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Bacterial Resistance to β-Lactam Antibiotics: Compelling Opportunism, Compelling Opportunity
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTBacterial Resistance to β-Lactam Antibiotics: Compelling Opportunism, Compelling Opportunity†Jed F. Fisher, Samy O. Meroueh, and Shahriar MobasheryView Author Information Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556 Cite this: Chem. Rev. 2005, 105, 2, 395–424Publication Date (Web):February 9, 2005Publication History Received3 June 2004Published online9 February 2005Published inissue 1 February 2005https://pubs.acs.org/doi/10.1021/cr030102ihttps://doi.org/10.1021/cr030102iresearch-articleACS PublicationsCopyright © 2005 American Chemical SocietyRequest reuse permissionsArticle Views10570Altmetric-Citations746LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose SUBJECTS:Antimicrobial agents,Bacteria,Genetics,Monomers,Peptides and proteins Get e-Alerts
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Citations
Cites
Molecular Basis of Bacterial Outer Membrane Permeability Revisited
Nikaido, H. (2003) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.67.4.593-656.2003 · Cited by 4,316
Antibacterial resistance worldwide: causes, challenges and responses
Levy, S. B., & Marshall, B. (2004) · Nature Medicine · doi:10.1038/nm1145 · Cited by 4,052
Bacterial Persistence as a Phenotypic Switch
Balaban, N. Q., Merrin, J., Chait, R., Kowalik, L., & Leibler, S. (2004) · Science · doi:10.1126/science.1099390 · Cited by 2,952
Bradford, P. A. (2001) · Clinical Microbiology Reviews · doi:10.1128/cmr.14.4.933-951.2001 · Cited by 2,618
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 2,475
beta-Lactamases in laboratory and clinical resistance
Livermore, D. M. (1995) · Clinical Microbiology Reviews · doi:10.1128/cmr.8.4.557 · Cited by 1,779
"Celbenin" - resistant Staphylococci
Jevons, M. P. (1961) · BMJ · doi:10.1136/bmj.1.5219.124-a · Cited by 1,680
Comprehensive natural products chemistry
(1999) · Choice Reviews Online · doi:10.5860/choice.37-0939 · Cited by 1,617
Molecular mechanisms that confer antibacterial drug resistance
Walsh, C. (2000) · Nature · doi:10.1038/35021219 · Cited by 1,578
Structures of Gram-Negative Cell Walls and Their Derived Membrane Vesicles
Beveridge, T. J. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.16.4725-4733.1999 · Cited by 1,528
Growing Group of Extended-Spectrum β-Lactamases: the CTX-M Enzymes
Bonnet, R. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.1.1-14.2004 · Cited by 1,494
Humans as the World's Greatest Evolutionary Force
Palumbi, S. R. (2001) · Science · doi:10.1126/science.293.5536.1786 · Cited by 1,290
A Perspective on Enzyme Catalysis
Benkovic, S. J., & Hammes-Schiffer, S. (2003) · Science · doi:10.1126/science.1085515 · Cited by 1,262
Tipper, D. J., & Strominger, J. L. (1965) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.54.4.1133 · Cited by 1,008
Ito, T., Katayama, Y., Asada, K., Mori, N., Tsutsumimoto, K., Tiensasitorn, C., & Hiramatsu, K. (2001) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.45.5.1323-1336.2001 · Cited by 963
Knothe, H., Shah, P., Krcmery, V., Antal, M., & Mitsuhashi, S. (1983) · Infection · doi:10.1007/bf01641355 · Cited by 912
Spoering, A. L., & Lewis, K. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.23.6746-6751.2001 · Cited by 902
Hartman, B. J., & Tomasz, A. (1984) · Journal of Bacteriology · doi:10.1128/jb.158.2.513-516.1984 · Cited by 890
Human intestinal bacteria as reservoirs for antibiotic resistance genes
SALYERS, A., GUPTA, A., & WANG, Y. (2004) · Trends in Microbiology · doi:10.1016/j.tim.2004.07.004 · Cited by 846
Where will new antibiotics come from?
