Cited by 1,709Antibiotic Resistance in BacteriaAntibiotics Pharmacokinetics and EfficacySynthesis of β-Lactam Compounds

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Three Decades of β-Lactamase Inhibitors

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Drawz, Sarah M., Bonomo, Robert A.·2010·Clinical Microbiology Reviews

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Abstract

Since the introduction of penicillin, beta-lactam antibiotics have been the antimicrobial agents of choice. Unfortunately, the efficacy of these life-saving antibiotics is significantly threatened by bacterial beta-lactamases. beta-Lactamases are now responsible for resistance to penicillins, extended-spectrum cephalosporins, monobactams, and carbapenems. In order to overcome beta-lactamase-mediated resistance, beta-lactamase inhibitors (clavulanate, sulbactam, and tazobactam) were introduced into clinical practice. These inhibitors greatly enhance the efficacy of their partner beta-lactams (amoxicillin, ampicillin, piperacillin, and ticarcillin) in the treatment of serious Enterobacteriaceae and penicillin-resistant staphylococcal infections. However, selective pressure from excess antibiotic use accelerated the emergence of resistance to beta-lactam-beta-lactamase inhibitor combinations. Furthermore, the prevalence of clinically relevant beta-lactamases from other classes that are resistant to inhibition is rapidly increasing. There is an urgent need for effective inhibitors that can restore the activity of beta-lactams. Here, we review the catalytic mechanisms of each beta-lactamase class. We then discuss approaches for circumventing beta-lactamase-mediated resistance, including properties and characteristics of mechanism-based inactivators. We next highlight the mechanisms of action and salient clinical and microbiological features of beta-lactamase inhibitors. We also emphasize their therapeutic applications. We close by focusing on novel compounds and the chemical features of these agents that may contribute to a "second generation" of inhibitors. The goal for the next 3 decades will be to design inhibitors that will be effective for more than a single class of beta-lactamases.

