Three Decades of β-Lactamase Inhibitors

Extended-Spectrum β-Lactamases: a Clinical Update

Paterson, D. L., & Bonomo, R. A. (2005) · Clinical Microbiology Reviews · doi:10.1128/cmr.18.4.657-686.2005 · Cited by 3,495

Extended-Spectrum β-Lactamases in the 21st Century: Characterization, Epidemiology, and Detection of This Important Resistance Threat

Bradford, P. A. (2001) · Clinical Microbiology Reviews · doi:10.1128/cmr.14.4.933-951.2001 · Cited by 2,646

Carbapenemases: the Versatile β-Lactamases

Queenan, A. M., & Bush, K. (2007) · Clinical Microbiology Reviews · doi:10.1128/cmr.00001-07 · Cited by 2,609

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

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

Federal Funding for the Study of Antimicrobial Resistance in Nosocomial Pathogens: No ESKAPE

Rice, L. B. (2008) · The Journal of Infectious Diseases · doi:10.1086/533452 · Cited by 2,328

AmpC β-Lactamases

Jacoby, G. A. (2009) · Clinical Microbiology Reviews · doi:10.1128/cmr.00036-08 · Cited by 2,277

Extended-spectrum β-lactamase-producing Enterobacteriaceae: an emerging public-health concern

Pitout, J. D. D., & Laupland, K. B. (2008) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(08)70041-0 · Cited by 2,068

The real threat of Klebsiella pneumoniae carbapenemase-producing bacteria

Nordmann, P., Cuzon, G., & Naas, T. (2009) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(09)70054-4 · Cited by 1,619

Prevention of Drug Access to Bacterial Targets: Permeability Barriers and Active Efflux

Nikaido, H. (1994) · Science · doi:10.1126/science.8153625 · Cited by 1,542

Efflux Pump (QacA, QacB, and QacC) and β-Lactamase Inhibitors? An Evaluation of 1,8-Naphthyridines against Staphylococcus aureus Strains

Oliveira–Tintino, C. D. D. M., Tintino, S. R., de Araújo, A. C. J., Barbosa, C. R. D. S., Freitas, P. R., Neto, J. B. D. A., Begnini, I. M., Rebelo, R. A., da Silva, L. E., Mireski, S. L., et al. (2023) · Molecules · doi:10.3390/molecules28041819 · Cited by 21

Molecular identification and antibiotic resistant bacteria isolated from primary dentition infections

Loyola-Rodríguez, J. P., Garcia-Cortés, J., Martínez-Martínez, R. E., Patiño‐Marín, N., Martínez-Castañón, G. A., Zavala-Alonso, N., & Amano, A. (2014) · Australian Dental Journal · doi:10.1111/adj.12213 · Cited by 21

Increased Structural Flexibility at the Active Site of a Fluorophore-conjugated β-Lactamase Distinctively Impacts Its Binding toward Diverse Cephalosporin Antibiotics

Wong, W., Chan, K.-C., So, P., Yap, H.-K., Chung, W. H., Leung, Y.-C., Wong, K., & Zhao, Y. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.198895 · Cited by 21

Resistance to the Third-Generation Cephalosporin Ceftazidime by a Deacylation-Deficient Mutant of the TEM β-Lactamase by the Uncommon Covalent-Trapping Mechanism

Antunes, N. T., Frase, H., Tóth, M., Mobashery, S., & Vakulenko, S. B. (2011) · Biochemistry · doi:10.1021/bi200403e · Cited by 21

Exploring the Landscape of Diazabicyclooctane (DBO) Inhibition: Avibactam Inactivation of PER-2 β-Lactamase

Ruggiero, M., Papp‐Wallace, K. M., Taracila, M. A., Mojica, M. F., Bethel, C. R., Rudin, S. D., Zeiser, E. T., Gutkind, G., Bonomo, R. A., & Power, P. P. (2017) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02476-16 · Cited by 21

Discovery of 1‐Hydroxypyridine‐2(1H)‐thione‐6‐carboxylic Acid as a First‐in‐Class Low‐Cytotoxic Nanomolar Metallo β‐Lactamase Inhibitor

Shin, W. S., Bergström, A., Bonomo, R. A., Crowder, M. W., Muthyala, R., & Sham, Y. Y. (2017) · ChemMedChem · doi:10.1002/cmdc.201700182 · Cited by 21

