Dieses Bild zeigt Patrick Buchholz

Patrick Buchholz

Herr Dr.

Bioinformatik
Institut für Biochemie und Technische Biochemie
Technische Biochemie

Kontakt

Allmandring 31
70569 Stuttgart
Deutschland
Raum: 0.315

  1. Buchholz, P., Feuerriegel, G., Zhang, H., Pérez-García, P., Nover, L., Chow, J., Streit, W., & Pleiss, J. (2022). Plastics degradation by hydrolytic enzymes: the Plastics-Active Enzymes Database - PAZy. Proteins, 90, 1443–1456.
  2. 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
  3. 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
  4. 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
  5. 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
  6. 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.
  7. 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
  8. 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
  9. Gräff, M., Buchholz, P., Le Roes-Hill, M., & Pleiss, J. (2020). Multicopper oxidases: modular structure, sequence space and evolutionary relationships. Proteins.
  10. 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.
  11. 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.
  12. 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.
  13. 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.
  14. 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.
  15. 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.
  16. 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.
  17. 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.
  18. Buchholz, P., Zeil, C., & Pleiss, J. (2018). The scale-free nature of protein sequence space. PLoS One, 13, e0200815.
  19. Buchholz, P., Fademrecht, S., & Pleiss, J. (2017). Percolation in protein sequence space. PLoS One, 12, e0189646.
  20. 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.
  21. 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.
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