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Items 401–462 of 462

Different Transition-State Structures for the Reactions of β-Lactams and Analogous β-Sultams with Serine β-Lactamases
Tsang, W. Y., Ahmed, N., Hinchliffe, P. S., Wood, J. M., Harding, L. P., Laws, A. P., & Page, M. I. (2005) · Journal of the American Chemical Society · doi:10.1021/ja056124z · Cited by 27
The Role of a Second-Shell Residue in Modifying Substrate and Inhibitor Interactions in the SHV β-Lactamase: A Study of Ambler Position Asn276
Drawz, S. M., Bethel, C. R., Hujer, K. M., Hurless, K. N., Distler, A. M., Caselli, E., Prati, F., & Bonomo, R. A. (2009) · Biochemistry · doi:10.1021/bi9003292 · Cited by 27
Self-citation
Mechanism of Inactivation of β-Lactamases by Novel 6-Methylidene Penems Elucidated Using Electrospray Ionization Mass Spectrometry
Tabei, K., Feng, X., Venkatesan, A. M., Abé, T., Ushirogochi, H., Mansour, T. S., & Siegel, M. M. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm049903j · Cited by 27
Structure-Based Design of β-Lactamase Inhibitors. 2. Synthesis and Evaluation of Bridged Sulfactams and Oxamazins
Hubschwerlen, C., Angehrn, P., Gubernator, K., Page, M. G. P., & Specklin, J. (1998) · Journal of Medicinal Chemistry · doi:10.1021/jm9800245 · Cited by 27
Studies on the mechanism of action of (5R)-(Z)-6-(1-methyl-1,2,3-triazol-4-ylmethylene)penem-3-carboxylic acid (BRL 427 15), a potent inhibitor of bacterial β-lactamase
BROOM, N. J. P., Farmer, T. H., Osborne, N. F., & Tyler, J. W. (1992) · Journal of the Chemical Society Chemical Communications · doi:10.1039/c39920001663 · Cited by 26
Multiple Conformations of the Acylenzyme Formed in the Hydrolysis of Methicillin by Citrobacter freundii β-Lactamase: a Time-Resolved FTIR Spectroscopic Study
Wilkinson, A.-S., Ward, S., Kania, M., Page, M. G. P., & Wharton, C. W. (1999) · Biochemistry · doi:10.1021/bi990030i · Cited by 26
The Lys234Arg Substitution in the Enzyme SHV-72 Is a Determinant for Resistance to Clavulanic Acid Inhibition
Mendonça, N., Manageiro, V., Robin, F., Salgado, M. J., Ferreira, E., Caniça, M., & Bonnet, R. (2008) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01381-07 · Cited by 26
Cephalosporin-derived inhibitors of β-Lactamase. Part 4: The C3 substituent
Buynak, J. D., Vogeti, L., Doppalapudi, V. R., Solomon, G. M., & Chen, H. (2002) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(02)00205-6 · Cited by 26
New molecules from old classes: revisiting the development of beta-lactams.
Page, M. G. P., & Heim, J. (2009) · PubMed · Cited by 25
Relatedness Among Penicillin-Binding Protein 2b Genes of Streptococcus mitis , Streptococcus oralis , and Streptococcus pneumoniae
Potgieter, E., & Chalkley, L. J. (1995) · Microbial Drug Resistance · doi:10.1089/mdr.1995.1.35 · Cited by 25
6-(1-Hydroxyalkyl)penam sulfone derivatives as inhibitors of class A and class C β-lactamases II
Bitha, P., Li, Z., Francisco, G. D., Yang, Y., Petersen, P. J., Lenoy, E., & Lin, Y. (1999) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(99)00107-9 · Cited by 25
Synthesis of metallo-β-lactamase inhibitors
Walter, M. W., Adlington, R. M., Baldwin, J. E., & Schofield, C. J. (1997) · Tetrahedron · doi:10.1016/s0040-4020(97)00404-3 · Cited by 25
AMOXYCILLIN/CLAVULANATE RESISTANT ESCHERICHIA COLI
Williams, H., King, A., Shannon, K. P., & Phillips, I. (1988) · The Lancet · doi:10.1016/s0140-6736(88)90391-1 · Cited by 24
In vitro activity of combinations of beta-lactam antibiotics with beta-lactamase inhibitors against cephalosporinase-producing bacteria
Kitzis, M.-D., Ferre, B., Coutrot, A., Acar, J. F., & Gutmann, L. (1989) · European Journal of Clinical Microbiology & Infectious Diseases · doi:10.1007/bf02185845 · Cited by 24
Kinetics and Mechanism of Inhibition of a Serine β-Lactamase by O-Aryloxycarbonyl Hydroxamates