Walsh, C. (2003) · Nature Reviews Microbiology · doi:10.1038/nrmicro727 · Cited by 755
The future challenges facing the development of new antimicrobial drugs
Coates, A., Hu, Y., Bax, R., & Page, C. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd940 · Cited by 704
The versatile bacterial type IV secretion systems
Cascales, E., & Christie, P. J. (2003) · Nature Reviews Microbiology · doi:10.1038/nrmicro753 · Cited by 694
Emerging carbapenemases in Gram-negative aerobes
Nordmann, P., & Poirel, L. (2002) · Clinical Microbiology and Infection · doi:10.1046/j.1469-0691.2002.00401.x · Cited by 684
Challis, G. L., & Hopwood, D. A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1934677100 · Cited by 597
SOS Response Induction by ß-Lactams and Bacterial Defense Against Antibiotic Lethality
Miller, C., Thomsen, L. E., Gaggero, C., Mosseri, R., Ingmer, H., & Cohen, S. N. (2004) · Science · doi:10.1126/science.1101630 · Cited by 584
Promoting resistance by the emission of antibiotics from hospitals and households into effluent
Kümmerer, K., & Henninger, A. (2003) · Clinical Microbiology and Infection · doi:10.1111/j.1469-0691.2003.00739.x · Cited by 581
Cellbenin-resistant staphylococci.
Jevons, M. P. (1961) · Medical Entomology and Zoology · Cited by 555
Goh, E.-B., Yim, G., Tsui, W., McClure, J., Surette, M. G., & Davies, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252607699 · Cited by 547
Chemical warfare between microbes promotes biodiversity
Czárán, T. L., Hoekstra, R. F., & Pagie, L. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.012399899 · Cited by 535
Molecular structure of the acyl-enzyme intermediate in β-lactam hydrolysis at 1.7 Å resolution
Strynadka, N. C. J., Adachi, H., Jensen, S. E., Johns, K., Sielecki, A., Betzel, C., Sutoh, K., & James, M. N. G. (1992) · Nature · doi:10.1038/359700a0 · Cited by 525
Why is big Pharma getting out of antibacterial drug discovery?
Projan, S. J. (2003) · Current Opinion in Microbiology · doi:10.1016/j.mib.2003.08.003 · Cited by 503
Microbial Cell Walls and Membranes
Rogers, H. J., Perkins, H. R., & Ward, J. B. (1980) · Springer eBooks · doi:10.1007/978-94-011-6014-8 · Cited by 495
Oliveira, D. C., Tomasz, A., & de Lencastre, H. (2002) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(02)00227-x · Cited by 494
Radzicka, A., & Wolfenden, R. (1996) · Journal of the American Chemical Society · doi:10.1021/ja954077c · Cited by 484
Natural products ? a simple model to explain chemical diversity
Firn, R. D., & Jones, C. G. (2003) · Natural Product Reports · doi:10.1039/b208815k · Cited by 467
Multidrug resistance mechanisms: drug efflux across two membranes
Zgurskaya, H. I., & Nikaido, H. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01926.x · Cited by 466
Evolution of an Antibiotic Resistance Enzyme Constrained by Stability and Activity Trade-offs
Wang, X., Minasov, G., & Shoichet, B. K. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00400-x · Cited by 458
Bradford, P. A., Urban, C., Mariano, N., Projan, S. J., Rahal, J. J., & Bush, K. (1997) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.41.3.563 · Cited by 450
Lim, D., & Strynadka, N. C. J. (2002) · Nature Structural Biology · doi:10.1038/nsb858 · Cited by 442
Persistence of antibiotic resistant bacteria
Andersson, D. I. (2003) · Current Opinion in Microbiology · doi:10.1016/j.mib.2003.09.001 · Cited by 438
Regulation of bacterial drug export systems
Grkovic, S., Brown, M. H., & Skurray, R. A. (2002) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.66.4.671-701.2002 · Cited by 423
Kinship and Diversification of Bacterial Penicillin-Binding Proteins and β-Lactamases
Massova, I., & Mobashery, S. (1998) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.42.1.1 · Cited by 422
Self-citationThe Structure of a Mycobacterial Outer-Membrane Channel
Faller, M., Niederweis, M., & Schulz, G. E. (2004) · Science · doi:10.1126/science.1094114 · Cited by 421
Standard Numbering Scheme for Class B β-Lactamases
Galleni, M., Lamotte-Brasseur, J., Rossolini, G. M., Spencer, J., Dideberg, O., Frère, J.-M., & The Metallo-β-Lactamase Working Group (2001) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.45.3.660-663.2001 · Cited by 414
Eliopoulos, G. M., & Bush, K. (2001) · Clinical Infectious Diseases · doi:10.1086/319610 · Cited by 392
Proteomic Approach to Understanding Antibiotic Action
Bandow, J. E., Brötz, H., Leichert, L. I. O., Labischinski, H., & Hecker, M. (2003) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.47.3.948-955.2003 · Cited by 391
Weiss, D. S., Chen, J. C., Ghigo, J.-M., Boyd, D., & Beckwith, J. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.2.508-520.1999 · Cited by 386
Why Are Secondary Metabolites (Natural Products) Biosynthesized?
