Outputs (3)

Accessing active fragments for drug discovery utilising nitroreductase biocatalysis. (2024)
Journal Article
Holder, L., Yuce, E., Oriomah, G., Jenkins, A.-P., Reynisson, J., Winter, A., & Cosgrove, S. (in press). Accessing active fragments for drug discovery utilising nitroreductase biocatalysis. ChemBioChem, Article e202400428. https://doi.org/10.1002/cbic.202400428

Biocatalysis has played a limited role in the early stages of drug discovery. This is often attributed to the limited substrate scope of enzymes not affording access to vast areas of novel chemical space. Here, we have shown a promiscuous nitroreduct... Read More about Accessing active fragments for drug discovery utilising nitroreductase biocatalysis..

Characterization and structural determination of a new anti-MET function-blocking antibody with binding epitope distinct from the ligand binding domain. (2017)
Journal Article
DiCara, D. M., Chirgadze, D. Y., Pope, A. R., Karatt-Vellatt, A., Winter, A., Slavny, P., …McCafferty, J. (2017). Characterization and structural determination of a new anti-MET function-blocking antibody with binding epitope distinct from the ligand binding domain. Scientific reports, 9000 - ?. https://doi.org/10.1038/s41598-017-09460-2

The growth and motility factor Hepatocyte Growth Factor/Scatter Factor (HGF/SF) and its receptor, the product of the MET proto-oncogene, promote invasion and metastasis of tumor cells and have been considered potential targets for cancer therapy. We... Read More about Characterization and structural determination of a new anti-MET function-blocking antibody with binding epitope distinct from the ligand binding domain..

Structural Insights into Separase Architecture and Substrate Recognition through Computational Modelling of Caspase-Like and Death Domains (2015)
Journal Article
Winter, A., Schmid, R., & Bayliss, R. (2015). Structural Insights into Separase Architecture and Substrate Recognition through Computational Modelling of Caspase-Like and Death Domains. PLoS Computational Biology, e1004548 - ?. https://doi.org/10.1371/journal.pcbi.1004548

Separases are large proteins that mediate sister chromatid disjunction in all eukaryotes. They belong to clan CD of cysteine peptidases and contain a well-conserved C-terminal catalytic protease domain similar to caspases and gingipains. However, unl... Read More about Structural Insights into Separase Architecture and Substrate Recognition through Computational Modelling of Caspase-Like and Death Domains.