PNGM-1, a novel subclass B3 metallo-β-lactamase from a deep-sea sediment metagenome

Park, K. S., Kim, T. Y., Kim, J. H., Lee, J. H., Jeon, J. H., Karim, A. M., Malik, S. K., & Lee, S. H. (2018) · Journal of Global Antimicrobial Resistance · doi:10.1016/j.jgar.2018.05.021 · Cited by 21

Multiscale Simulations of Clavulanate Inhibition Identify the Reactive Complex in Class A β-Lactamases and Predict the Efficiency of Inhibition

Fritz, R. A., Alzate‐Morales, J. H., SPENCER, J. M., Mulholland, A. J., & van der Kamp, M. W. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00480 · Cited by 20

H2depda: An acyclic adjuvant potentiates meropenem activity in vitro against metallo-β-lactamase-producing enterobacterales

Shi, X., Wang, M., Huang, S.-C., Han, J., Chu, W.-C., Xiao, C., Zhang, E., & Qin, S. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.01.083 · Cited by 21

Pharmacokinetics-pharmacodynamics of β-lactamase inhibitors: are we missing the target?

Monogue, M. L., & Nicolau, D. P. (2019) · Expert Review of Anti-infective Therapy · doi:10.1080/14787210.2019.1647781 · Cited by 21

Multicenter Evaluation of the New Etest Gradient Diffusion Method for Piperacillin-Tazobactam Susceptibility Testing of Enterobacterales , Pseudomonas aeruginosa , and Acinetobacter baumannii Complex

Fernández, S. G., Bala, Y., Armstrong, T., García-Castillo, M., Burnham, C. D., Wallace, M. A., Hardy, D. J., Zambardi, G., & Cantón, R. (2019) · Journal of Clinical Microbiology · doi:10.1128/jcm.01042-19 · Cited by 21

Contribution of β-lactamase and efflux pump overproduction to tazobactam-piperacillin resistance in clinical isolates of Escherichia coli

Suzuki, Y., Sato, T., Fukushima, Y., Nakajima, C., Suzuki, Y., Takahashi, S., & Yokota, S. (2020) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2020.105919 · Cited by 21

Structure and Molecular Recognition Mechanism of IMP-13 Metallo-β-Lactamase

Softley, C. A., Żak, K. M., Bostock, M. J., Fino, R., Zhou, R. X., Kolonko, M., Mejdi-Nitiu, R., Meyer, H., Sattler, M., & Popowicz, G. M. (2020) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00123-20 · Cited by 21

A drug-resistant β-lactamase variant changes the conformation of its active-site proton shuttle to alter substrate specificity and inhibitor potency

Soeung, V., Lu, S., Hu, L., Judge, A., Sankaran, B., Prasad, B. V. V., & Palzkill, T. G. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.016103 · Cited by 21

Zinc Finger Nuclease: A New Approach to Overcome Beta-Lactam Antibiotic Resistance

Dastjerdeh, M. S., Kouhpayeh, S., Sabzehei, F., Khanahmad, H., Salehi, M., Mohammadi, Z., Shariati, L., Hejazi, Z., Rabiei, P., & Manian, M. (2016) · Jundishapur Journal of Microbiology · doi:10.5812/jjm.29384 · Cited by 21

Management of Severe Infections

Pérez, F., Chakhtoura, N. G. E., & Bonomo, R. A. (2025) · Medical Clinics of North America · doi:10.1016/j.mcna.2025.01.003 · Cited by 20

In Vitro Activity of Ceftolozane Alone and in Combination with Tazobactam against Extended-Spectrum-β-Lactamase-Harboring Enterobacteriaceae

Melchers, M. J. B., van Mil, A. C. H. A. M., & Mouton, J. W. (2015) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.04498-14 · Cited by 20

Optimization of amino acid thioesters as inhibitors of metallo-β-lactamase L1

Liu, X., Yang, K., Zhang, Y., Ge, Y., Yang, X., Chang, Y., & Oelschlaeger, P. (2016) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2016.08.048 · Cited by 20

Structural Investigations of the Inhibition of Escherichia coli AmpC β-Lactamase by Diazabicyclooctanes

Lang, P. A., Leissing, T. M., Page, M. G. P., Schofield, C. J., & Brem, J. (2020) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02073-20 · Cited by 24

Evolutionary Trajectories toward High-Level β-Lactam/β-Lactamase Inhibitor Resistance in the Presence of Multiple β-Lactamases