Williams, D. H., Stone, M. J., Hauck, P. R., & Rahman, S. K. (1989) · Journal of Natural Products · doi:10.1021/np50066a001 · Cited by 374
Utsui, Y., & Yokota, T. (1985) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.28.3.397 · Cited by 365
Resistance to ?-lactam antibiotics
Poole, K. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4060-9 · Cited by 358
Crystal structure of Escherichia coli TEM1 β‐lactamase at 1.8 Å resolution
Jelsch, C., Mourey, L., Masson, J., & Samama, J. (1993) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340160406 · Cited by 357
Ullah, J. H., Walsh, T. R., Taylor, I. A., Emery, D. C., Verma, C. S., Gamblin, S. J., & Spencer, J. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2148 · Cited by 337
Carbapenemases: a problem in waiting?
Livermore, D. M., & Woodford, N. (2000) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(00)00128-4 · Cited by 323
Evolution of the serine β-lactamases: past, present and future
Hall, B. G., & Barlow, M. (2004) · Drug Resistance Updates · doi:10.1016/j.drup.2004.02.003 · Cited by 314
Cooper, B. S., Medley, G. F., Stone, S. P., Kibbler, C. C., Cookson, B. D., Roberts, J. A., Duckworth, G., Lai, R., & Ebrahim, S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401324101 · Cited by 307
Concha, N. O., Janson, C. A., Rowling, P., Pearson, S., Cheever, C. A., Clarke, B. P., Lewis, C., Galleni, M., Frère, J.-M., Payne, D. J., et al. (2000) · Biochemistry · doi:10.1021/bi992569m · Cited by 307
Staphylococcal Cell Wall: Morphogenesis and Fatal Variations in the Presence of Penicillin
Giesbrecht, P., Kersten, T., Maidhof, H., & Wecke, J. (1998) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.62.4.1371-1414.1998 · Cited by 304
Zhao, G., Meier, T. I., Kahl, S. D., Gee, K. R., & Blaszczak, L. C. (1999) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.43.5.1124 · Cited by 300
Oefner, C., D'Arcy, A., Daly, J. J., Gubernator, K., Charnas, R. L., Heinze, I., Hubschwerlen, C., & Winkler, F. K. (1990) · Nature · doi:10.1038/343284a0 · Cited by 299
Update of the Standard Numbering Scheme for Class B β-Lactamases
Garau, G., García-Sáez, I., Bebrone, C., Anne, C., Mercuri, P., Galleni, M., Frère, J.-M., & Dideberg, O. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.7.2347-2349.2004 · Cited by 286
Afzal-Shah, M., Woodford, N., & Livermore, D. M. (2001) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.45.2.583-588.2001 · Cited by 282
Structure and function of efflux pumps that confer resistance to drugs
BORGES-WALMSLEY, M. I., McKEEGAN, K. S., & WALMSLEY, A. R. (2003) · Biochemical Journal · doi:10.1042/bj20020957 · Cited by 278
Challenges in Enzyme Mechanism and Energetics
Kraut, D. A., Carroll, K. S., & Herschlag, D. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161617 · Cited by 265
Expression of methicillin resistance in heterogeneous strains of Staphylococcus aureus
Hartman, B. J., & Tomasz, A. (1986) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.29.1.85 · Cited by 263
Vollmer, W., & Höltje, J.-V. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.18.5978-5987.2004 · Cited by 258
Inhibitor-resistant TEM -lactamases: phenotypic, genetic and biochemical characteristics
Chaibi, E. B., Sirot, D., Paul, G., & Labia, R. (1999) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/43.4.447 · Cited by 256
A Proteolytic Transmembrane Signaling Pathway and Resistance to β-Lactams in Staphylococci
Zhang, H. Z., Hackbarth, C. J., Chansky, K. M., & Chambers, H. F. (2001) · Science · doi:10.1126/science.1055144 · Cited by 252
Morphogenesis of Escherichia coli
Nanninga, N. (1998) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.62.1.110-129.1998 · Cited by 251
Antimicrobial use and bacterial resistance
Monroe, S., & Polk, R. (2000) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(00)00129-6 · Cited by 247
Critical involvement of a carbamylated lysine in catalytic function of class D β-lactamases
Golemi, D., Maveyraud, L., Vakulenko, S., Samama, J.-P., & Mobashery, S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.241442898 · Cited by 240
Self-citationPredicting the emergence of antibiotic resistance by directed evolution and structural analysis.
