., Pleiss, J., Wiechert, W., Pohl, M., Rother, D.: Exploring the Sequence-Function Space of ThDP-Dependent Enzymes. Chemie Ingenieur Technik. 88, 1246 (2016).
- Benson, S., Pleiss, J.: Computational modeling of a biocatalyst at a hydrophobic substrate interface. Springer International Publishing (2016).
- Kulschewski, T., Pleiss, J.: Binding of solvent molecules to a protein surface in binary mixtures follows a competitive Langmuir model. Langmuir. 32, 8960–8968 (2016).
- Notonier, S., Gricman, L., Pleiss, J., Hauer, B.: 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 (2016).
- Eichler, A., Gricman, L., Herter, S., Kelly, P., Turner, N., Pleiss, J., Flitsch, S.: Enantioselective benzylic hydroxylation catalysed by P450 monooxygenases: characterisation of a P450cam mutant library and molecular modelling. ChemBioChem. 17, 426–432 (2016).
- Jozwik, I., Kiss, F., Gricman, L., Abdulmughni, A., Brill, E., Zapp, J., Pleiss, J., Bernhardt, R., Thunnissen, A.: Structural basis of steroid binding and oxidation by the cytochrome P450 CYP109E1 from Bacillus megaterium. FEBS J. 283, 4128–4148 (2016).
- Widmann, M., Pleiss, J.: Sequence, structure, function: what we learn from analyzing protein families. pan Standord Publishing, Singapore (2016).
- Pleiss, J., Zeil, C.: Reply to The Curious Case of TEM-116. Antimicrob Agents Chemother. 60, 7001–7001 (2016).
- Schäfer, I., Lasko, G., Do, T., Pleiss, J., Weber, U., Schmauder, S.: Peptide–zinc oxide interaction: Finite element simulation using cohesive zone models based on molecular dynamics simulation. De Gruyter (2016).
- Gricman, L., Weissenborn, M., Hoffmann, S., Borlinghaus, N., Hauer, B., Pleiss, J.: Redox Partner Interaction Sites in Cytochrome P450 Monooxygenases: In Silico Analysis and Experimental Validation. ChemistrySelect. 6, 1243–1251 (2016).
- Buchholz, P., Vogel, C., Reusch, W., Pohl, M., Rother, D., Spieß, A., Pleiss, J.: BioCatNet: a database system for the integration of enzyme sequences and biocatalytic experiments. ChemBioChem. 17, 2093–2098 (2016).
- Hoffmann, S., Weissenborn, M., Gricman, L., Notonier, S., Pleiss, J., Hauer, B.: The Impact of Linker Length on P450 Fusion Constructs: Activity, Stability and Coupling. ChemCatChem. 8, 1591–1597 (2016).
- Fademrecht, S., Scheller, P., Nestl, B., Hauer, B., Pleiss, J.: Identification of imine reductase-specific sequence motifs. Proteins. 84, 600–610 (2016).
2015
- Gricman, L., Vogel, C., Pleiss, J.: Identification of universal selectivity-determining positions in cytochrome P450 monooxygenases by systematic sequence-based literature mining. Proteins. 83, 1593-1603. (2015).
- Prins, A., Kleinsmidt, L., Khan, N., Kirby, B., Kudanga, T., Vollmer, J., Pleiss, J., Burton, S., Le, R.-H.M.: 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 (2015).
- Taudt, A., Arnold, A., Pleiss, J.: Simulation of protein association - Kinetic pathways towards crystal contacts. Phys Rev E. 91, 033311 (2015).
- Lotti, M., Pleiss, J., Valero, F., Ferrer, P.: Effects of methanol on lipases: molecular, kinetic and process issues in the production of biodiesel. Biotechnol J. 10, 22–30 (2015).
- Sasso, F., Kulschewski, T., Secundo, F., Lotti, M., Pleiss, J.: 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 (2015).
2014
- Widmann, M., Pleiss, J.: Protein variants form a system of networks: microdiversity of IMP metallo-beta-lactamases. PLoS ONE. 9, e101813 (2014).
- Westphal, R., Vogel, C., Schmitz, C., Pleiss, J., Müller, M., Pohl, M., Rother, D.: A Tailor-Made Chimeric Thiamine Diphosphate Dependent Enzyme for the Direct Asymmetric Synthesis of (S)-Benzoins. Angew. Chem. Int. Ed. 53, 9376–9379 (2014).
