Outputs (6)

Heparin Inhibits Cellular Invasion by SARS-CoV-2: Structural Dependence of the Interaction of the Spike S1 Receptor-Binding Domain with Heparin. (2020)
Journal Article
Mycroft-West, C. J., Su, D., Pagani  , I., Rudd  , T. R., Elli  , S., Gandhi  , N. S., …Skidmore   , M. A. (2020). Heparin Inhibits Cellular Invasion by SARS-CoV-2: Structural Dependence of the Interaction of the Spike S1 Receptor-Binding Domain with Heparin. Thrombosis and Haemostasis, 120(12), 1700 - 1715. https://doi.org/10.1055/s-0040-1721319

The dependence of development and homeostasis in animals on the interaction of hundreds of extracellular regulatory proteins with the peri- and extracellular glycosaminoglycan heparan sulfate (HS) is exploited by many microbial pathogens as a means o... Read More about Heparin Inhibits Cellular Invasion by SARS-CoV-2: Structural Dependence of the Interaction of the Spike S1 Receptor-Binding Domain with Heparin..

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..

Development of a nano-luciferase based assay to measure the binding of SARS-CoV-2 spike receptor binding domain to ACE-2 (2020)
Journal Article
Andrade De Lima, M., Skidmore, M., Khanim, F., & Richardson, A. (2020). Development of a nano-luciferase based assay to measure the binding of SARS-CoV-2 spike receptor binding domain to ACE-2. Biochemical and Biophysical Research Communications, 534, 485--490. https://doi.org/10.1016/j.bbrc.2020.11.055

To identify drugs that could potentially be used to treat infection with SARS-CoV-2, a high throughput 384-well assay was developed to measure the binding of the receptor binding domain (RBD) of the viral S1 protein to its main receptor, angiotensin... Read More about Development of a nano-luciferase based assay to measure the binding of SARS-CoV-2 spike receptor binding domain to ACE-2.

Glycosaminoglycans induce conformational change in the SARS-CoV-2 Spike S1 Receptor Binding Domain (2020)
Journal Article
Mycroft-West, C. J., Su, D., Li, Y., Guimond, S. E., Rudd, T. R., Elli, S., …Skidmore, M. A. Glycosaminoglycans induce conformational change in the SARS-CoV-2 Spike S1 Receptor Binding Domain. bioRxiv, https://doi.org/10.1101/2020.04.29.068767

The glycosaminoglycan (GAG) class of polysaccharides are utilised by a plethora of microbial pathogens as receptors for adherence and invasion. The GAG heparin prevents infection by a range of viruses when added exogenously, including the S-associate... Read More about Glycosaminoglycans induce conformational change in the SARS-CoV-2 Spike S1 Receptor Binding Domain.

SARS-CoV-2 Spike S1 Receptor Binding Domain undergoes Conformational Change upon Interaction with Low Molecular Weight Heparins (2020)
Journal Article
Mycroft-West, C. J., Su, D., Li, Y., Guimond, S. E., Rudd, T. R., Elli, S., …Skidmore, M. A. SARS-CoV-2 Spike S1 Receptor Binding Domain undergoes Conformational Change upon Interaction with Low Molecular Weight Heparins. arXiv, https://doi.org/10.1101/2020.04.29.068486

The dependence of the host on the interaction of hundreds of extracellular proteins with the cell surface glycosaminoglycan heparan sulphate (HS) for the regulation of homeostasis is exploited by many microbial pathogens as a means of adherence and i... Read More about SARS-CoV-2 Spike S1 Receptor Binding Domain undergoes Conformational Change upon Interaction with Low Molecular Weight Heparins.

Inhibition of BACE1, the ß-secretase implicated in Alzheimer's disease, by a chondroitin sulfate extract from Sardina pilchardus. (2020)
Journal Article
Mycroft-West, C. J., Devlin, A. J., Cooper, L. C., Procter, P., Miller, G. J., Fernig, D. G., …Skidmore, M. A. (2020). Inhibition of BACE1, the ß-secretase implicated in Alzheimer's disease, by a chondroitin sulfate extract from Sardina pilchardus. Neural Regeneration Research, 15(8), 1546 - 1553. https://doi.org/10.4103/1673-5374.274341

The pharmaceutical and anticoagulant agent heparin, a member of the glycosaminoglycan family of carbohydrates, has previously been identified as a potent inhibitor of a key Alzheimer's disease drug target, the primary neuronal ß-secretase, ß-site amy... Read More about Inhibition of BACE1, the ß-secretase implicated in Alzheimer's disease, by a chondroitin sulfate extract from Sardina pilchardus..