Orencia, M. C., Yoon, J. S., Ness, J. E., Stemmer, W. P. C., & Stevens, R. C. (2001) · Nature Structural Biology · doi:10.1038/84981 · Cited by 239
The modular architecture of protein–protein binding interfaces
Reichmann, D., Rahat, O., Albeck, S., Meged, R., Dym, O., & Schreiber, G. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407280102 · Cited by 239
Donald, H. M., Scaife, W., Amyes, S. G. B., & Young, H.-K. (2000) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.44.1.196-199.2000 · Cited by 235
Garau, G., Bebrone, C., Anne, C., Galleni, M., Frère, J.-M., & Dideberg, O. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.10.070 · Cited by 231
Weldhagen, G. F., Poirel, L., & Nordmann, P. (2003) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.47.8.2385-2392.2003 · Cited by 231
Bacterial Wall as Target for Attack: Past, Present, and Future Research
Koch, A. L. (2003) · Clinical Microbiology Reviews · doi:10.1128/cmr.16.4.673-687.2003 · Cited by 231
The evolution of secondary metabolism – a unifying model
Firn, R. D., & Jones, C. G. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.02098.x · Cited by 230
Fernandez-Cuenca, F. (2003) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkg097 · Cited by 229
Pinho, M. G., Filipe, S. R., de Lencastre, H., & Tomasz, A. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.22.6525-6531.2001 · Cited by 225
McCormick, A. W., Whitney, C. G., Farley, M. M., Lynfield, R., Harrison, L. H., Bennett, N. M., Schaffner, W., Reingold, A., Hadler, J., Cieslak, P., et al. (2003) · Nature Medicine · doi:10.1038/nm839 · Cited by 222
Multidrug efflux pumps and resistance: regulation and evolution
Paulsen, I. T. (2003) · Current Opinion in Microbiology · doi:10.1016/j.mib.2003.08.005 · Cited by 220
Fabiane, S. M., Sohi, M. K., Wan, T., Payne, D. J., Bateson, J. H., Mitchell, T., & Sutton, B. J. (1998) · Biochemistry · doi:10.1021/bi980506i · Cited by 215
Minasov, G., Wang, X., & Shoichet, B. K. (2002) · Journal of the American Chemical Society · doi:10.1021/ja0259640 · Cited by 211
The evolution of a resistant pathogen – the case of MRSA
Enright, M. (2003) · Current Opinion in Pharmacology · doi:10.1016/s1471-4892(03)00109-7 · Cited by 205
Jacoby, G. A., Mills, D. M., & Chow, N. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.8.3203-3206.2004 · Cited by 205
Carbapenem Resistance Mechanisms in Pseudomonas aeruginosa Clinical Isolates
Pai, H., Kim, J.-W., Kim, J., Lee, J. H., Choe, K. W., & Gotoh, N. (2001) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.45.2.480-484.2001 · Cited by 205
Van Bambeke, F. (2003) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkg224 · Cited by 203
Role of penicillin-binding proteins in bacterial cell morphogenesis
Popham, D. L., & Young, K. D. (2003) · Current Opinion in Microbiology · doi:10.1016/j.mib.2003.10.002 · Cited by 201
Lobkovsky, E., Moews, P. C., Liu, H., Zhao, H., Frere, J. M., & Knox, J. R. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.11257 · Cited by 191
X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme
Pares, S., Mouz, N., Pétillot, Y., Hakenbeck, R., & Dideberg, O. (1996) · Nature Structural Biology · doi:10.1038/nsb0396-284 · Cited by 183
Extended broad spectrum β-lactamase in Klebsiella pneumoniae including resistance to cephamycins
Bauernfeind, A., Schweighart, S., & Chong, Y. (1989) · Infection · doi:10.1007/bf01650718 · Cited by 182
Role of Klebsiella pneumoniae LamB Porin in Antimicrobial Resistance
García-Sureda, L., Juan, C., Doménech-Sánchez, A., & Albertí, S. (2011) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01441-10 · Cited by 182
Filipe, S. R., & Tomasz, A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.080067697 · Cited by 177
Mechanism of acyl transfer by the class A serine β-lactamase of Streptomyces albus G
Lamotte-Brasseur, J., Dive, G., Dideberg, O., Charlier, P., Frère, J. M., & Ghuysen, J. M. (1991) · Biochemical Journal · doi:10.1042/bj2790213 · Cited by 173
β‐Lactamase of Bacillus licheniformis 749/C at 2 Å resolution
Moews, P. C., Knox, J. R., Dideberg, O., Charlier, P., & Frère, J. (1990) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340070205 · Cited by 173
Targeted gene evolution in Escherichia coli using a highly error-prone DNA polymerase I
Camps, M., Naukkarinen, J., Johnson, B. P., & Loeb, L. A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1333928100 · Cited by 169
Antibiotic-induced lateral transfer of antibiotic resistance
HASTINGS, P., ROSENBERG, S., & SLACK, A. (2004) · Trends in Microbiology · doi:10.1016/j.tim.2004.07.003 · Cited by 168
On functional and structural heterogeneity of VIM-type metallo-beta-lactamases
Docquier, J.-D. (2003) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkg067 · Cited by 167
Wu, S. W., de Lencastre, H., & Tomasz, A. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.8.2417-2424.2001 · Cited by 167
Kyriacou, S. V., Brownlow, W. J., & Xu, X. N. (2003) · Biochemistry · doi:10.1021/bi0351110 · Cited by 165
Young, K. D. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03607.x · Cited by 162
Crystal structure of the class D beta-lactamase OXA-10.