- Scharnowski, K., Krone, M., Reina, G., Kulschewski, T., Pleiss, J., Ertl, T.: Comparative Visualization of Molecular Surfaces Using Deformable Models. Comput Graph Forum. 3, 191–200 (2014).
- Benson, S., Pleiss, J.: Molecular dynamics simulations of self-emulsifying drug delivery systems (SEDDS): influence of excipients on droplet nanostructure and drug localization. Langmuir. 30, 8471–8480 (2014).
- Scheller, P., Fademrecht, S., Hofelzer, S., Pleiss, J., Leipold, F., Turner, N., Nestl, B., Hauer, B.: Enzyme Toolbox: Novel Enantiocomplementary Imine Reductases. ChemBioChem. 15, 2201–2204 (2014).
- Benson, S., Pleiss, J.: Solvent Flux Method (SFM): A case study of water access to Candida antarctica lipase B. J Chem Theory Comput. 10, 5206–5214 (2014).
- Pleiss, J.: Systematic analysis of large enzyme families: identification of specificity- and selectivity-determining hotspots. ChemCatChem. 6, 944–950 (2014).
- Gricman, L., Vogel, C., Pleiss, J.: Conservation analysis of class-specific positions in cytochrome P450 monooxygenases: functional and structural relevance. Proteins. 82, 491–504 (2014).
- Westphal, R., Jansen, S., Vogel, C., Pleiss, J., Müller, M., Rother, D., Pohl, M.: MenD from Bacillus subtilis: A Potent Catalyst for the Enantiocomplementary Asymmetric Synthesis of Functionalized α-Hydroxy Ketones. ChemCatChem. 6, 1082–1088 (2014).
- Schäfer, I., Lasko, G., Do, T., Pleiss, J., Weber, U., Schmauder, S.: Peptide - zinc oxide interaction: finite element simulation using cohesive zone models based on molecular dynamics simulation. Comp Mater Sci. 95, 320–327 (2014).
- Bogazkaya, A., von, B.C., Kriening, S., Busch, A., Seifert, A., Pleiss, J., Laschat, S., Urlacher, V.: Selective allylic hydroxylation of acyclic terpenoids by CYP154E1 from Thermobifida fusca YX. Beilstein J. Org. Chem. 10, 1347–1353 (2014).
- Baier, J., Blumenstein, N., Preusker, J., Jeurgens, L., Welzel, U., Do, T., Pleiss, J., Bill, J.: The influence of ZnO-binding 12-mer peptides on bio-inspired ZnO formation. Cryst Eng Comm. 16, 5301–5307 (2014).
- Vogel, C., Pleiss, J.: The modular structure of ThDP-dependent enzymes. Proteins. 82, 2523–2537 (2014).
2013
- Krone, M., Reina, G., Schulz, C., Kulschewski, T., Pleiss, J., Ertl, T.: Interactive Extraction and Tracking of Biomolecular Surface Features. Comput Graph Forum. 32, 331–340 (2013).
- Benson, S., Pleiss, J.: Incomplete mixing versus clathrate-like structures: a molecular view on hydrophobicity in methanol-water mixtures. J Mol Model. 19, 3427–3436 (2013).
- Roduner, E., Kaim, W., Sarkar, B., Urlacher, V., Pleiss, J., Gläser, R., Einicke, W., Sprenger, G., Beifuss, U.: Selective catalytic oxidation of CH bonds with molecular oxygen. ChemCatChem. 5, 82–112 (2013).
- Hailes, H., Rother, D., Müller, M., Westphal, R., Ward, J., Pleiss, J., Vogel, C., Pohl, M.: Engineering stereoselectivity of ThDP-dependent enzymes. FEBS J. 280, 6374–6394 (2013).
- Kulschewski, T., Pleiss, J.: 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 (2013).
- Westphal, R., Waltzer, S., Mackfeld, U., Widmann, M., Pleiss, J., Beigi, M., Müller, M., Rother, D., Pohl, M.: (S)-Selective MenD variants from Escherichia coli provide access to new functionalized chiral 2-hydroxy ketones. Chem Commun. 49, 2061–2063 (2013).
- Kulschewski, T., Sasso, F., Secundo, F., Lotti, M., Pleiss, J.: Molecular mechanism of deactivation of C. antarctica lipase B by methanol. J Biotechnol. 168, 462–469 (2013).
