| Title | Structure and inhibition of N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus |
| Publication Type | Journal Article |
| Year of Publication | 2016 |
| Authors | North, R.A., Watson A.J.A., Pearce F.G., Muscroft-Taylor A.C., Friemann R., Fairbanks A.J., and Dobson R.C.J. |
| Journal | FEBS Letters |
| Volume | 590 |
| Issue | 23 |
| Pagination | 4414 - 4428 |
| Date Published | 2016 |
| ISSN | 00145793 (ISSN) |
| Keywords | amino acid sequence, antagonists and inhibitors, bacterial strain, binding affinity, chemistry, Clostridium botulinum, Clostridium perfringens, crystal structure, diastereoisomer, enzyme active site, enzyme inhibition, enzyme inhibitor, Enzyme Inhibitors, enzyme kinetics, enzyme structure, enzyme substrate, enzyme synthesis, enzymology, Escherichia coli, Gemella haemolysans, Haemophilus influenzae, human, Humans, Kinetics, letter, lyase, metabolism, methicillin resistant Staphylococcus aureus, Methicillin-Resistant Staphylococcus aureus, Models, Molecular, molecular model, Molecular weight, n acetylneuraminate lyase, n acetylneuraminic acid, N-acetylneuraminate lyase, N-acetylneuraminic acid, nonhuman, Oxo-Acid-Lyases, Pasteurella multocida, priority journal, protein quaternary structure, Protein Structure, Quaternary, sialic acid, species difference, Species Specificity, Staphylococcus aureus, structure analysis, unclassified drug |
| URL | https://www.scopus.com/inward/record.uri?eid=2-s2.0-84997815909&doi=10.1002%2f1873-3468.12462&partnerID=40&md5=5cb981a609e8c2045e90bfe24cafe71e |
| DOI | 10.1002/1873-3468.12462 |
