Researcher Portfolio
Prasad, Beluvalli E.
Inorganic Chemistry, Max Planck Institute for Chemical Physics of Solids, Max Planck Society
Researcher Profile
Position: Inorganic Chemistry, Max Planck Institute for Chemical Physics of Solids, Max Planck Society
Researcher ID: https://pure.mpg.de/cone/persons/resource/persons194829
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Publications
: Maier, M., Rajendran, C., Malisi, C., Fox, N., Xu, C., Schlee, S., Barondeau, D., Höcker, B., Sterner, R., & Raushel, F. (2013). Molecular engineering of organophosphate hydrolysis activity from a weak promiscuous lactonase template. Journal of the American Chemical Society, 135(31), 11670-11677. doi:10.1021/ja405911h. [PubMan] : Malisi, C., Schumann, M., Toussaint, N., Kageyama, J., Kohlbacher, O., & Höcker, B. (2012). Binding pocket optimization by computational protein design. PLoS One, 7(12): e52505. doi:10.1371/journal.pone.0052505. [PubMan] : Engel, D., Kottler, V., Malisi, C., Röttig, M., Willing, E., & Schultheiss, S. (2012). Crowd-Sourcing Design: Sketch Minimization using Crowds for Feedback. In 4th Human Computation Workshop (HCOMP 2012) (pp. 71-77). [PubMan] : Malisi, C., Stiel, A., & Höcker, B. (2011). Enzyme am Reißbrett. Biospektrum, 17(7), 736-738. doi:10.1007/s12268-011-0117-0. [PubMan] : Engel, D., Kottler, V., Malisi, C., Röttig, M., Schultheiss, S., Willing, E., Curio, C., & Bülthoff, H. (2010). Optimizing minimal sketches of visual object categories. Perception, 39(ECVP Abstract Supplement), 11. [PubMan] : Malisi, C., Kohlbacher, O., & Höcker, B. (2009). Automated scaffold selection for enzyme design. Proteins: Structure, Function, and Genetics, 77(1), 74-83. doi:10.1002/prot.22418. [PubMan] : Malisi, C., Höcker, B., & Kohlbacher, O. (2009). Automated scaffold selection in enzyme design. Poster presented at 17th Annual International Conference on Intelligent Systems for Molecular Biology & 8th European Conference on Computational Biology (ISMB ECCB 2009), Stockholm, Sweden. [PubMan] : Claren, J., Malisi, C., Höcker, B., & Sterner, R. (2009). Establishing wild-type levels of catalytic activity on natural and artificial (βα)8-barrel protein scaffolds. Proceedings of the National Academy of Sciences of the United States of America, 106(10), 3704-3709. doi:10.1073/pnas.0810342106. [PubMan]