Rajer, F., Allander, L., Karlsson, P. A., & Sandegren, L. (2022) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00290-22 · Cited by 20

Syntheses and studies of new forms of N-sulfonyloxy β-lactams as potential antibacterial agents and β-lactamase inhibitors

Carosso, S., & Miller, M. J. (2015) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2015.08.005 · Cited by 20

Biosensors for the detection of antibiotic residues in milk

Kivirand, K., Kagan, M., & Rinken, T. (2015) · InTech eBooks · doi:10.5772/60464 · Cited by 20

Application of cyclic phosphonamide reagents in the total synthesis of natural products and biologically active molecules

Focken, T., & Hanessian, S. (2014) · Beilstein Journal of Organic Chemistry · doi:10.3762/bjoc.10.195 · Cited by 20

No Outbreak of Vancomycin and Linezolid Resistance in Staphylococcal Pneumonia over a 10-Year Period

Yayan, J., Ghebremedhin, B., & Rasche, K. (2015) · PLoS ONE · doi:10.1371/journal.pone.0138895 · Cited by 20

An Efficient Computational Assay for β-Lactam Antibiotic Breakdown by Class A β-Lactamases

Hirvonen, V. H. A., Hammond, K., Chudyk, E. I., Limb, M. A. L., SPENCER, J. M., Mulholland, A. J., & van der Kamp, M. W. (2019) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.9b00442 · Cited by 22

Insight into the screening of potential beta-lactamase inhibitors as anti-bacterial chemical agents through pharmacoinformatics study

Parida, P. K., Bhowmick, S., Saha, A., & Islam, M. A. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1720819 · Cited by 20

Ceftazidime-avibactam: new rules for the game against multidrug-resistant gram-negative bacteria

Kozlov, R. S., Stetsiouk, О. U., & Andreeva, I. V. (2018) · Clinical Microbiology and Antimicrobial Chemotherapy · doi:10.36488/cmac.2018.1.24-34 · Cited by 20

Insect—Symbiont Gene Expression in the Midgut Bacteriocytes of a Blood-Sucking Parasite

Husník, F., Hypša, V., & Darby, A. C. (2020) · Genome Biology and Evolution · doi:10.1093/gbe/evaa032 · Cited by 20

Unraveling the energetic significance of chemical events in enzyme catalysis via machine-learning based regression approach

Song, Z., Zhou, H.-Y., Tian, H., Wang, X., & Tao, P. (2020) · Communications Chemistry · doi:10.1038/s42004-020-00379-w · Cited by 20

Boronic Acids as Prospective Inhibitors of Metallo-β-Lactamases: Efficient Chemical Reaction in the Enzymatic Active Site Revealed by Molecular Modeling

Krivitskaya, A. V., & Khrenova, M. G. (2021) · Molecules · doi:10.3390/molecules26072026 · Cited by 20

The β-lactamase inhibitor avibactam (NXL104) does not induce ampC β -lactamase in Enterobacter cloacae

Miossec, C., Claudon, M., Levasseur, P., & Black, M. (2013) · Infection and Drug Resistance · doi:10.2147/idr.s53874 · Cited by 20

Use of ferrous iron by metallo-β-lactamases

Cahill, S. T., Tarhonskaya, H., Rydzik, A. M., Flashman, E., McDonough, M. A., Schofield, C. J., & Brem, J. (2016) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2016.07.013 · Cited by 21

Clinical efficacy, safety and pharmacokinetics of novel β-lactam/β-lactamase inhibitor combinations: a systematic review

Alarcia-Lacalle, A., Canut, A., Solinís, M. Á., Isla, A., & Rodríguez‐Gascón, A. (2025) · JAC-Antimicrobial Resistance · doi:10.1093/jacamr/dlaf096 · Cited by 26

Kinetic Characterization of Fragment Binding in AmpC β-Lactamase by High-Throughput Molecular Simulations

Bisignano, P., Doerr, S., Harvey, M. J., Favia, A. D., Cavalli, A., & Fabritiis, G. D. (2014) · Journal of Chemical Information and Modeling · doi:10.1021/ci4006063 · Cited by 19

Dithiocarbamate as a Valuable Scaffold for the Inhibition of Metallo-β-Lactmases

Ge, Y., Xu, L.-W., Liu, Y., Sun, L.-Y., Gao, H., Li, J., & Yang, K. (2019) · Biomolecules · doi:10.3390/biom9110699 · Cited by 19