- Westphal, R., Hahn, D., Mackfeld, U., Waltzer, S., Beigi, M., Widmann, M., Vogel, C., Pleiss, J., Müller, M., Pohl, M.: Tailoring (S)-selectivity of MenD from Escherichia coli. ChemCatChem. 13, 3587–3594 (2013).
2012
- Fademrecht, S., Juhl, P., Sirim, D., Pleiss, J.: The triterpene cyclase protein family: a systematic analysis. Proteins. 80, 2009–2019 (2012).
- Kulschewski, T., Pleiss, J.: Simulation of enzymes in organic solvents. Wiley-VCH, Weinheim (2012).
- Gruber, C., Pleiss, J.: 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 (2012).
- Seifert, A., Pleiss, J.: Identification of selectivity determinants in CYP monooxygenases by modelling and systematic analysis of sequence and structure. Curr Drug Metab. 13, 197–202 (2012).
- Siedenburg, G., Jendrossek, D., Breuer, M., Juhl, B., Pleiss, J., Seitz, M., Klebensberger, J., Hauer, B.: Activation-independent cyclization of monoterpenoids. Appl Environ Microbiol. 78, 1055–1062 (2012).
- Pickel, B., Pfannstiel, J., Steudle, A., Lehmann, A., Gerken, U., Pleiss, J., Schaller, A.: A model of dirigent proteins derived from structural and functional similarities with alleneoxide cyclase and lipocalins. FEBS J. 279, 1980–1993 (2012).
- Baier, J., Naumburg, T., Blumenstein, N., Jeurgens, L., Welzel, U., Do, T., Pleiss, J., Bill, J.: Bio-inspired mineralization of zinc oxide in presence of ZnO-binding peptides. Biointerface Res Appl Chem. 2, 380–391 (2012).
- Widmann, M., Pleiss, J., Oelschlaeger, P.: Systematic analysis of metallo-b-lactamases using an automated database. Antimicrob Agents Ch. 56, 3481–3491 (2012).
- Pleiss, J.: Rational design of enzymes. Wiley-VCH, Weinheim (2012).
- Widmann, M., Pleiss, J., Samland, A.: Computational tools for rational protein engineering of aldolases. Comput Struct Biotechnol J. 2, e201209016–e201209016 (2012).
- Ferrario, V., Braiuca, P., Tessaro, P., Knapic, L., Gruber, C., Pleiss, J., Ebert, C., Eichhorn, E., Gardossi, L.: Elucidating the structural and conformational factors responsible for the activity and substrate specificity of alkanesulfonate monooxygenase. J Biomol Struct Dyn. 30, 74–88 (2012).
- Gruber, C., Pleiss, J.: Molecular modeling of lipase binding to a substrate-water interface. Methods Mol Biol. 861, 313–327 (2012).
- Hutt, M., Kulschewski, T., Pleiss, J.: Molecular modelling of the mass density of single proteins. J Biomol Struct Dyn. 30, 318–327 (2012).
- Vogel, C., Widmann, M., Pohl, M., Pleiss, J.: A standard numbering scheme for thiamine diphosphate-dependent decarboxylases. BMC Biochemistry. 13, 24–24 (2012).
2011
- Rother, D., Kolter, G., Gerhards, T., Berthold, C., Gauchenova, E., Knoll, M., Pleiss, J., Müller, M., Schneider, G., Pohl, M.: S-selective mixed carboligation by structure-based design of the pyruvate decarboxylase from Acetobacter pasteurianus. ChemCatChem. 3, 1587–1596 (2011).
- Habeych, D., Juhl, P., Pleiss, J., Vanegas, D., Eggink, G., Boeriu, C.: Biocatalytic synthesis of polyesters from sugar-based building blocks using immobilized Candida antarctica lipase B. J Mol Catal B - Enzym. 71, 1–9 (2011).
- Steudle, A., Pleiss, J.: Modelling of lysozyme binding to a cation exchange surface at atomic detail: the role of flexibility. Biophys.J. 100, 3016–3024 (2011).
- Pleiss, J.: Protein design in metabolic engineering and synthetic biology. Curr.Opin.Biotech. 22, 1–7 (2011).
- Krone, M., Falk, M., Rehm, S., Pleiss, J., Ertl, T.: Interactive exploration of protein cavities. Comput Graph Forum. 30, 673–682 (2011).
