All Outputs (3)

Characterisation of geranylgeranyl diphosphate synthase from the sandfly Lutzomyia longipalpis (2023)
Journal Article
Ducker, C., French, S., Pathak, M., Taylor, H., Sainter, A., Askem, W., …Oldham, N. J. (2023). Characterisation of geranylgeranyl diphosphate synthase from the sandfly Lutzomyia longipalpis. Insect Biochemistry and Molecular Biology, 161, Article 104001. https://doi.org/10.1016/j.ibmb.2023.104001

Leishmaniasis is a debilitating and often fatal neglected tropical disease. Males from sub-populations of the Leishmania-harbouring sandfly, Lutzomyia longipalpis, produce the diterpene sex and aggregation pheromone, sobralene, for which geranylgeran... Read More about Characterisation of geranylgeranyl diphosphate synthase from the sandfly Lutzomyia longipalpis.

Factor XII and kininogen asymmetric assembly with gC1qR/C1QBP/P32 is governed by allostery (2020)
Journal Article
Kaira, B. G., Slater, A., McCrae, K. R., Dreveny, I., Sumya, U., Mutch, N. J., …Emsley, J. (2020). Factor XII and kininogen asymmetric assembly with gC1qR/C1QBP/P32 is governed by allostery. Blood, 136(14), 1685–1697. https://doi.org/10.1182/blood.2020004818

The contact system is composed of Factor XII (FXII), prekallikrein (PK) and co-factor kininogen (HK). The globular C1q receptor (gC1qR) has been shown to interact with FXII and HK. We reveal the FXII fibronectin type II domain (FnII) binds gC1qR in a... Read More about Factor XII and kininogen asymmetric assembly with gC1qR/C1QBP/P32 is governed by allostery.

Structural and biochemical evaluation of bisubstrate inhibitors of protein arginine N-methyltransferases PRMT1 and CARM1 (PRMT4) (2020)
Journal Article
Gunnell, E. A., Al-Noori, A., Muhsen, U., Davies, C. C., Dowden, J., & Dreveny, I. (2020). Structural and biochemical evaluation of bisubstrate inhibitors of protein arginine N-methyltransferases PRMT1 and CARM1 (PRMT4). Biochemical Journal, 477(4), 787–800. https://doi.org/10.1042/bcj20190826

Attenuating the function of protein arginine methyltransferases (PRMTs) is an objective for the investigation and treatment of several diseases including cardiovascular disease and cancer. Bisubstrate inhibitors that simultaneously target binding sit... Read More about Structural and biochemical evaluation of bisubstrate inhibitors of protein arginine N-methyltransferases PRMT1 and CARM1 (PRMT4).