All Outputs (23)

Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins (2016)
Journal Article
Jenner, M., Afonso, J. P., Kohlhaas, C., Karbaum, P., Frank, S., Piel, J., & Oldham, N. J. (in press). Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins. Chemical Communications, 52(30), https://doi.org/10.1039/C6CC01453D

Acyl hydrolase (AH) domains are a common feature of trans-AT PKSs. They have been hypothesised to perform a proofreading function by removing acyl chains from stalled sites. This study determines the substrate tolerance of the AH PedC for a range of... Read More about Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins.

Genomic analysis of serogroup Y Neisseria meningitidis isolates reveals extensive similarities between carriage and disease-associated organisms (2016)
Journal Article
Oldfield, N. J., Harrison, O. B., Bayliss, C. D., Maiden, M. C., Ala'Aldeen, D. A., & Turner, D. P. (2016). Genomic analysis of serogroup Y Neisseria meningitidis isolates reveals extensive similarities between carriage and disease-associated organisms. Journal of Infectious Diseases, 213(11), 1777-1785. https://doi.org/10.1093/infdis/jiw008

Background. Neisseria meningitidis is a frequent colonizer of the human nasopharynx with asymptomatic carriage providing the reservoir for invasive, disease-causing strains. Serogroup Y (MenY) strains are a major cause of meningococcal disease. High... Read More about Genomic analysis of serogroup Y Neisseria meningitidis isolates reveals extensive similarities between carriage and disease-associated organisms.

Ion mobility-mass spectrometry reveals conformational flexibility in the deubiquitinating enzyme USP5 (2015)
Journal Article
Scott, D., Layfield, R., & Oldham, N. J. (2015). Ion mobility-mass spectrometry reveals conformational flexibility in the deubiquitinating enzyme USP5. Proteomics, 15(16), https://doi.org/10.1002/pmic.201400457

Many proteins exhibit conformation flexibility as part of their biological function, whether through the presence of a series of well-defined states or by the existence of intrinsic disorder. Ion mobility spectrometry, in combination with MS (IM–MS),... Read More about Ion mobility-mass spectrometry reveals conformational flexibility in the deubiquitinating enzyme USP5.