Strynadka, N. C. J., Paetzel, M., Danel, F., de Castro, L., Mosimann, S. C., & Page, M. G. P. (2000) · Nature Structural Biology · doi:10.1038/79688 · Cited by 161
On the evolution of functional secondary metabolites (natural products)
Stone, M. J., & Williams, D. H. (1992) · Molecular Microbiology · doi:10.1111/j.1365-2958.1992.tb00834.x · Cited by 161
Several distinct localization patterns for penicillin‐binding proteins in Bacillus subtilis
Scheffers, D., Jones, L. J. F., & Errington, J. (2004) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03854.x · Cited by 158
Barlow, M., & Hall, B. G. (2002) · Journal of Molecular Evolution · doi:10.1007/s00239-002-2328-y · Cited by 158
Origin and impact of plasmid-mediated extended-spectrum beta-lactamases
Philippon, A., Arlet, G., & Lagrange, P. H. (1994) · European Journal of Clinical Microbiology & Infectious Diseases · doi:10.1007/bf02390681 · Cited by 156
Jones, R. N., Marshall, S. A., Pfaller, M. A., Wilke, W. W., Hollis, R. J., Erwin, M. E., Edmond, M. B., & Wenzel, R. P. (1997) · Diagnostic Microbiology and Infectious Disease · doi:10.1016/s0732-8893(97)00115-6 · Cited by 153
Fitness Cost of SCC mec and Methicillin Resistance Levels in Staphylococcus aureus
Ender, M., Holmes, N., Adhikari, R. P., & Berger‐Bächi, B. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.6.2295-2297.2004 · Cited by 153
Prediction of Mechanisms of Action of Antibacterial Compounds by Gene Expression Profiling
Hutter, B., Schaab, C., Albrecht, S., Borgmann, M., Brunner, N. A., Freiberg, C., Ziegelbauer, K. B., Rock, C. O., Ivanov, I., & Loferer, H. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.8.2838-2844.2004 · Cited by 153
The evolutionary role of secondary metabolites — a review
Maplestone, R. A., Stone, M. J., & Williams, D. H. (1992) · Gene · doi:10.1016/0378-1119(92)90553-2 · Cited by 152
Yano, H., Kuga, A., Okamoto, R., Kitasato, H., Kobayashi, T., & Inoue, M. (2001) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.45.5.1343-1348.2001 · Cited by 152
Role of Klebsiella pneumoniae OmpK35 Porin in Antimicrobial Resistance
Doménech-Sánchez, A., Martínez-Martínez, L., Hernández-Allés, S., del Carmen Conejo, M., Pascual, A., Tomás, J. M., Albertí, S., & Benedí, V. J. (2003) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.47.10.3332-3335.2003 · Cited by 151
Tertiary Structure of Staphylococcus aureus Cell Wall Murein
Dmitriev, B. A., Toukach, F. V., Holst, O., Rietschel, E., & Ehlers, S. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.21.7141-7148.2004 · Cited by 150
Maveyraud, L., Mourey, L., Kotra, L. P., Pédelacq, J. D., Guillet, V., Mobashery, S., & Samama, J. (1998) · Journal of the American Chemical Society · doi:10.1021/ja9818001 · Cited by 149
Self-citationReynolds, P. E., & Brown, D. F. J. (1985) · FEBS Letters · doi:10.1016/0014-5793(85)80036-3 · Cited by 148
Snyder, D. S., & McIntosh, T. J. (2000) · Biochemistry · doi:10.1021/bi000810n · Cited by 148
Rand, K. H., & Houck, H. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.8.2871-2875.2004 · Cited by 148
McKinney, T. K., Sharma, V. K., Craig, W. A., & Archer, G. L. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.23.6862-6868.2001 · Cited by 145
Toleman, M. A., Rolston, K. V., Jones, R. N., & Walsh, T. R. (2003) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.1.329-332.2004 · Cited by 143