- Seifert, A., Antonovici, M., Hauer, B., Pleiss, J.: An efficient route to selective bio-oxidation catalysts: an iterative approach comprising modeling, diversification, and screening, based on CYP102A1. ChemBioChem. 12, 1346–1351 (2011).
- Weber, E., Seifert, A., Antonovici, M., Geinitz, C., Pleiss, J., Urlacher, V.: Screening of a minimal enriched P450 BM3 mutant library for hydroxylation of cyclic and acyclic alkanes. Chem.Commun. 47, 944–946 (2011).
- Sirim, D., Wagner, F., Wang, L., Schmid, R., Pleiss, J.: The Laccase Engineering Database: a classification and analysis system for laccases and related multicopper oxidases. Database. bar006, (2011).
- Gruber, C., Pleiss, J.: Systematic benchmarking of large molecular dynamics simulations employing GROMACS on massive multiprocessing facilities. J.Comput.Chem. 32, 600–606 (2011).
2010
- Widmann, M., Juhl, P., Pleiss, J.: Structural classification by the Lipase Engineering Database: a case study of Candida antarctica lipase A. BMC Genomics. 11, 123 (2010).
- Juhl, P., Doderer, K., Hollmann, F., Thum, O., Pleiss, J.: Engineering of Candida antarctica lipase B forhydrolysis of bulky carboxylic acid esters. J Biotechnol. 150, 474–480 (2010).
- Thai, K., Pleiss, J.: SHV Lactamase Engineering Database: a reconciliation tool for SHV β-lactamases in public databases. BMC Genomics. 11, 563–563 (2010).
- Rehm, S., Trodler, P., Pleiss, J.: Solvent-induced lid opening in lipases: A molecular dynamics study. Protein Sci. 19, 2122–2130 (2010).
- Widmann, M., Radloff, R., Pleiss, J.: The Thiamine diphosphate dependent Enzyme Engineering Database: A tool for the systematic analysis of sequence and structure relations. BMC Biochemistry. 11, 9–9 (2010).
- Liu, D., Trodler, P., Eiben, S., Koschorrek, K., Mueller, M., Pleiss, J., Maurer, S., Branneby, C., Schmid, R.: Rational Design of Pseudozyma antarctica Lipase B Yielding a General Esterification Catalyst. Chem. Bio. Chem. 11, 789–795 (2010).
- Trodler, P., Eiben, S., Koschorreck, K., Müller, M., Pleiss, J., Maurer, S., Branneby, C., Schmid, R.: Rational design of Pseudozyma antarctica lipase B yielding a general esterification catalyst. ChemBioChem. 11, 789–795 (2010).
- Widmann, M., Trodler, P., Pleiss, J.: The isoelectric region of proteins: a systematic analysis. PLoS One. 5, e10546–e10546 (2010).
- Weber, E., Sirim, D., Schreiber, T., Bejoy, T., Pleiss, J., Hunger, M., Gläser, R., Urlacher, V.: Immobilization of P450 BM-3 monooxygenase on mesoporous molecular sieves with differentpore diameters. J Mol Catal B. 64, 29–37 (2010).
- Gatti-Lafranconi, P., Natalello, A., Rehm, S., Doglia, S., Pleiss, J., Lotti, M.: 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 (2010).
- Sirim, D., Widmann, M., Wagner, F., Pleiss, J.: Prediction and analysis of the modular structure of cytochrome P450 monooxygenases. BMC Struct Biol. 10, 34–34 (2010).
2009
- Knoll, M., Hamm, T., Wagner, F., Martinez, V., Pleiss, J.: The PHA Depolymerase Engineering Database: A systematic analysis tool for the diverse family of polyhydroxyalkanoate (PHA) depolymerases. BMC Bioinformatics. 10, 89 (2009).
- Seifert, A., Pleiss, J.: Identification of selectivity-determining residues in cytochrome P450 monooxygenases: a systematic analysis of the substrate recognition site 5. Proteins. 74, 1028–1035 (2009).
- Seifert, A., Vomund, S., Grohmann, K., Kriening, S., Urlacher, V., Laschat, S., Pleiss, J.: Rational design of a minimal and highly enrichedCYP102A1 mutant library with improved regio-, stereo- and chemoselectivity. ChemBioChem. 10, 853–861 (2009).
- Bös, F., Pleiss, J.: Multiple molecular dynamics simulations of TEMbeta-lactamase: Dynamics and water binding of the Omega-loop. Biophys J. 97, 2550–2558 (2009).
