Outputs (5)

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, 25(18), 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..

Effect of cardiolipin on the lamellarity and elongation of liposomes hydrated in PBS (2024)
Journal Article
Piccinini, A., Kohlbrecher, J., Moussaoui, D., Winter, A., & Prévost, S. (in press). Effect of cardiolipin on the lamellarity and elongation of liposomes hydrated in PBS. Journal of Colloid and Interface Science, 669, 844-855. https://doi.org/10.1016/j.jcis.2024.04.211

Lamellarity and shape are important factors in the formation of vesicles and determine their role in biological systems and pharmaceutical applications. Cardiolipin (CL) is a major lipid in many biological membranes and exerts a gr... Read More about Effect of cardiolipin on the lamellarity and elongation of liposomes hydrated in PBS.

Galactokinase-like protein from Leishmania donovani: Biochemical and structural characterization of a recombinant protein. (2024)
Journal Article
Baber, H., Aghajani, A., Gallimore, B. H., Bethel, C., Hyatt, J. G., King, E. F. B., …Winter, A. (2024). Galactokinase-like protein from Leishmania donovani: Biochemical and structural characterization of a recombinant protein. Biochimie, 223, 31-40. https://doi.org/10.1016/j.biochi.2024.03.017

Leishmaniasis is a spectrum of conditions caused by infection with the protozoan Leishmania spp. parasites. Leishmaniasis is endemic in 98 countries around the world, and resistance to current anti-leishmanial drugs is rising. Our work has identified... Read More about Galactokinase-like protein from Leishmania donovani: Biochemical and structural characterization of a recombinant protein..

Molecular Changes in Dengue Envelope Protein Domain III upon Interaction with Glycosaminoglycans. (2020)
Journal Article
Hyatt, J. G., Prévost, S., Devos, J. M., Mycroft-West, C. J., Skidmore, M. A., & Winter, A. (2020). Molecular Changes in Dengue Envelope Protein Domain III upon Interaction with Glycosaminoglycans. Pathogens an international, open access journal of pathogens and pathogen-host interactions, 9(11), Article 935. https://doi.org/10.3390/pathogens9110935

Dengue fever is a rapidly emerging vector-borne viral disease with a growing global burden of approximately 390 million new infections per annum. The Dengue virus (DENV) is a flavivirus spread by female mosquitos of the aedes genus, but the mechanism... Read More about Molecular Changes in Dengue Envelope Protein Domain III upon Interaction with Glycosaminoglycans..

Exploring the chemical space of the lysine-binding pocket of the first kringle domain of hepatocyte growth factor/scatter factor (HGF/SF) yields a new class of inhibitors of HGF/SF-MET binding. (2015)
Journal Article
Winter. (2015). Exploring the chemical space of the lysine-binding pocket of the first kringle domain of hepatocyte growth factor/scatter factor (HGF/SF) yields a new class of inhibitors of HGF/SF-MET binding. Chemical Science, 6147 - 6157. https://doi.org/10.1039/C5SC02155C

The growth/motility factor hepatocyte growth factor/scatter factor (HGF/SF) and its receptor, the tyrosine kinase MET, constitute a signalling system essential for embryogenesis and for tissue/organ regeneration in post-natal life. HGF/SF-MET signall... Read More about Exploring the chemical space of the lysine-binding pocket of the first kringle domain of hepatocyte growth factor/scatter factor (HGF/SF) yields a new class of inhibitors of HGF/SF-MET binding..