Pelto, R. B., & Pratt, R. F. (2008) · Biochemistry · doi:10.1021/bi8015247 · Cited by 24
Inhibition of Class D β-Lactamases by Acyl Phosphates and Phosphonates
Adediran, S. A., Nukaga, M., Baurin, S., Frère, J.-M., & Pratt, R. F. (2005) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.49.10.4410-4412.2005 · Cited by 24
Effect of conalbumin on the activity of Syn 2190, a 1,5 dihydroxy-4-pyridon monobactam inhibitor of AmpC beta-lactamases
Babini, G. S. (2000) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/45.1.105 · Cited by 24
Mechanisms of reduced susceptibility to amoxycillin-clavulanic acid in Escherichia coli strains from the health region of Tortosa (Catalonia, Spain)
Pérez-Moreno, M. O., Katargina, O., Pérez-Moreno, M., Carulla, M., Rubio, C., Jardí, A. M., & Zaragoza, J. (2004) · Clinical Microbiology and Infection · doi:10.1111/j.1198-743x.2004.00766.x · Cited by 23
Raman Crystallographic Studies of the Intermediates Formed by Ser130Gly SHV, a β-Lactamase that Confers Resistance to Clinical Inhibitors
Helfand, M. S., Taracila, M. A., Totir, M. A., Bonomo, R. A., Buynak, J. D., van den Akker, F., & CAREY, P. R. (2007) · Biochemistry · doi:10.1021/bi700581q · Cited by 23
Self-citation
In Vitro and In Vivo Activities of AM-112, a Novel Oxapenem
Jamieson, C., Lambert, P. A., & Simpson, I. N. (2003) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.47.5.1652-1657.2003 · Cited by 23
N-Sulfonyloxy-β-lactam Inhibitors for β-Lactamases
Bulychev, A., Bellettini, J. R., O'Brien, M., Crocker, P. J., Samama, J., Miller, M. J., & Mobashery, S. (2000) · Tetrahedron · doi:10.1016/s0040-4020(00)00427-0 · Cited by 23
Clavulanate inactivation of Staphylococcus aureus β-lactamase
Rizwi, I., Tan, A. K., Fink, A. L., & Virden, R. (1989) · Biochemical Journal · doi:10.1042/bj2580205 · Cited by 22
Efficient Inhibition of Class A and Class D β-Lactamases by Michaelis Complexes
Kalp, M., Sheri, A., Buynak, J. D., Bethel, C. R., Bonomo, R. A., & CAREY, P. R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c700080200 · Cited by 22
Self-citation
Kinetic Study of Two Novel Enantiomeric Tricyclic β-Lactams Which Efficiently Inactivate Class C β-Lactamases
Vilar, M., Galleni, M., Šolmajer, T., Turk, B., Frère, J., & Matagne, A. (2001) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.45.8.2215-2223.2001 · Cited by 22
6-(1-hydroxyalkyl)penam sulfone derivatives as inhibitors of class a and class C β-lactamases I
Bitha, P., Li, Z., Francisco, G. D., Rasmussen, B. A., & Lin, Y. (1999) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(99)00106-7 · Cited by 22
6-(Hydroxyalkyl)penicillanates as Probes for Mechanisms of .BETA.-Lactamases.
Golemi, D., Maveyraud, L., Ishiwata, A., TRAMER, S., Miyashita, K., Nagase, T., Massova, I., Mourey, L., Samama, J., & Mobashery, S. (2000) · The Journal of Antibiotics · doi:10.7164/antibiotics.53.1022 · Cited by 21
Inhibition of the Broad Spectrum Nonmetallocarbapenamase of Class A (NMC-A) β-Lactamase from Enterobacter cloacae by Monocyclic β-Lactams
Mourey, L., Kotra, L. P., Bellettini, J. R., Bulychev, A., O'Brien, M., Miller, M. J., Mobashery, S., & Samama, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25260 · Cited by 21
SYN-1012: A New .BETA.-Lactamase Inhibitor of Penem Skeleton.
Phillips, O. A., Czajkowski, D. P., Spevak, P., Singh, M. P., Kunugita, C., HYODO, A., Micetich, R. G., & Maiti, S. N. (1997) · The Journal of Antibiotics · doi:10.7164/antibiotics.50.350 · Cited by 21
Susceptibility testing with clavulanic acid: fixed concentration versus fixed ratio
Thomson, C. J., Miles, R. S., & Amyes, S. G. B. (1995) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.39.11.2591 · Cited by 21