Predicting the evolution of antibiotic resistance genes
Hall, B. G. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro888 · Cited by 142
Imtiaz, U., Billings, E. M., Knox, J. R., Manavathu, E. K., Lerner, S. A., & Mobashery, S. (1993) · Journal of the American Chemical Society · doi:10.1021/ja00064a003 · Cited by 138
Self-citationStructure-Based Approach for Binding Site Identification on AmpC β-Lactamase
Powers, R. A., & Shoichet, B. K. (2002) · Journal of Medicinal Chemistry · doi:10.1021/jm020002p · Cited by 138
Garcia-Saez, I., Hopkins, J., Papamicaël, C. A., Franceschini, N., Amicosante, G., Rossolini, G. M., Galleni, M., Frère, J., & Dideberg, O. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301062200 · Cited by 137
Okamoto, K., Gotoh, N., & Nishino, T. (2001) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.45.7.1964-1971.2001 · Cited by 137
Galleni, M., Amicosante, G., & Frère, J.-M. (1988) · Biochemical Journal · doi:10.1042/bj2550123 · Cited by 134
Molecular evolution of bacterial β-lactam resistance
Knox, J. R., Moews, P. C., & Frère, J. (1996) · Chemistry & Biology · doi:10.1016/s1074-5521(96)90182-9 · Cited by 132
Maveyraud, L., Golemi, D., Kotra, L. P., Tranier, S., Vakulenko, S. B., Mobashery, S., & Samama, J. (2000) · Structure · doi:10.1016/s0969-2126(00)00534-7 · Cited by 131
Self-citationGarcia-Saez, I., Mercuri, P. S., Papamicaël, C. A., Kahn, R., Frère, J.-M., Galleni, M., Rossolini, G. M., & Dideberg, O. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01271-8 · Cited by 131
A review of the antimicrobial activity of clavulanate
Finlay, J. (2003) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkg286 · Cited by 129
Poirel, L., Girlich, D., Naas, T., & Nordmann, P. (2001) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.45.2.447-453.2001 · Cited by 129
Héritier, C., Poirel, L., Aubert, D., & Nordmann, P. (2002) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.47.1.268-273.2003 · Cited by 129
β-Lactams in the New Millennium. Part-II: Cephems, Oxacephems, Penams and Sulbactam
Singh, G. S. (2004) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557043487547 · Cited by 129
Impact of Specific pbp5 Mutations on Expression of β-Lactam Resistance in Enterococcus faecium
Rice, L. B., Bellais, S., Carias, L. L., Hutton‐Thomas, R., Bonomo, R. A., Caspers, P., Page, M. G. P., & Gutmann, L. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.8.3028-3032.2004 · Cited by 128
Taking inventory: antibacterial agents currently at or beyond Phase 1
Bush, K., Macielag, M. J., & Weidner‐Wells, M. A. (2004) · Current Opinion in Microbiology · doi:10.1016/j.mib.2004.08.013 · Cited by 126
Rohrer, S., & Berger‐Bächi, B. (2003) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.47.3.837-846.2003 · Cited by 126
Nukaga, M., Mayama, K., Hujer, A. M., Bonomo, R. A., & Knox, J. R. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00210-9 · Cited by 123
Evolution of Multiresistance in Nontyphoid Salmonella Serovars from 1984 to 1998 in Argentina
Orman, B. E., Piñeiro, S. A., Arduino, S., Galas, M., Melano, R. G., Caffer, M. I., Sordelli, D. O., & Centrón, D. (2002) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.46.12.3963-3970.2002 · Cited by 123
New (and not so new) antibacterial targets – from where and when will the novel drugs come?
