References
- Bairoch, A., Boeckmann, B., Ferro, S., & Gasteiger, E. (2004). Swiss-Prot: Juggling between evolution and stability. Briefings in Bioinformatics, 5, 39–55.10.1093/bib/5.1.39
- Bebrone, C. (2007). Metallo-ß-lactamases (classification, activity, genetic, organization, structure, zinc coordination) and their superfamily. Biochemical Pharmacology, 4, 1686–1707.10.1016/j.bcp.2007.05.021
- Berman, H. M., Westbrook, Z., Feng, G., Gilliland, T. N., Bhat, T. N., Weissig, I. N., … Bourne, P. E. (2000). The protein data bank. Nucleic Acids Research, 28, 235–242.10.1093/nar/28.1.235
- Bonomo, R. A. (2017). ß-Lactamases: A focus on current challenges. Cold Spring Harbor Perspectives in Medicine, 7, a025239.
- Bush, K., & Bradford, P. A. (2016). ß-Lactams and ß-lactamase inhibitors: An overview. Cold Spring Harbor Perspectives in Medicine, 6, a025247.
- Bush, K., & Jacoby, G. A. (2010). Updated functional classification of beta-lactamases. Antimicrobial Agents and Chemotherapy, 54, 969–976.10.1128/AAC.01009-09
- Cag, Y., Caskurlu, H., Fan, Y., Cao, B., & Vahaboglu, H. (2016). Resistance mechanisms. Annals of Translational Medicine, 4, 326.10.21037/atm
- Derouaux, A., Wolf, B., Fraipont, C., Breukink, E., Nguyen-Distèche, M., & Terrak, M. (2008). The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with penicillin-binding protein 3, FtsW, and FtsN. Journal of Bacteriology, 190, 1831–1834.10.1128/JB.01377-07
- Fisher, J. F., Meroueh, S. O., & Mobashery, S. (2005). Bacterial resistance to beta-lactam antibiotics: compelling opportunism, compelling opportunity. Chemical Reviews, 105, 395–424.10.1021/cr030102i
- Frère, J. M., & Page, M. G. (2014). Penicillin-binding proteins: Evergreen drug targets. Current Opinion in Pharmacology, 18, 112–119.10.1016/j.coph.2014.09.012
- Ghuysen, J.-M. (1991). Serine β-lactamases and penicillin-binding proteins. Annual review Microbiology, 45, 37–67.10.1146/annurev.mi.45.100191.000345
- Guentzel, M. N. (1996). Escherichia, Klebsiella, Enterobacter, Serratia, Citrobacter, and Proteus. In S. Baron (Ed.), Medical Microbiology, Chapter 26 (4th ed.). Galveston (TX): University of Texas Medical Branch at Galveston. Retrieved from https://www.ncbi.nlm.nih.gov/books/NBK8035/
- Hirsh, H. L. (1948). Penicillin; a review of the basic principles and their clinical application. Medical Annals of the District of Columbia, 17, 7–20.
- Huang, B. (2009). MetaPocket: A meta approach to improve protein ligand binding site prediction. OMICS, 13, 325–330.10.1089/omi.2009.0045
- Iredell, J., Brown, J., & Tagg, K. (2016). Antibiotic resistance in Enterobacteriaceae: Mechanisms and clinical implications. British Medical Journal, 352, h6420.10.1136/bmj.h6420
- Krissinel, E., & Henrick, K. (2004). Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta crystallographica, D60, 2256–2268.
- Leinonen, R., Diez, F. G., Binns, D., Fleischmann, W., Lopez, R., & Apweiler, R. (2004). UniProt archive. Bioinformatics, 20, 3236–3237.10.1093/bioinformatics/bth191
- Livermore, D. M. (2009). Has the era of untreatable infections arrived? Journal of Antimicrobial Chemotherapy, 64(Suppl 1), 29–36.10.1093/jac/dkp255
- Page, M. G. P., & Bush, K. (2014). Discovery and development of new antibacterial agents targeting Gram-negative bacteria in the era of pandrug resistance: Is the future promising? Current Opinion in Pharmacology, 18, 91–97.10.1016/j.coph.2014.09.008
- Pfeifle, D., Janas, E., & Wiedeman, B. (2000). Role of penicillin-binding proteins in the initiation of the AmpC β-lactamase expression in Enterobacter cloacae. Antimicrobial Agents and Chemotherapy, 44, 169–172.10.1128/AAC.44.1.169-172.2000
- Pratt, R. F. (2016). β-Lactamases: Why and How. Journal of Medicinal Chemistry, 2016(59), 8207–8220.10.1021/acs.jmedchem.6b00448
- Qin, W., Panunzio, M., & Biondi, S. (2014). β-lactam antibiotics renaissance. Antibiotics, 3, 193–215.10.3390/antibiotics3020193
- Ruggiero, M., Curto, L., Brunetti, F., Sauvage, E., Galleni, M., Power, P., Gutkind, G. (2017). Impact of mutations at Arg220 and Thr237 in PER-2 β-lactamase on conformation, activity, and susceptibility to inhibitors. Antimicrobial Agents and Chemotherapy, 61, e02193-16.
- Sauvage, E., Kerff, F., Terrak, M., Ayala, J. A., & Charlier, P. (2008). The penicillin-binding proteins: Structure and role in peptidoglycan biosynthesis. FEMS Microbiology Reviews, 32, 234–258.10.1111/j.1574-6976.2008.00105.x
- Sievers, F., & Higgins, D. G. (2014). Clustal omega. Current Protocols in Bioinformatics, 48, 3.13.1–3.13.16.10.1002/0471250953.bi0313s48
- Van Boeckel, T. P., Gandra, S., Ashok, A., Caudron, Q., Grenfell, B. T., & Levin, S. A., Laxminarayan R (2014). Global antibiotic consumption 2000−2010: An analysis of national pharmaceutical sales data. Lancet Infectious Diseases, 14, 742–750.10.1016/S1473-3099(14)70780-7
- Wise, E. M., & Park, J. T. (1965). Penicillin: Its basic site of action as an inhibitor of a peptide cross-linking reaction in cell wall mucopeptide synthesis. Proceedings of the National Academy of Sciences U.S.A., 54, 75−81.10.1073/pnas.54.1.75
- Zhang, Z., Li, Y., Lin, B., Schroeder, M., & Huang, B. (2011). Identification of cavities on protein surface using multiple computational approaches for drug binding site prediction. Bioinformatics, 27, 2083–2088.10.1093/bioinformatics/btr331