Establishment of In Vitro Susceptibility Testing Methodologies and Comparative Activities of Piperacillin in Combination with the Penem β-Lactamase Inhibitor BLI-489
Petersen, P. J., Jones, C. H., Venkatesan, A. M., Mansour, T. S., Projan, S. J., & Bradford, P. A. (2008) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01047-08 · Cited by 21
Substitution of Arg-244 by Cys or Ser in SHV-1 and SHV-5 β-lactamases confers resistance to mechanism-based inhibitors and reduces catalytic efficiency of the enzymes
Giakkoupi, P., Tzelepi, Ε., Legakis, N. J., & TZOUVELEKIS, L. S. (1998) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1998.tb12889.x · Cited by 20
Inhibition of Class D β-Lactamases by Diaroyl Phosphates
Majumdar, S., Adediran, S. A., Nukaga, M., & Pratt, R. F. (2005) · Biochemistry · doi:10.1021/bi051719s · Cited by 19
Fine Mapping of the Sequence Requirements for Binding of β-Lactamase Inhibitory Protein (BLIP) to TEM-1 β-Lactamase Using a Genetic Screen for BLIP Function
Yuan, J., Huang, W., Chow, D., & Palzkill, T. G. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.04.028 · Cited by 18
Synthesis and antibacterial activity of (1′R,5R,6R)-2-tert-butyl-6-(1′-hydroxyethyl)oxapenem-3-carboxylic acid
Pfaendler, H. R., Weisner, F., & Metzger, K. (1993) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(01)80927-6 · Cited by 18
Inhibition of Serine β-Lactamases by Acyl Phosph(on)ates: A New Source of Inert Acyl [and Phosphyl] Enzymes
Li, N., & Pratt, R. F. (1998) · Journal of the American Chemical Society · doi:10.1021/ja9741537 · Cited by 18
Timentin and -lactamases
Labia, R., Morand, A., & Péduzzi, J. (1986) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/17.suppl_c.17 · Cited by 17
Design, synthesis and bioactivity evaluation of tribactam β lactamase inhibitors
Čopar, A., Prevec, T., Anžič, B., Mesar, T., Selič, L., Vilar, M., & Šolmajer, T. (2002) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(02)00061-6 · Cited by 17
Analysis of β-lactamases produced by cephalothin-susceptible Escherichia coli clinical isolates resistant to co-amoxiclav and ticarcillin-clavulanic acid
Chardon, H., Farzaneh, S., Labia, R., Jarlier, V., Nicolas-Chanoine, M.-H., PAUL, G., Poyart, C., Sirot, D., & Sirot, J. (1995) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/36.1.267 · Cited by 16
Thermodynamic Cycle Analysis and Inhibitor Design against Beta-Lactamase
Roth, T. A., Minasov, G., Morandi, S., Prati, F., & Shoichet, B. K. (2003) · Biochemistry · doi:10.1021/bi035054a · Cited by 16
Use of Novel Boronic Acid Transition State Inhibitors To Probe Substrate Affinity in SHV-Type Extended-Spectrum β-Lactamases
Thomson, J. M., Prati, F., Bethel, C. R., & Bonomo, R. A. (2007) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01293-06 · Cited by 16
Self-citation
Allyl and propargyl substituted penam sulfones as versatile intermediates toward the syntheses of new β-lactamase inhibitors
Sandanayaka, V. P., Feigelson, G. B., Prashad, A. S., Yang, Y., & Petersen, P. J. (2001) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(01)00148-2 · Cited by 15
Characterization of extended spectrum β-lactamase-producing Klebsiella pneumoniae from Beijing, China
Shen, D., Winokur, P. L., & Jones, R. N. (2001) · International Journal of Antimicrobial Agents · doi:10.1016/s0924-8579(01)00351-x · Cited by 15
Inhibition of Class A and C β-Lactamases by Diaroyl Phosphates
Majumdar, S., & Pratt, R. F. (2009) · Biochemistry · doi:10.1021/bi900807e · Cited by 15
Kinetic studies on the inhibition of Proteus vulgaris beta-lactamase by imipenem
Hashizume, T., Yamaguchi, A., Hirata, T., & Sawai, T. (1984) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.25.1.149 · Cited by 15
Aspartic acid for asparagine substitution at position 276 reduces susceptibility to mechanism-based inhibitors in SHV-1 and SHV-5 β-lactamases
