The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.
Penicillin‐binding protein 2a of methicillin‐resistant Staphylococcus aureus
Open accessAbstract
High‐level resistance to β‐lactam antibiotics in methicillin‐resistant Staphylococcus aureus (MRSA) is due to expression of penicillin‐binding protein 2a (PBP2a), a transpeptidase that catalyzes cell‐wall crosslinking in the face of the challenge by β‐lactam antibiotics. The activity of this protein is regulated by allostery at a site 60 Å distant from the active site, where crosslinking of cell wall takes place. This review discusses the state of knowledge on this important enzyme of cell‐wall biosynthesis in MRSA. © 2014 IUBMB Life, 66(8):572–577, 2014
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Cites
Methicillin-resistant Staphylococcus aureus clinical strain with reduced vancomycin susceptibility
Hiramatsu, K. (1997) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/40.1.135 · Cited by 1,984
Dundas, J., Ouyang, Z., Tseng, J., Binkowski, A., Turpaz, Y., & Liang, J. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl282 · Cited by 1,725
"Celbenin" - resistant Staphylococci
Jevons, M. P. (1961) · BMJ · doi:10.1136/bmj.1.5219.124-a · Cited by 1,680
Antimicrobial resistance: the example of Staphylococcus aureus
Lowy, F. D. (2003) · Journal of Clinical Investigation · doi:10.1172/jci18535 · Cited by 1,445
The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis
Sauvage, E., Kerff, F., Terrak, M., Ayala, J. A., & Charlier, P. (2008) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2008.00105.x · Cited by 1,317
Infection with Vancomycin-Resistant Staphylococcus aureus Containing the vanA Resistance Gene
Chang, S., Sievert, D. M., Hageman, J. C., Boulton, M. L., Tenover, F. C., Downes, F. P., Shah, S., Rudrik, J. T., Pupp, G. R., Brown, W. J., et al. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa025025 · Cited by 1,095
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“This supports the Tipper–Strominger hypothesis (14) that ceftaroline is recognized not only at the active site but also at a second site as a result of the similarity of its core structure to the peptidoglycan peptide stem.”
BackgroundProtein states and proteinquakes.
Ansari, A., Berendzen, J., Bowne, S. F., Frauenfelder, H., Iben, I. E., Sauke, T. B., Shyamsunder, E., & Young, R. D. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.15.5000 · Cited by 828
Intrinsic antibiotic resistance: Mechanisms, origins, challenges and solutions
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Allosteric regulation and catalysis emerge via a common route
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Cited by
Papadopoulos, P., Papadopoulos, T., Angelidis, A. S., Kotzamanidis, C., Zdragas, A., Papa, A., Filioussis, G., & Sergelidis, D. (2019) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2018.11.007 · Cited by 54
Metadata
- Authors
- Fishovitz, J., Hermoso, J. A., Chang, M., & Mobashery, S.
- Venue
- IUBMB Life
- Publisher
- Wiley
- Published
- 2014-07-14
- Volume
- 66
- Issue
- 8
- Pages
- 572-577
- ISSN
- 1521-6543 (ISSN-L)
- 1521-6551
- OpenAlex
- W1926375223
- Cited by
- 279
- References
- 51
- FWCI
- 5.19
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