FT-IR/ATR Solid Film Formation: Qualitative and Quantitative Analysis of a Piperacillin-Tazobactam Formulation

Chrisikou, I., Orkoula, M. G., & Kontoyannis, C. G. (2020) · Molecules · doi:10.3390/molecules25246051 · Cited by 19

Iron-Zinc Co-Doped Titania Nanocomposite: Photocatalytic and Photobiocidal Potential in Combination with Molecular Docking Studies

Riaz, N., Chia, D. A. S. F., Khan, M. S., Naz, S., Sarwar, R., Farooq, U., Bustam, M. A., Batiha, G. E., Azab, I. H. E., Uddin, J., et al. (2021) · Catalysts · doi:10.3390/catal11091112 · Cited by 19

C6 Hydroxymethyl-Substituted Carbapenem MA-1-206 Inhibits the Major Acinetobacter baumannii Carbapenemase OXA-23 by Impeding Deacylation

Stewart, N. K., Tóth, M., Alqurafi, M. A., Chai, W., Nguyen, T., Quan, P., Lee, M., Buynak, J. D., Smith, C. A., & Vakulenko, S. B. (2022) · mBio · doi:10.1128/mbio.00367-22 · Cited by 19

Penicillanic Acid Sulfones Inactivate the Extended-Spectrum β-Lactamase CTX-M-15 through Formation of a Serine-Lysine Cross-Link: an Alternative Mechanism of β-Lactamase Inhibition

Hinchliffe, P., Tooke, C. L., Bethel, C. R., Wang, B., Arthur, C. J., Heesom, K. J., Shapiro, S., Schlatzer, D., Papp‐Wallace, K. M., Bonomo, R. A., et al. (2022) · mBio · doi:10.1128/mbio.01793-21 · Cited by 19

A review on the mechanistic details of OXA enzymes of ESKAPE pathogens

Avcı, F. G., Taştekil, I., Jaisi, A., Özbek, P., & Akbulut, B. S. (2022) · Pathogens and Global Health · doi:10.1080/20477724.2022.2088496 · Cited by 19

The role of adjuvants in overcoming antibacterial resistance due to enzymatic drug modification

El-Khoury, C., Mansour, E., Yuliandra, Y., Lai, F., Hawkins, B. A., Du, J. J., Sundberg, E. J., Sluis‐Cremer, N., Hibbs, D. E., & Groundwater, P. W. (2022) · RSC Medicinal Chemistry · doi:10.1039/d2md00263a · Cited by 19

Resistance to aztreonam-avibactam due to a mutation of SHV-12 in Enterobacter

Wu, S., Ma, K., Feng, Y., & Zong, Z. (2023) · Annals of Clinical Microbiology and Antimicrobials · doi:10.1186/s12941-023-00605-y · Cited by 19

Repurposing Amphotericin B: anti-microbial, molecular docking and molecular dynamics simulation studies suggest inhibition potential of Amphotericin B against MRSA

Farid, N., Bux, K., Ali, K., Bashir, A., & Tahir, R. (2023) · BMC Chemistry · doi:10.1186/s13065-023-00980-9 · Cited by 19

Enzyme activity measurement via spectral evolution profiling and PARAFAC

Baum, A., Meyer, A. S., García, J. L. M., Egebo, M., Hansen, P. W., & Mikkelsen, J. D. (2013) · Analytica Chimica Acta · doi:10.1016/j.aca.2013.03.029 · Cited by 19

The Analysis of the Antibiotic Resistome Offers New Opportunities for Therapeutic Intervention

Corona, F., Blanco, P., Alcalde‐Rico, M., Hernando‐Amado, S., Lira, F., Bernardini, A., Sánchez, M. B., & Martínez, J. L. (2016) · Future Medicinal Chemistry · doi:10.4155/fmc-2016-0027 · Cited by 20

Structural and Biochemical Characterization of Rm3, a Subclass B3 Metallo-β-Lactamase Identified from a Functional Metagenomic Study

Salimraj, R., Zhang, L., Hinchliffe, P., Wellington, E. M. H., Brem, J., Schofield, C. J., Gaze, W. H., & SPENCER, J. M. (2016) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00750-16 · Cited by 19

Antimicrobial activities of LCB10-0200, a novel siderophore cephalosporin, against the clinical isolates of Pseudomonas aeruginosa and other pathogens

