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Fructose-1,6-bisphosphate aldolase (FBA)-A conserved glycolytic enzyme with virulence functions in bacteria: 'Ill met by moonlight' (2014)
Journal Article
Shams, F., Oldfield, N. J., Wooldridge, K. G., & Turner, D. P. J. (2014). Fructose-1,6-bisphosphate aldolase (FBA)-A conserved glycolytic enzyme with virulence functions in bacteria: 'Ill met by moonlight'. Biochemical Society Transactions, 42(6), 1792-1795. https://doi.org/10.1042/BST20140203

© 2014 Biochemical Society. Moonlighting proteins constitute an intriguing class of multifunctional proteins. Metabolic enzymes and chaperones, which are often highly conserved proteins in bacteria, archaea and eukaryotic organisms, are among the mos... Read More about Fructose-1,6-bisphosphate aldolase (FBA)-A conserved glycolytic enzyme with virulence functions in bacteria: 'Ill met by moonlight'.

Deciphering the complex three-way interaction between the non-integrin laminin receptor, galectin-3 and Neisseria meningitidis (2014)
Journal Article
Alqahtani, F. Y. S., Mahdavi, J., Wheldon, L. M., Vassey, M., Pirinccioglu, N., Royer, P., …Ala'Aldeen, D. A. (2014). Deciphering the complex three-way interaction between the non-integrin laminin receptor, galectin-3 and Neisseria meningitidis. Open Biology, 4(10), Article 140053. https://doi.org/10.1098/rsob.140053

The non-integrin laminin receptor (LAMR1/RPSA) and galectin-3 (Gal-3) are multi-functional host molecules with roles in diverse pathological processes, particularly of infectious or oncogenic origins. Using bimolecular fluorescence complementation an... Read More about Deciphering the complex three-way interaction between the non-integrin laminin receptor, galectin-3 and Neisseria meningitidis.

A novel O-linked glycan modulates Campylobacter jejuni major outer membrane protein-mediated adhesion to human histo-blood group antigens and chicken colonization (2014)
Journal Article
Mahdavi, J., Pirinccioglu, N., Oldfield, N. J., Carlsohn, E., Stoof, J., Aslam, A., …Ala'Aldeen, D. A. (2014). A novel O-linked glycan modulates Campylobacter jejuni major outer membrane protein-mediated adhesion to human histo-blood group antigens and chicken colonization. Open Biology, 4(1), Article 130202. https://doi.org/10.1098/rsob.130202

Campylobacter jejuni is an important cause of human foodborne gastroenteritis; strategies to prevent infection are hampered by a poor understanding of the complex interactions between host and pathogen. Previous work showed that C. jejuni could bind... Read More about A novel O-linked glycan modulates Campylobacter jejuni major outer membrane protein-mediated adhesion to human histo-blood group antigens and chicken colonization.