- Juhl, P., Trodler, P., Tyagi, S., Pleiss, J.: Modelling substrate specificity and enantioselectivity for lipases and esterases by substrate-imprinted docking. BMC Struct Biol. 9, 39 (2009).
- Thai, Q., Bös, F., Pleiss, J.: The Lactamase Engineering Database: a critical survey of TEM sequences in public databases. BMC Genomics. 10, 390 (2009).
- Branco, R., Graber, M., Denis, V., Pleiss, J.: Molecular mechanism of the hydration of Candida antarctica lipase B in gas phase: water adsorption isotherms and molecular dynamics simulations. ChemBioChem. 10, 2913–2919 (2009).
- Trodler, P., Schmid, R., Pleiss, J.: Modeling of solvent-dependent conformational transitions in Burkholderia cepacia lipase. BMC Struct Biol. 9, 38 (2009).
- Sirim, D., Wagner, F., Lisitsa, A., Pleiss, J.: The Cytochrome P450 Engineering Database: integration of biochemical properties. BMC Biochemistry. 10, 27 (2009).
- Chen, B., Huang, Y., Pleiss, J., Lin, Z.: Morphing activity between structurally similar enzymes: from heme-free bromoperoxidase to lipase. Biochemistry. 48, 11496–11504 (2009).
- Dietrich, M., Schmid, R., Pleiss, J., Urlacher, V.: Altering the regioselectivity of the subterminal fatty acid hydroxylase P450 BM-3 towards gamma- and delta-positions. J Biotechnol. 139, 115–117 (2009).
2008
- Trodler, P., Pleiss, J.: Modeling structure and flexibility of Candida antarctica lipase B in organic solvents. BMC Struct Biol. 8, 9 (2008).
- Widmann, M., Clairo, M., Dippon, J., Pleiss, J.: Analysis of the distribution of functionally relevant rare codons. BMC Genomics. 9, 207 (2008).
- Trodler, P., Nieveler, J., Rusnak, M., Schmid, R., Pleiss, J.: Rational design of a new one-step purification strategy for Candida antarctica lipase B by ion-exchange chromatography. J Chromatogr A. 1179, 161–167 (2008).
- Gocke, D., Walter, L., Gauchenova, E., Kolter, G., Knoll, M., Berthold, C., Schneider, G., Pleiss, J., Müller, M., Pohl, M.: Rational protein design of ThDP-dependent enzymes: engineering stereoselectivity. ChemBioChem. 9, 406–412 (2008).
- Bös, F., Pleiss, J.: Conserved water molecules stabilize the omega-loop in class A beta-lactamases. Antimicrob Agents Chemother. 52, 1072–1079 (2008).
- Branco, R., Seifert, A., Budde, M., Urlacher, V., Ramos, M., Pleiss, J.: Anchoring effects in a wide binding pocket: The molecular basis of regioselectivity in engineered cytochrome P450 monooxygenase from B. megaterium. Proteins. 73, 597–607 (2008).
- Messerschmidt, S., Kolbe, A., Müller, D., Knoll, M., Pleiss, J., Kontermann, R.: Novel single-chain Fv′ formats for the generation of immunoliposomes by site-directed coupling. Bioconjugate Chem. 19, 362–369 (2008).
- Bidmon, K., Grottel, S., Bös, F., Pleiss, J., Ertl, T.: Visual abstractions of solvent pathlines near protein cavities. Comput Graph Forum. 27, 935–942 (2008).
- Dietrich, M., Eiben, S., Asta, C., Pleiss, J., Urlacher, V.: Cloning, expression and characterisation of CYP102A7, a self-sufficient P450 from Bacillus licheniformis. Appl Microbiol Biotechnol. 79, 931–940 (2008).
- Knoll, M., Pleiss, J.: 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 (2008).
2007
- Pleiss, J.: Human Cytochrome P450 Monooxygenases – a General Model of Substrate Specificity and Regioselectivity. Wiley-VCH, NULL (2007).
- Klein, K., Tatzel, S., Raimundo, S., Saussele, T., Hustert, E., Pleiss, J., Eichelbaum, M., Zanger, U.: A natural variant of the heme-bindingsignature (R441C) resulting in complete loss of the function of CYP2D6. Drug Metab Dispos. 35, 1247–1250 (2007).