Giakkoupi, P., Tzelepi, Ε., Legakis, N. J., & TZOUVELEKIS, L. S. (1999) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/43.1.23 · Cited by 15
Evaluation of enzyme inhibition data in screening for new drugs.
Bush, K. (1986) · PubMed · Cited by 13
Expression, purification, and crystallization of meso‐diaminopimelate dehydrogenase from Corynebacterium glutamicum
Reddy, S. G., Scapin, G., & Blanchard, J. S. (1996) · Proteins Structure Function and Bioinformatics · doi:10.1002/(sici)1097-0134(199608)25:4 · Cited by 12
Inhibitor-Resistant TEM-33 β-Lactamase in a Shigella sonnei Isolate
Sirot, D., Chanal, C., Bonnet, R., de Champs, C., Sirot, J., & Bret, L. (2001) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.45.7.2179-2180.2001 · Cited by 12
OHIO-1 β-lactamase mutants: the Arg244Ser mutant and resistance to β-lactams and β-lactamase inhibitors
Lin, S., Thomas, M., Mark, S., Anderson, V. E., & Bonomo, R. A. (1999) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00025-4 · Cited by 11
Self-citation
Global distribution of penicillinase-producing Neisseria gonorrhoeae (PPNG).
(1982) · PubMed · Cited by 11
In vitro activities of parenteral beta-lactam antimicrobials against TEM-10-, TEM-26- and SHV-5-derived extended-spectrum beta-lactamases expressed in an isogenic Escherichia coli host
Rebuck, J. A. (2000) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/46.3.461 · Cited by 10
Effect of a β-lactamase inhibitor, tazobactam, on growth and penicillin-binding proteins of Borrelia burgdorferi
Urban, C. M. (1991) · FEMS Microbiology Letters · doi:10.1016/0378-1097(91)90430-i · Cited by 9
Crystallization and preliminary X-ray study of OXA-1, a class D β-lactamase
Sun, T., Nukaga, M., Mayama, K., Crichlow, G. V., Kuzin, A. P., & Knox, J. R. (2001) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444901016274 · Cited by 9
Inhibition of Serine β-Lactamases by Vanadate−Catechol Complexes
Adediran, S. A., & Pratt, R. F. (2008) · Biochemistry · doi:10.1021/bi801153j · Cited by 8
Problems encountered in the characterization of IRT β-lactamase-producing clinical Escherichia coil isolates intermediate-resistant to cephalothin
Chaibi, E. B., Farzaneh, S., Morand, A., Péduzzi, J., Barthélémy, M., Sirot, D., & Labia, R. (1996) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/37.1.190 · Cited by 8
TEM-103/IRT-28 β-Lactamase, a New TEM Variant Produced by Escherichia coli BM4511
Alonso, R., Gerbaud, G., Galimand, M., & Courvalin, P. M. (2002) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.46.11.3627-3629.2002 · Cited by 8
ChemInform Abstract: Structure‐Based Design of β‐Lactamase Inhibitors. Part 2. Synthesis and Evaluation of Bridged Sulfactams and Oxamazins.
Hubschwerlen, C., Angehrn, P., Gubernator, K., Page, M. G. P., & Specklin, J. (1999) · ChemInform · doi:10.1002/chin.199911131 · Cited by 7
Intramolecular Cooperativity in the Reaction of Diacyl Phosphates with Serine β-Lactamases
Majumdar, S., & Pratt, R. F. (2009) · Biochemistry · doi:10.1021/bi900808x · Cited by 5
Clinical experience with aztreonam in urinary and respiratory tract infections
Hollingsworth, J., Donohoe, J. F., Hone, R., & Keelan, P. J. (1984) · Current Medical Research and Opinion · doi:10.1185/03007998409109599 · Cited by 5
β-Lactamases: Historical Perspectives
Bush, K., & Bradford, P. A. (2014) · ASM Press eBooks · doi:10.1128/9781555815615.ch6 · Cited by 4
Treatment with beta-lactam antibiotics in skin and soft tissue infections.
Hedström, S. A. (1984) · PubMed · Cited by 2
Corrigendum to “allyl and Propargyl substituted penam sulfones as versatile intermediates toward the syntheses of new β-lactamase inhibitors”
Sandanayaka, V. P., Feigelson, G. B., Prashad, A. S., Yang, Y., & Petersen, P. J. (2001) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(01)00342-0 · Cited by 2

