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Preparation of an antibacterial poly(ionic liquid) graft copolymer of hydroxyethyl cellulose (2015)
Journal Article
Joubert, F., Yeo, R. P., Sharples, G. J., Musa, O. M., Hodgson, D. R., & Cameron, N. R. (2015). Preparation of an antibacterial poly(ionic liquid) graft copolymer of hydroxyethyl cellulose. Biomacromolecules, 16(12), 397-3979. https://doi.org/10.1021/acs.biomac.5b01300

Poly(ionic liquid)s (P(IL)s) of different degrees of polymerisation (10, 50 and 100) were prepared via RAFT polymerisation using an alkyne-terminated xanthate as transfer agent, with a monomer conversion of up to ~80% and a ƉM of 1.5 for P(IL)100. Su... Read More about Preparation of an antibacterial poly(ionic liquid) graft copolymer of hydroxyethyl cellulose.

Influence of Lipids on the Interfacial Disposition of Respiratory Syncytical Virus Matrix Protein (2011)
Journal Article
McPhee, H., Carlisle, J., Beeby, A., Money, V., Watson, M., Yeo, R., & Sanderson, J. (2011). Influence of Lipids on the Interfacial Disposition of Respiratory Syncytical Virus Matrix Protein. Langmuir, 27(1), 304-311. https://doi.org/10.1021/la104041n

The propensity of a matrix protein from an enveloped virus of the Mononegavirales family to associate with lipids representative of the viral envelope has been determined using label-free methods, including tensiometry and Brewster angle microscopy o... Read More about Influence of Lipids on the Interfacial Disposition of Respiratory Syncytical Virus Matrix Protein.

The Respiratory syncytial virus M2-1 protein forms tetramers and interacts with RNA and P in a competitive manner (2009)
Journal Article
Tran, T., Castagné, N., Dubosclard, V., Noinville, S., Koch, E., Moudjou, M., …Eléouët, J. (2009). The Respiratory syncytial virus M2-1 protein forms tetramers and interacts with RNA and P in a competitive manner. Journal of Virology, 83(13), 6363-6374. https://doi.org/10.1128/jvi.00335-09

The Respiratory Syncytial Virus (RSV) M2-1 protein is an essential cofactor of the viral RNA polymerase complex and functions as a transcriptional processivity and antitermination factor. M2-1, which exists as a phosphorylated or non-phosphorylated f... Read More about The Respiratory syncytial virus M2-1 protein forms tetramers and interacts with RNA and P in a competitive manner.

Surface features of a Mononegavirales matrix protein indicate sites of membrane interaction (2009)
Journal Article
Money, V., McPhee, H., Mosely, J., Sanderson, J., & Yeo, R. (2009). Surface features of a Mononegavirales matrix protein indicate sites of membrane interaction. Proceedings of the National Academy of Sciences, 106(11), 4441-4446. https://doi.org/10.1073/pnas.0805740106

The matrix protein (M) of respiratory syncytial virus (RSV), the prototype viral member of the Pneumovirinae (family Paramyxoviridae, order Mononegavirales), has been crystallized and the structure determined to a resolution of 1.6 A. The structure c... Read More about Surface features of a Mononegavirales matrix protein indicate sites of membrane interaction.

The 24-angstrom structure of respiratory syncytial virus nucleocapsid protein-RNA decameric rings (2007)
Journal Article
MacLellan, K., Loney, C., Yeo, R., & Bhella, D. (2007). The 24-angstrom structure of respiratory syncytial virus nucleocapsid protein-RNA decameric rings. Journal of Virology, 81(17), 9519-9524. https://doi.org/10.1128/jvi.00526-07

Respiratory syncytial virus (RSV), a nonsegmented, negative-sense RNA-containing virus, is a common cause of lower respiratory tract disease. Expression of RSV nucleocapsid protein (N) in insect cells using the baculovirus expression system leads to... Read More about The 24-angstrom structure of respiratory syncytial virus nucleocapsid protein-RNA decameric rings.