- Oelschlaeger, P., Pleiss, J.: 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 (2007).
- Fischer, M., Knoll, M., Sirim, D., Wagner, F., Funke, S., Pleiss, J.: The Cytochrome P450 Engineering Database: a navigation and prediction tool for the cytochrome P450 protein family. Bioinformatics. 23, 2015–2017 (2007).
2006
- Fischer, M., Thai, Q., Grieb, M., Pleiss, J.: DWARF - a data warehouse system for analyzing protein families. BMC Bioinformatics. 7, 495–495 (2006).
- Knoll, M., Müller, M., Pleiss, J., Pohl, M.: Factors mediating activity, selectivity, and substrate specificity for the thiamin diphosphate-dependent enzymes benzaldehyde lyase and benzoylformate decarboxylase. Chembiochem. 7, 1928–1934 (2006).
- Tyagi, S., Pleiss, J.: Biochemical profiling in silico - Predicting substrate specificities of large enzyme families. J Biotechnol. 124, 108–116 (2006).
- Pleiss, J.: The promise of synthetic biology. Appl Microbiol Biotechnol. 73, 735–739 (2006).
- Seifert, A., Tatzel, S., Schmid, R., Pleiss, J.: Multiple molecular dynamics simulations of human P450 monooxygenase CYP2C9: the molecular basis of substrate binding and regioselectivity toward warfarin. Proteins. 64, 147–155 (2006).
2005
- Riepe, F., Tatzel, S., Sippell, W., Pleiss, J., Krone, N.: Congenital adrenal hyperplasia: the molecular basis of 21-hydroxylase deficiency in H-2(aw18) mice. Endocrinology. 146, 2563–2574 (2005).
- Koschorreck, M., Fischer, M., Barth, S., Pleiss, J.: How to find soluble proteins: a comprehensive analysis of alpha/beta hydrolases for recombinant expression in E. coli. BMC Genomics. 6, 1–10 (2005).
- Oelschlaeger, P., Mayo, S., Pleiss, J.: Impact of remote mutations on metallo-beta-lactamase substrate specificity: implications for the evolution of antibiotic resistance. Protein Sci. 14, 765–774 (2005).
- Bornscheuer, U., Henke, E., Pleiss, J.: Enzymatic methods. Wiley-VCH, Weinheim (2005).
2004
- Tejo, B., Salleh, A., Pleiss, J.: Structure and dynamics of Candida rugosa lipase: the role of organic solvent. J Mol Model. 10, 358–366 (2004).
- Barth, S., Fischer, M., Schmid, R., Pleiss, J.: The database of epoxide hydrolases andhaloalkane dehalogenases: one structure, manyfunctions. Bioinformatics. 20, 2845–2847 (2004).
- Strohmeier, M., Hrmova, M., Fischer, M., Harvey, A., Fincher, G., Pleiss, J.: 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 (2004).
- Schmid, R., Pleiss, J., Urlacher, V.: Biokatalyse: Selektivoxidation von C-H-Bindungen mit O2. Nachr Chem. 52, 767–772 (2004).
- Currle-Linde, N., Boes, F., Lindner, P., Pleiss, J., Resch, M.: A Management System for Complex Parameter Studies and Experiments in Grid Computing. Acta press, Cambridge (2004).
- Richter, T., Muerdter, T., Heinkele, G., Pleiss, J., Tatzel, S., Schwab, M., Eichelbaum, U., Zanger, M.: Potent mechanism-based inhibition of human CYP2B6 by clopidogrel and ticlopidine. J Pharmacol Exp Ther. 303, 189–197 (2004).
- Barth, S., Fischer, M., Schmid, R., Pleiss, J.: Sequence and structure of epoxide hydrolases: a systematic analysis. Proteins. 55, 846–855 (2004).
2003
- Oelschlaeger, P., Schmid, R., Pleiss, J.: Insight into the mechanism of the IMP-1 metallo-beta-lactamase by molecular dynamics simulations. Protein Eng. 16, 341–350 (2003).
- Henke, E., Bornscheuer, U., Schmid, R., Pleiss, J.: A molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases. ChemBioChem. 4, 485–493 (2003).
- Oelschlaeger, P., Schmid, R., Pleiss, J.: 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 (2003).
- Fischer, M., Pleiss, J.: The Lipase Engineering Database: a navigation and analysis tool for protein families. Nucleic Acids Res. 31, 319–321 (2003).