Projan, S. J. (2002) · Current Opinion in Pharmacology · doi:10.1016/s1471-4892(02)00197-2 · Cited by 122
Kaldalu, N., Mei, R., & Lewis, K. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.3.890-896.2004 · Cited by 122
Structure-Based Discovery of a Novel, Noncovalent Inhibitor of AmpC β-Lactamase
Powers, R. A., Morandi, F., & Shoichet, B. K. (2002) · Structure · doi:10.1016/s0969-2126(02)00799-2 · Cited by 121
Substrate-activated Zinc Binding of Metallo-β-lactamases
Wommer, S., Rival, S. G., Heinz, U., Galleni, M., Frère, J., Franceschini, N., Amicosante, G., Rasmussen, B. W., Bauer, R., & Adolph, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202467200 · Cited by 120
Thiomandelic Acid, a Broad Spectrum Inhibitor of Zinc β-Lactamases
Mollard, C., Moali, C., Papamicaël, C. A., Damblon, C., Vessilier, S., Amicosante, G., Schofield, C. J., Galleni, M., Frère, J., & Roberts, G. C. K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107054200 · Cited by 118
Malléa, M., Mahamoud, A., Chevalier, J., Alibert, S., Brouant, P., Barbe, J., & Pagès, J. (2003) · Biochemical Journal · doi:10.1042/bj20030963 · Cited by 117
Dynamics of the Lipopolysaccharide Assembly on the Surface of Escherichia c oli
Kotra, L. P., Golemi, D., Amro, N. A., Liu, G.-Y., & Mobashery, S. (1999) · Journal of the American Chemical Society · doi:10.1021/ja991374z · Cited by 116
Self-citationPowers, R. A., Caselli, E., Focia, P. J., Prati, F., & Shoichet, B. K. (2001) · Biochemistry · doi:10.1021/bi0109358 · Cited by 115
Damblon, C., Raquet, X., Lian, L., Lamotte‐Brasseur, J., Fonzé, E., Charlier, P., Roberts, G. C. K., & Frère, J.-M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.5.1747 · Cited by 114
Elucidation of the role of arginine-224 in the turnover processes of class A .beta.-lactamases
Zafaralla, G. C., Manavathu, E. K., Lerner, S. A., & Mobashery, S. (1992) · Biochemistry · doi:10.1021/bi00130a016 · Cited by 114
Self-citationNiemeyer, D. M., Pucci, M. J., Thanassi, J. A., Sharma, V. K., & Archer, G. L. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.18.5464-5471.1996 · Cited by 112
Luzzaro, F., Docquier, J., Colinon, C., et al. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.2.648-650.2004 · Cited by 109
High-Level β-Lactam Resistance Associated with Acquired Multidrug Resistance in Helicobacter pylori
Kwon, D. H., Dore, M. P., Kim, J. J., Kato, M., Lee, M., Wu, J., & Graham, D. Y. (2003) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.47.7.2169-2178.2003 · Cited by 107
Shimamura, T., Shimizu‐Ibuka, A., Fushinobu, S., Wakagi, T., Ishiguro, M., Ishii, Y., & Matsuzawa, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207884200 · Cited by 107
Active site restructuring regulates ligand recognition in class A penicillin-binding proteins
Machebœuf, P., Guilmi, A. M. D., Job, V., Vernet, T., Dideberg, O., & Dessen, A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407186102 · Cited by 107
Can better prescribing turn the tide of resistance?
Livermore, D. M. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro798 · Cited by 104
Chevalier, J., Bredin, J., Mahamoud, A., Malléa, M., Barbe, J., & Pagès, J. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.3.1043-1046.2004 · Cited by 104
Studies of the repressor (BlaI) of β‐lactamase synthesis in Staphylococcus aureus
Gregory, P. D., Lewis, R. A., Curnock, S. P., et al. (1997) · Molecular Microbiology · doi:10.1046/j.1365-2958.1997.4051770.x · Cited by 103
Sun, T., Nukaga, M., Mayama, K., Braswell, E. H., & Knox, J. R. (2003) · Protein Science · doi:10.1110/ps.0224303 · Cited by 102
Armand-Lefèvre, L., Leflon‐Guibout, V., Bredin, J., Barguellil, F., Amor, A., Pagès, J., & Nicolas-Chanoine, M.-H. (2003) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.47.3.1165-1168.2003 · Cited by 102
Schumacher, M. A., & Brennan, R. G. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03039.x · Cited by 101
Buynak, J. D. (2004) · Current Medicinal Chemistry · doi:10.2174/0929867043364847 · Cited by 99
Couto, I., Wu, S. W., Tomasz, A., & de LENCASTRE, H. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.2.645-653.2003 · Cited by 99
Middlemiss, J. K., & Poole, K. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.5.1258-1269.2004 · Cited by 99
Renau, T. E., Léger, R., FILONOVA, L. K., Flamme, E. M., Wang, M., Yen, R., Madsen, D., Griffith, D. E., Chamberland, S., Dudley, M. N., et al. (2003) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(03)00556-0 · Cited by 98
Patera, A., Blaszczak, L. C., & Shoichet, B. K. (2000) · Journal of the American Chemical Society · doi:10.1021/ja001676x · Cited by 98
Delaire, M., Labia, R., Samama, J., & Masson, J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36729-8 · Cited by 97
Multidrug-exporting secondary transporters
Murakami, S., & Yamaguchi, A. (2003) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(03)00109-x · Cited by 97
Crystal Structure of Wild-type Penicillin-binding Protein 5 from Escherichia coli
Nicholas, R. A., Krings, S., Tomberg, J., Nicola, G., & Davies, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m310177200 · Cited by 97
A 1.2-Å snapshot of the final step of bacterial cell wall biosynthesis
Lee, W., McDonough, M. A., Kotra, L. P., Li, Z., Silvaggi, N. R., Takeda, Y., Kelly, J. A., & Mobashery, S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.4.1427 · Cited by 97
Self-citationAntibacterials: are the new entries enough to deal with the emerging resistance problems?