Conformational Flexibility in Recombinant Measles Virus Nucleocapsids Visualised by Cryo-negative Stain Electron Microscopy and Real-space Helical Reconstruction (2004)
Journal Article
Yeo, R., Bhella, D., & Ralph, A. (2004). Conformational Flexibility in Recombinant Measles Virus Nucleocapsids Visualised by Cryo-negative Stain Electron Microscopy and Real-space Helical Reconstruction. Journal of Molecular Biology, 340(2), 319-331. https://doi.org/10.1016/j.jmb.2004.05.015

Measles virus is a highly contagious virus that, despite the existence of an effective vaccine, is a major cause of illness and mortality worldwide. The virus has a negative-sense, single-stranded RNA genome that is encapsidated by the nucleocapsid p... Read More about Conformational Flexibility in Recombinant Measles Virus Nucleocapsids Visualised by Cryo-negative Stain Electron Microscopy and Real-space Helical Reconstruction.

Investigations into the amino-terminal domain of the respiratory syncytial virus nucleocapsid protein reveal elements important for nucleocapsid formation and interaction with the phosphoprotein (2003)
Journal Article
Murphy, L., Loney, C., Murray, J., Bhella, D., Ashton, P., & Yeo, P. (2003). Investigations into the amino-terminal domain of the respiratory syncytial virus nucleocapsid protein reveal elements important for nucleocapsid formation and interaction with the phosphoprotein. Virology, 307(1), 143-153. https://doi.org/10.1016/s0042-6822%2802%2900063-6

Bacterially expressed nucleocapsid (N) protein, from respiratory syncytial virus (RSV), was used to investigate RNA binding in a modified North–Western blotting protocol. The recombinant protein demonstrated no sequence specificity in binding RNA rep... Read More about Investigations into the amino-terminal domain of the respiratory syncytial virus nucleocapsid protein reveal elements important for nucleocapsid formation and interaction with the phosphoprotein.

Sorting of the Respiratory Syncytial Virus Matrix Protein into Detergent-Resistant Structures Is Dependent on Cell-Surface Expression of the Glycoproteins (2002)
Journal Article
Henderson, G., Murray, J., & Yeo, R. (2002). Sorting of the Respiratory Syncytial Virus Matrix Protein into Detergent-Resistant Structures Is Dependent on Cell-Surface Expression of the Glycoproteins. Virology, 300(2), 244-254. https://doi.org/10.1006/viro.2002.1540

The interaction of the respiratory syncytial virus (RSV) Matrix (M) protein with the plasma membrane was investigated using polyclonal and monoclonal antisera raised against recombinant M expressed in bacteria. M bound mainly to the plasma membrane,... Read More about Sorting of the Respiratory Syncytial Virus Matrix Protein into Detergent-Resistant Structures Is Dependent on Cell-Surface Expression of the Glycoproteins.

Characterization of Monoclonal Antibodies raised against Recombinant Respiratory Syncytial Virus Nucleocapsid (N) Protein: Identification of a Region in the Carboxy Terminus of N Involved in the Interaction with P Protein (2001)
Journal Article
Murray, J., Loney, C., Murphy, L., Graham, S., & Yeo, R. (2001). Characterization of Monoclonal Antibodies raised against Recombinant Respiratory Syncytial Virus Nucleocapsid (N) Protein: Identification of a Region in the Carboxy Terminus of N Involved in the Interaction with P Protein. Virology, 289(2), 252-261. https://doi.org/10.1006/viro.2001.1150

To investigate structure and biological properties of the nucleocapsid (N) protein of respiratory syncytial virus (RSV), we have generated a panel of 16 monoclonal antibodies, raised against recombinant N protein, and epitope mapped seven of these to... Read More about Characterization of Monoclonal Antibodies raised against Recombinant Respiratory Syncytial Virus Nucleocapsid (N) Protein: Identification of a Region in the Carboxy Terminus of N Involved in the Interaction with P Protein.