- Lich, N., Barth, F., Pleiss, J., Hai, T.: Homology modelling of alpha-amylase from Saccharomycopsis fibuligera with maltohexaose substrate. Vietnam Journal of Biotechnology. 1, 149–159 (2003).
2002
- Bathelt, C., Schmid, R., Pleiss, J.: Regioselectivity of CYP2B6: homology modeling, molecular dynamics simulation, docking. J Mol Model. 8, 327–335 (2002).
- Kusharyoto, W., Pleiss, J., Bachmann, T., Schmid, R.: Mapping of a hapten-binding site: molecular modeling and site-directed mutagenesis study of an anti-atrazine antibody. Protein Eng. 15, 233–241 (2002).
- Gentner, C., Schmid, R., Pleiss, J.: Primary alcohols in a ring structure: quantifying enantioselectivity of Pseudomonas cepacia lipase by an in silico assay. Colloids Surf B Biointerfaces. 26, 57–66 (2002).
- Henke, E., Pleiss, J., Bornscheuer, U.: Activity of lipases and esterases towards tertiary alcohols: insights into structure-function relationships. Angew Chem Int Ed. 41, 3211–3213 (2002).
- Schmitt, J., Brocca, S., Schmid, R., Pleiss, J.: Blocking the tunnel: engineering of Candida rugosa lipase mutants with short chain length specificity. Protein Eng. 15, 595–601 (2002).
2001
- Kahlow, U., Schmid, R., Pleiss, J.: A model of the pressure dependence of the enantioselectivity of Candida rugosa lipase towards (±)-menthol. Protein Sci. 10, 1942–1952 (2001).
- Schulz, T., Schmid, R., Pleiss, J.: Structural basis of stereoselectivity in Candida rugosa lipase-catalyzed hydrolysis of secondary alcohols. J Mol Model. 7, 265–270 (2001).
- Schwaneberg, U., Fischer, M., Schmitt, J., Pleiss, J., Lutz-Wahl, S., Schmid, R.: Rational evolution of a medium chain-specific cytochrome P-450 BM-3 variant. Biochim Biophys Acta. 1545, 114–121 (2001).
- Bachmann, T., Pleiss, J., Villatte, F., Schmid, R.: Bioresponse-Linked Analysis Based on Acetylcholinesterase Inhibition. B.G. Teubner, Stuttgart (2001).
2000
- Bornscheuer, U., Pleiss, J., Schmidt-Dannert, C., Schmid, R.: Lipases from Rhizopus species: genetics, structure and applications. CRC Press (2000).
- Otto, R., Scheib, H., Bornscheuer, U., Pleiss, J., Syldatk, C., Schmid, R.: Substrate specificity of lipase B from Candida antarctica in the synthesis of arylaliphatic glycolipids. J Mol Catal B Enzym. 8, 201–211 (2000).
- Pleiss, J., Fischer, M., Peiker, M., Thiele, C., Schmid, R.: Lipase Engineering Database: understanding and exploiting sequence-structure-function relationships. J Mol Catal B: Enzym. 10, 491–508 (2000).
- Kovac, A., Scheib, H., Pleiss, J., Schmid, R., Paltauf, F.: Molecular basis of lipase stereoselectivity. Eur J Lipid Sci Tech. 102, 61–77 (2000).
- Pleiss, J., Fischer, M., Scheib, H., Schulz, T., Schmid, R.: Modelling structure-function relationship of lipase binding sites-a case study of specificity and selectivity. Crete University Press (2000).
- Pleiss, J.: In silico-Assays: Computergestuetzte Modellierung der Stereoselektivität von Lipasen. Transkript. 9, 38–40 (2000).
- Pleiss, J., Scheib, H., Schmid, R.: The his gap motif in microbial lipases: a determinant of stereoselectivity toward triacylglycerols and analogs. Biochimie. 82, 1043–1052 (2000).
- Hwang, B., Scheib, H., Pleiss, J., Kim, B., Schmid, R.: Computer-aided molecular modeling of the enantioselectivity of Pseudomonas cepacia lipase toward g- and d-lactones. J Mol Catal B Enzym. 10, 223–231 (2000).
- Schulz, T., Pleiss, J., Schmid, R.: Stereoselectivity of Pseudomonas cepacia lipase towards secondary alcohols: a quantitative model. Protein Sci. 9, 1053–1062 (2000).