Oh, S., Park, H.-S., Kim, H., Yun, J.-Y., Oh, K., Cho, Y. L., & Kwak, J. (2017) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2017.06.001 · Cited by 19

Antibiotic-Nanomedicines: Facing the Challenge of Effective Treatment of Antibiotic-Resistant Respiratory Tract Infections

Ritsema, J. A. S., van der Weide, H., Welscher, Y. M. T., Goessens, W. H. F., van Nostrum, C. F., Storm, G., Bakker‐Woudenberg, I. A. J. M., & Hays, J. P. (2018) · Future Microbiology · doi:10.2217/fmb-2018-0194 · Cited by 19

A complex suite of loci and elements in eukaryotic type II topoisomerases determine selective sensitivity to distinct poisoning agents

Blower, T. R., Bandak, A. F., Lee, A. S. Y., Austin, C. A., Nitiss, J. L., & Berger, J. M. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz579 · Cited by 19

4-Amino-1,2,4-triazole-3-thione as a Promising Scaffold for the Inhibition of Serine and Metallo-β-Lactamases

Linciano, P., Gianquinto, E., Montanari, M., Maso, L., Bellio, P., Cebrián-Sastre, E., Celenza, G., Blázquez, J., Cendron, L., Spyrakis, F., et al. (2020) · Pharmaceuticals · doi:10.3390/ph13030052 · Cited by 19

Permeability enhancers sensitize β-lactamase-expressing Enterobacteriaceae and Pseudomonas aeruginosa to β-lactamase inhibitors, thereby restoring their β-lactam susceptibility

Ferrer‐Espada, R., Sánchez-Gómez, S., Pitts, B., Stewart, P. S., & de Tejada, G. M. (2020) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2020.105986 · Cited by 19

Discovery of ferrocene-carborane derivatives as novel chemical antimicrobial agents against multidrug-resistant bacteria

Li, S., Wu, C., Lv, X., Tang, X., Zhao, X., Yan, H., Jiang, H., & Wang, X. (2012) · Science China Chemistry · doi:10.1007/s11426-012-4621-y · Cited by 19

Hemoglobin and hematocrit: an analysis of clinical accuracy. Case study of the anemic patient.

Keen, M. L. (1998) · PubMed · Cited by 19

The rise of neutron cryo-crystallography

Kwon, H., Langan, P. S., Coates, L., Raven, E. L., & Moody, P. C. E. (2018) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s205979831800640x · Cited by 19

Beta‐Lactams

Balsalobre, L., Blanco, A., & Alarcón, T. (2019) · Wiley eBooks · doi:10.1002/9781119282549.ch3 · Cited by 19

Does Antibiotic Resistance Evolve in Hospitals?

Seigal, A., Mira, P., Sturmfels, B., & Barlow, M. (2017) · Bulletin of Mathematical Biology · doi:10.1007/s11538-016-0232-7 · Cited by 18

Synthesis and antibacterial evaluation of quinoline–sulfonamide hybrid compounds: a promising strategy against bacterial resistance

Saifi, Z., Ali, A., Inam, A., Azam, A., Kamthan, M., Abid, M., & Ali, I. (2025) · RSC Advances · doi:10.1039/d4ra05069j · Cited by 18

The Next Frontier: Unveiling Novel Approaches for Combating Multidrug-Resistant Bacteria

Mallari, P., Rostami, L. D., Alanko, I., Howaili, F., Ran, M., Bansal, K. K., Rosenholm, J. M., & Salo‐Ahen, O. M. H. (2025) · Pharmaceutical Research · doi:10.1007/s11095-025-03871-x · Cited by 19

Serratia marcescens: A Versatile Opportunistic Pathogen with Emerging Clinical and Biotechnological Significance

Boldeanu, L., Boldeanu, M. V., Novac, M. B., Assani, M.-Z., & Radu, L. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262311479 · Cited by 18

Carbamylmethyl Mercaptoacetate Thioether: A Novel Scaffold for the Development of L1 Metallo-β-lactamase Inhibitors

Chang, Y., Yang, X., Zhang, Y., Wang, W., Chen, C., Oelschlaeger, P., & Yang, K. (2017) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.7b00058 · Cited by 18

Atomic‐Resolution Structure of a Class C β‐Lactamase and Its Complex with Avibactam

Pozzi, C., Pisa, F. D., Luca, F. D., Benvenuti, M., Docquier, J., & Mangani, S. (2018) · ChemMedChem · doi:10.1002/cmdc.201800213 · Cited by 18