Flagged first, then by citations

2 of the 464 references couldn’t be matched to a known paper.

Research works printed but not linked: 14

Danel, F., M. G. Page, and D. M. Livermore. 2007. Class D β-lactamases, p. 163-194. In R. A. Bonomo and M. E. Tolmasky (ed.), Enzyme-mediated resistance to antibiotics: mechanisms, dissemination, and prospects for inhibition. ASM Press, Washington, DC.
Abstr. 47th Intersci. Conf. Antimicrob. Agents Chemother. 2007
Dubus, A., P. Ledent, J. Lamotte-Brasseur, and J. M. Frere. 1996. The roles of residues Tyr150, Glu272, and His314 in class C β-lactamases. Proteins25:473-485.
Foulds, G., W. E. Barth, J. R. Bianchine, A. R. English, D. Girard, S. L. Hayes, M. O'Brien, and P. Somani. 1980. Pharmacokinetics of CP-45.899 and pro-drug CP-47.904 in animals and humans, p. 353-356. In J. D. Nelson and C. Grassi (ed.), Current chemotherapy and infectious disease. American Society for Microbiology, Washington DC.
Galleni, M., and J. M. Frere. 2007. Kinetics of β-lactamases and pencillin-binding proteins, p. 195-213. In R. A. Bonomo and M. E. Tolmasky (ed.), Enzyme-mediated resistance to antibiotics: mechanisms, dissemination, and prospects for inhibition. ASM Press, Washington, DC.
F1-310. Abstr. 47th Intersci. Conf. Antimicrob. Agents Chemother. 2007
F1-333a. Abstr. 47th Intersci. Conf. Antimicrob. Agents Chemother. 2007
Livermore, D. M., M. Akova, P. J. Wu, and Y. J. Yang. 1989. Clavulanate and β-lactamase induction. J. Antimicrob. Chemother.24(Suppl. B):23-33.
A1-006. Abstr. 49th Intersci. Conf. Antimicrob. Agents Chemother. 2009
Meroueh, S., J. Cha, and S. Mobashery. 2007. Inhibition of class A β-lactamases, p. 101-114. In R. A. Bonomo and M. E. Tolmasky (ed.), Enzyme-mediated resistance to antibiotics: mechanisms, dissemination, and prospects for inhibition. ASM Press, Washingtion, DC.
Page, M. G. 2007. Resistance mediated by penicllin-binding proteins, p. 81-99. In R. A. Bonomo and M. E. Tolmasky (ed.), Enzyme-mediated resistance to antibiotics: mechanisms, dissemination, and prospects for Inhibition. ASM Press, Washington, DC.
F1-311. Abstr. 47th Intersci. Conf. Antimicrob. Agents Chemother. 2007
F1-0882. Abstr. 47th Intersci. Conf. Antimicrob. Agents Chemother. 2007
Slocombe, B., A. S. Beale, R. J. Boon, K. E. Griffin, P. J. Masters, R. Sutherland, and A. R. White. 1984. Antibacterial activity in vitro and in vivo of amoxicillin in the presence of clavulanic acid, p. 29-49. InProgress and perspectives on β-lactamase inhibition: a review of Augmentin. Custom Communications: Postgraduate Medicine, New York, NY.

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Authors: Drawz, S. M., & Bonomo, R. A.
Affiliations: Departments of Pathology
United States Department of Veterans Affairs (US)
Corresponding author: Bonomo, Robert A.
ORCID: Bonomo, Robert A.
Venue: Clinical Microbiology Reviews
Publisher: American Society for Microbiology
Published: 2010-01
Volume: 23
Issue: 1
Pages: 160-201
ISSN: 0893-8512 (ISSN-L)
1098-6618
DOI: 10.1128/cmr.00037-09
PMC: PMC2806661
OpenAlex: W1895007034
Cited by: 1,709
References: 464
Citations by year: 2026: 83 · 2025: 100 · 2024: 87 · 2023: 86 · 2022: 106 · 2021: 126 · 2020: 151 · 2019: 130 · 2018: 131 · 2017: 119 · 2016: 120 · 2015: 108 · 2014: 93 · 2013: 88 · 2012: 81
FWCI: 4.26
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Clinical Microbiology Reviews (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: U.S. Public Health Service (1R01A1063517-01)
National Institute of General Medical Sciences (T32GM007250, T32GM07250)
Topics: Health Sciences › Medicine › Microbiology (medical) › Antibiotic Resistance in Bacteria
Health Sciences › Medicine › Pharmacology (medical) › Antibiotics Pharmacokinetics and Efficacy
Physical Sciences › Chemistry › Organic Chemistry › Synthesis of β-Lactam Compounds
Keywords: beta-lactamase inhibitors, beta-lactamase, beta-lactam resistance, clavulanic acid, sulbactam, tazobactam, mechanism-based inactivators, carbapenemase inhibitors, extended-spectrum cephalosporin resistance, Enterobacteriaceae, penicillin-resistant staphylococci
MeSH terms: Bacteria, Bacterial Infections, Bacterial Proteins, beta-Lactamases, Enzyme Inhibitors, Humans, beta-Lactam Resistance, beta-Lactamase Inhibitors

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Three Decades of β-Lactamase Inhibitors

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