1999
- Scheib, H., Pleiss, J., Kovac, A., Paltauf, F., Schmid, R.: Stereoselectivity of Mucorales lipases toward triradylglycerols--a simple solution to a complex problem. Protein Sci. 8, 215–221 (1999).
- Pleiss, J., Schmid, R.: Bioinformatics and the internet. Chemistry International. 21, 33–36 (1999).
- Pleiss, J., Mionetto, N., Schmid, R.: Probing the acyl binding site of acetylcholinesterase by protein engineering. J Mol Catal B: Enzym. 6, 287–296 (1999).
1998
- Schmidt-Dannert, C., Pleiss, J., Schmid, R.: A toolbox of recombinant lipases for industrial applications. Ann N Y Acad Sci. 864, 14–22 (1998).
- Scheib, H., Pleiss, J., Stadler, P., Kovac, A., Potthoff, A., Haalck, L., Spener, F., Paltauf, F., Schmid, R.: Rational design of Rhizopus oryzae lipase with modified stereoselectivity toward triradylglycerols. Protein Eng. 11, 675–682 (1998).
- Hülser, D., Eckert, R., Irmer, U., Krisciukaitis, A., Mindermann, A., Pleiss, J., Rehkopf, B., Sharovskaya, J., Traub, O.: Intercellular communication via gap junction channels. Bioelectrochem Bioenerg. 45, 55–65 (1998).
- Pleiss, J., Fischer, M., Schmid, R.: Anatomy of lipase binding sites: the scissile fatty acid binding site. Chem Phys Lipids. 93, 67–80 (1998).
- Mindermann, A., Pleiss, J., Hülser, D.: Molecular Modeling of Gap Junction Pores. IOS Press, Florida (1998).
- Drees, R., Pleiss, J., Schmid, R., Roller, D.: Integrating molecular modeling tools and virtual reality engines: an architecture for a highly immersive molecular modeling (HIMM) environment. Proceedings of CGI. 391–392 (1998).
- Otto, R., Bornscheuer, U., Scheib, H., Pleiss, J., Syldatk, C., Schmid, R.: Lipase-catalyzed esterification of unusual substrates: synthesis of glucuronic acid and ascorbic acid. Biotechnol Lett. 20, 1091–1094 (1998).
1997
- Pleiss, J., Mionetto, N., Schmid, R.: Protein engineering of rat brain acetylcholinesterase: a point mutation enhances sensitivityto pesticides. Protein Eng. 10, 66–66 (1997).
- Holzwarth, H.-C., Pleiss, J., Schmid, R.: Computer-aided modelling of stereoselective triglyceride hydrolysis catalyzed by Rhizopus oryzae lipase. J Mol Catal B Enzym. 3, 73–82 (1997).
- Weber, H., Zuegg, J., Faber, J., Pleiss, J.: Molecular reasons for lipase-sensitivity against acetaldehyde. J Mol Catal B: Enzym. 3, 131–138 (1997).
- Haalck, L., Paltauf, F., Pleiss, J., Schmid, R., Spener, F., Stadler, P.: Stereoselectivity of lipase from Rhizopus oryzae toward triacylglycerols and anlogs: computer aided modelling and experimental validation. Methods Enzymol. 284, 353–376 (1997).
1996
- Drees, R., Pleiss, J., Schmid, R.: Highly immersive molecular modeling (HIMM): an architecture for the integration of molecular modelling and virtual reality. Universität Leipzig, Leipzig (1996).
1994
- Pleiss, J.: Molecular basis of specificity and stereoselectivity of microbial lipases toward triacylglycerols. Wiley-VCH, Weinheim (1994).
- Pleiss, J.: Quantitative modelling of lipase enantioselectivity. Marcel Dekker (1994).
1992
- Pleiss, J., Jähnig, F.: Conformational transition of an alpha-helix studied by molecular dynamics. Eur Biophys J. 21, 63–70 (1992).
1991
- Pleiss, J., Jähnig, F.: Collective vibrations of an alpha-helix. A molecular dynamics study. Biophys J. 59, 795–804 (1991).
1989
- Roditi, I., Schwarz, H., Pearson, T., Beecroft, R., Liu, M., Richardson, J., Bühring, H., Pleiss, J., Bülow, R., et, al.: Procyclin gene expression and loss of the variant surface glycoprotein during differentiation of Trypanosoma brucei. J Cell Biol. 108, 737–746 (1989).