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Profile of Enterobacteria Resistant to Beta-Lactams

Santos, A. L., dos Santos, A. P., Ito, C. R. M., de Queiroz, P. H. P., de Almeida, J. A., Júnior, M. A. B. D. C., de Oliveira, C. Z., Avelino, M. A. G., Wastowski, I. J., Gomes, G. P. L. A., et al. (2020) · Antibiotics · doi:10.3390/antibiotics9070410 · Cited by 34 · see citing works

Diversity and Global Distribution of IncL/M Plasmids Enabling Horizontal Dissemination ofβ-Lactam Resistance Genes among the Enterobacteriaceae

Adamczuk, M., Zaleski, P., Dziewit, Ł., Wolinowska, R., Nieckarz, M., Wawrzyniak, P., Kierył, P., Płucienniczak, A., & Bartosik, D. (2015) · BioMed Research International · doi:10.1155/2015/414681 · Cited by 31 · see citing works

Punica granatum sarcotesta lectin (PgTeL) has antibacterial activity and synergistic effects with antibiotics against β-lactamase-producing Escherichia coli

da Silva, P. M., da Silva, B. R., Silva, J. N. D. O., de Moura, M. C., Soares, T., Feitosa, A. P. S., Brayner, F. A., Alves, L. C., Paiva, P. M. G., Damborg, P., et al. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.06.011 · Cited by 30 · see citing works

Microspectrofluorimetry to dissect the permeation of ceftazidime in Gram-negative bacteria

Allam, A., Maigre, L., Vergalli, J., Dumont, E., Cinquin, B. P., de Sousa, R. A., Pajović, J. D., Pinet, E., Smith, N., Herbeuval, J., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-00945-8 · Cited by 29 · see citing works

Inhibitors of β-Lactamases. New Life of β-Lactam Antibiotics

Egorov, A. M., Ulyashova, M. M., & Rubtsova, M. Y. (2020) · Biochemistry (Moscow) · doi:10.1134/s0006297920110024 · Cited by 28 · see citing works

β-Lactamase diversity in Pseudomonas aeruginosa

Mack, A. R., Hujer, A. M., Mojica, M. F., Taracila, M. A., Feldgarden, M., Haft, D. H., Klimke, W. A., Prasad, A. B., & Bonomo, R. A. (2025) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00785-24 · Cited by 27 · see citing works

Emerging antibiotic resistance by various novel proteins/enzymes

Sun, S. (2025) · European Journal of Clinical Microbiology & Infectious Diseases · doi:10.1007/s10096-025-05126-4 · Cited by 32 · see citing works

Optimization of 1,2,4-Triazole-3-thiones toward Broad-Spectrum Metallo-β-lactamase Inhibitors Showing Potent Synergistic Activity on VIM- and NDM-1-Producing Clinical Isolates

Legru, A., Verdirosa, F., Vo‐Hoang, Y., Tassone, G., Vascon, F., Thomas, C. A., Sannio, F., Corsica, G., Benvenuti, M., Feller, G., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01257 · Cited by 27 · see citing works

Structure, function, and evolution of metallo-β-lactamases from the B3 subgroup—emerging targets to combat antibiotic resistance

Krco, S., Davis, S. J., Joshi, P., Wilson, L. A., Pedroso, M. M., Douw, A., Schofield, C. J., Hugenholtz, P., Schenk, G., & Morris, M. T. (2023) · Frontiers in Chemistry · doi:10.3389/fchem.2023.1196073 · Cited by 26 · see citing works

Structure, activity and thermostability investigations of OXA-163, OXA-181 and OXA-245 using biochemical analysis, crystal structures and differential scanning calorimetry analysis

Lund, B. A., Thomassen, A. M., Carlsen, T. J. O., & Leiros, H. S. (2017) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x17013838 · Cited by 25 · see citing works

Origin, Diversity, and Multiple Roles of Enzymes with Metallo-β-Lactamase Fold from Different Organisms

Diene, S., Pontarotti, P., Azza, S., Armstrong, N., Pinault, L., Chabrière, E., Colson, P., Rolain, J., & Raoult, D. (2023) · Cells · doi:10.3390/cells12131752 · Cited by 21 · see citing works

Susceptibility of Ocular Staphylococcus aureus to Antibiotics and Multipurpose Disinfecting Solutions

Afzal, M., Vijay, A. K., Stapleton, F. J., & Willcox, M. D. P. (2021) · Antibiotics · doi:10.3390/antibiotics10101203 · Cited by 27 · see citing works

Pharmacokinetics of Non-β-Lactam β-Lactamase Inhibitors

Luci, G., Mattioli, F., Falcone, M., & Paolo, A. D. (2021) · Antibiotics · doi:10.3390/antibiotics10070769 · Cited by 24 · see citing works

Methicillin Resistant Staphylococcus aureus and Extended Spectrum Beta-lactamase Producing Enterobacteriaceae: A Therapeutic Challenge in the 21st Century

Donkor, E. S., & Codjoe, F. S. (2019) · The Open Microbiology Journal · doi:10.2174/1874285801913010094 · Cited by 22 · see citing works

Characterisation of extended-spectrum β-lactamase and AmpC β-lactamase-producing Enterobacteriaceae isolated from companion animals in New Zealand

Karkaba, A., Grinberg, A., Benschop, J., & Pleydell, E. J. (2016) · New Zealand Veterinary Journal · doi:10.1080/00480169.2016.1271730 · Cited by 23 · see citing works

Classification for β-lactamases: historical perspectives

Bush, K. (2023) · Expert Review of Anti-infective Therapy · doi:10.1080/14787210.2023.2194633 · Cited by 43 · see citing works

Updated Functional Classification of β-Lactamases

Bush, K., & Jacoby, G. A. (2010) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01009-09 · Cited by 2,367 · see citing works

A functional classification scheme for beta-lactamases and its correlation with molecular structure

Bush, K., Jacoby, G. A., & Medeiros, A. A. (1995) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.39.6.1211 · Cited by 2,485 · see citing works

Comment on: Redefining extended-spectrum -lactamases: balancing science and clinical need

Bush, K., Jacoby, G. A., Amicosante, G., Bonomo, R. A., Bradford, P. A., Cornaglia, G., Garau, J., Giamarellou, H., Jarlier, V., Martı́nez-Martı́nez, L., et al. (2009) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkp104 · Cited by 21 · see citing works

Updated Functional Classification of -Lactamases

Bush, K., & Jacoby, G. A. (2016)