The DOI matches its Crossref record; 68 of the 68 references it cites were found in a registry or an index.
The Growing Genetic and Functional Diversity of Extended Spectrum Beta-Lactamases
Open accessAbstract
The β-lactams—a large class of diverse compounds—due to their excellent safety profile and broad antimicrobial spectrum are considered to be the most widely used therapeutic class of antibacterials prescribed in human and veterinary clinical practices. This, unfortunately, has also given rise to a continuous increased resistance globally in health care settings as well as in the community due to their permanent selective force driving diversification of the resistance mechanism. Resistance against β-lactams is increasing rapidly as novel β-lactamases, enzymes that degrade β-lactams, are being discovered each day such as recent emergence of extended spectrum β-lactamases (ESBL) that have the ability to inactivate most of the cephalosporins. The complexity and diversity of ESBL are increasing so rapidly that more than 170 variants have thus far been described for only a single genotype, theblaCTX-M-encoding ESBL. This review is to organize all the current updated literature describing genomic features, organization, and mechanism of resistance and mode of dissemination of all known ESBLs.
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Cites
Host–microbe interactions have shaped the genetic architecture of inflammatory bowel disease
The International IBD Genetics Consortium (IIBDGC), Jostins, L., Ripke, S., Weersma, R. K., Duerr, R. H., McGovern, D. P., Hui, K. Y., Lee, J. C., Philip Schumm, L., Sharma, Y., et al. (2012) · Nature · doi:10.1038/nature11582 · Cited by 4,722
Updated Functional Classification of β-Lactamases
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Jacoby, G. A. (2009) · Clinical Microbiology Reviews · doi:10.1128/cmr.00036-08 · Cited by 2,165
Outer membrane permeability and antibiotic resistance
Delcour, A. H. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2008.11.005 · Cited by 1,762
An Enzyme from Bacteria able to Destroy Penicillin
ABRAHAM, E. P., & CHAIN, E. (1940) · Nature · doi:10.1038/146837a0 · Cited by 1,333
The CTX-M β-lactamase pandemic
Cantón, R., & Coque, T. M. (2006) · Current Opinion in Microbiology · doi:10.1016/j.mib.2006.08.011 · Cited by 1,147
Integrons: agents of bacterial evolution
Mazel, D. (2006) · Nature Reviews Microbiology · doi:10.1038/nrmicro1462 · Cited by 1,107
A standard numbering scheme for the class A β-lactamases
Ambler, R. P., Coulson, A. F. W., Frère, J. M., Ghuysen, J. M., Joris, B., Forsman, M., Levesque, R. C., Tiraby, G., & Waley, S. G. (1991) · Biochemical Journal · doi:10.1042/bj2760269 · Cited by 1,073
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Cited by
Molecular mechanisms of antibiotic resistance revisited
Darby, E. M., Trampari, E., Siasat, P., Gaya, M. S., Alav, I., Webber, M. A., & Blair, J. M. A. (2023) · Nature Reviews Microbiology · doi:10.1038/s41579-022-00820-y · Cited by 1,398
Exploring phytochemicals for combating antibiotic resistance in microbial pathogens
Khare, T., Anand, U., Dey, A., Assaraf, Y. G., Chen, Z.-S., Liu, Z., & Kumar, V. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.720726 · Cited by 281
“The Plectranthus amboinicus EOs also displayed striking biofilm inhibitory activities against antibiotic resistant S. aureus (Vasconcelos et al., 2017).”
Background
Metadata
- Authors
- ur Rahman, S., Ali, T., Ali, I., Khan, N. A., Han, B., & Gao, J.
- Venue
- BioMed Research International
- Publisher
- Wiley
- Published
- 2018
- Volume
- 2018
- Pages
- 1-14
- ISSN
- 1110-7243 (ISSN-L)
- 2314-6133
- 2314-6141
- OpenAlex
- W2789345104
- Cited by
- 283
- References
- 68
- FWCI
- 11.70
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- ur Rahman, S., Ali, T., Ali, I., Khan, N. A., Han, B., & Gao, J. (2018). The Growing Genetic and Functional Diversity of Extended Spectrum Beta-Lactamases. BioMed Research International. https://doi.org/10.1155/2018/9519718
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