Access to Unprotected β-Fluoroalkyl β-Amino Acids and Their α-Hydroxy Derivatives

Sukach, V. A., Melnykov, S., Bertho, S., Diachenko, I., Retailleau, P., Vovk, M., & Gillaizeau, I. (2019) · Organic Letters · doi:10.1021/acs.orglett.9b00622 · Cited by 18

Population Pharmacokinetics of Meropenem and Vaborbactam Based on Data from Noninfected Subjects and Infected Patients

Trang, M., Griffith, D. C., Bhavnani, S. M., Loutit, J., Dudley, M. N., Ambrose, P. G., & Rubino, C. M. (2021) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02606-20 · Cited by 18

In Vitro and In Vivo Development of a β-Lactam-Metallo-β-Lactamase Inhibitor: Targeting Carbapenem-Resistant Enterobacterales

Peters, B. K., Reddy, N., Shungube, M., Girdhari, L., Baijnath, S., Mdanda, S., Chetty, L. C., Ntombela, T., Arumugam, T., Bester, L. A., et al. (2023) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.2c00485 · Cited by 18

Risk Factors for Cefoperazone/Sulbactam-Induced Coagulation Disorder

Miao, W., Guo, J., Cheng, H., & Zhao, Q. (2023) · Infection and Drug Resistance · doi:10.2147/idr.s429706 · Cited by 18

Preserving the efficacy of antibiotics to tackle antibiotic resistance

Laborda, P., Gil‐Gil, T., Martínez, J. L., & Hernando‐Amado, S. (2024) · Microbial Biotechnology · doi:10.1111/1751-7915.14528 · Cited by 18

Private benefit of β-lactamase dictates selection dynamics of combination antibiotic treatment

Ma, H. R., Xu, H. Z., Kim, K., Anderson, D. J., & You, L. (2024) · Nature Communications · doi:10.1038/s41467-024-52711-w · Cited by 18

Understanding the Structural Mechanisms of Antibiotic Resistance Sets the Platform for New Discovery

Reeve, S. M., Lombardo, M. N., & Anderson, A. C. (2015) · Future Microbiology · doi:10.2217/fmb.15.78 · Cited by 18

Inactivation of a class A and a class C β-lactamase by 6β-(hydroxymethyl)penicillanic acid sulfone

Papp‐Wallace, K. M., Bethel, C. R., Gootz, T. D., Shang, W., Stroh, J. G., Lau, W., McLeod, D., Price, L. M., Marfat, A., Distler, A. M., et al. (2011) · Biochemical Pharmacology · doi:10.1016/j.bcp.2011.11.015 · Cited by 18

Combinatorial active‐site variants confer sustained clavulanate resistance in B laC β‐lactamase from M ycobacterium tuberculosis

Egesborg, P., Carlettini, H., Volpato, J. P., & Doucet, N. (2014) · Protein Science · doi:10.1002/pro.2617 · Cited by 18

Enantioselective Synthesis and Profiling of Two Novel Diazabicyclooctanone β-Lactamase Inhibitors

Xiong, H., Chen, B., Durand-Réville, T. F., Joubran, C., Alelyunas, Y. W., Wu, D., & Huynh, H. K. (2014) · ACS Medicinal Chemistry Letters · doi:10.1021/ml500284k · Cited by 18

Characterization of β-lactamase activity using isothermal titration calorimetry

Wang, W., Wang, Q., Zhang, Y., Lu, R., Zhang, Y., Yang, K., Lei, J., & He, Y. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.04.011 · Cited by 18

Improvement of clavulanic acid production in Streptomyces clavuligerus F613-1 by using a claR - neo reporter strategy

Qin, R., Zhong, C., Zong, G., Fu, J., Pang, X., & Cao, G. (2017) · Electronic Journal of Biotechnology · doi:10.1016/j.ejbt.2017.05.002 · Cited by 18

Mechanisms of proton relay and product release by Class A β‐lactamase at ultrahigh resolution

Lewandowski, E. M., Lethbridge, K. G., Sanishvili, R., Skiba, J., Kowalski, K., & Chen, Y. (2017) · FEBS Journal · doi:10.1111/febs.14315 · Cited by 18

The role of conserved residues in the catalytic activity of NDM-1: an approach involving site directed mutagenesis and molecular dynamics

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