All Outputs (2)

The role of glyceraldehyde 3-phosphate dehydrogenase (GapA-1) in Neisseria meningitidis adherence to human cells (2010)
Journal Article
Tunio, S. A., Oldfield, N. J., Ala'Aldeen, D. A. A., Wooldridge, K. G., & Turner, D. P. J. (2010). The role of glyceraldehyde 3-phosphate dehydrogenase (GapA-1) in Neisseria meningitidis adherence to human cells. BMC Microbiology, 10, Article 280. https://doi.org/10.1186/1471-2180-10-280

Background Glyceraldehyde 3-phosphate dehydrogenases (GAPDHs) are cytoplasmic glycolytic enzymes, which although lacking identifiable secretion signals, have also been found localized to the surface of several bacteria (and some eukaryotic organisms... Read More about The role of glyceraldehyde 3-phosphate dehydrogenase (GapA-1) in Neisseria meningitidis adherence to human cells.

The moonlighting protein fructose-1, 6-bisphosphate aldolase of Neisseria meningitidis: Surface localization and role in host cell adhesion (2010)
Journal Article
Tunio, S. A., Oldfield, N. J., Berry, A., Ala'Aldeen, D. A. A., Wooldridge, K. G., & Turner, D. P. J. (2010). The moonlighting protein fructose-1, 6-bisphosphate aldolase of Neisseria meningitidis: Surface localization and role in host cell adhesion. Molecular Microbiology, 76(3), 605-615. https://doi.org/10.1111/j.1365-2958.2010.07098.x

Fructose-1, 6-bisphosphate aldolases (FBA) are cytoplasmic glycolytic enzymes, which despite lacking identifiable secretion signals, have also been found localized to the surface of several bacteria where they bind host molecules and exhibit non-glyc... Read More about The moonlighting protein fructose-1, 6-bisphosphate aldolase of Neisseria meningitidis: Surface localization and role in host cell adhesion.