Barrett, C. T., & Barrett, J. F. (2003) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2003.10.003 · Cited by 97
Integrons and β-lactamases—a novel perspective on resistance
Weldhagen, G. F. (2004) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2004.03.007 · Cited by 97
Sauvage, E., Kerff, F., Fonzé, E., Herman, R., Schoot, B. M., Marquette, J.-P., Taburet, Y., Prevost, D. D. C., Dumas, J., Leonard, G. A., et al. (2002) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-002-8500-0 · Cited by 96
Jumping the Barrier to β-Lactam Resistance in Staphylococcus aureus
Katayama, Y., Zhang, H.-Z., Hong, D. H., et al. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.18.5465-5472.2003 · Cited by 96
Structural Aspects for Evolution of β-Lactamases from Penicillin-Binding Proteins
Meroueh, S. O., Minasov, G., Lee, W., Shoichet, B. K., & Mobashery, S. (2003) · Journal of the American Chemical Society · doi:10.1021/ja034861u · Cited by 95
Self-citationSite-directed Mutagenesis of Glutamate 166 in Two β-Lactamases
Guillaume, G., Vanhove, M., Lamotte‐Brasseur, J., Ledent, P., Jamin, M., Joris, B., & Frère, J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.9.5438 · Cited by 94
Sifaoui, F., Arthur, M., Rice, L. B., & Gutmann, L. (2001) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.45.9.2594-2597.2001 · Cited by 94
Mutations in the Active Site of Penicillin-binding Protein PBP2x from Streptococcus pneumoniae
Mouz, N., Guilmi, A. M. D., Gordon, E. J., Hakenbeck, R., Dideberg, O., & Vernet, T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.27.19175 · Cited by 91
Smith, A. M., & Klugman, K. P. (2001) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.45.8.2393-2396.2001 · Cited by 91
SPENCER, J. M., Clarke, A. R., & Walsh, T. R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105550200 · Cited by 90
Experimental Prediction of the Natural Evolution of Antibiotic Resistance
Barlow, M., & Hall, B. G. (2003) · Genetics · doi:10.1093/genetics/163.4.1237 · Cited by 89
Mechanisms of Decreased Susceptibility to Cefpodoxime in Escherichia coli
Oliver, A., Weigel, L. M., Rasheed, J. K., McGowan, J. E., Raney, P. M., & Tenover, F. C. (2002) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.46.12.3829-3836.2002 · Cited by 88
Pernot, L., Chesnel, L., Gouëllec, A. L., Croizé, J., Vernet, T., Dideberg, O., & Dessen, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313492200 · Cited by 87
Molecular Evolution of a Class C β-Lactamase Extending Its Substrate Specificity
Nukaga, M., Haruta, S., Tanimoto, K., Kogure, K., Taniguchi, K., Tamaki, M., & Sawai, T. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.11.5729 · Cited by 87
Arbeloa, A., Hugonnet, J., Sentilhes, A., Josseaume, N., Dubost, L., Monsempès, C., Blanot, D., Brouard, J., & Arthur, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407149200 · Cited by 86
Nakayama, K., Ishida, Y., Ohtsuka, M., Kawato, H. C., Yoshida, K., Yokomizo, Y., Hosono, S., Ohta, T., Hoshino, K., Ishida, H., et al. (2003) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2003.07.024 · Cited by 86
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(2002) · Journal of Tropical Pediatrics · doi:10.1093/tropej/48.5.318 · Cited by 84
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Thomson, C. J., Power, E., Rübsamen‐Waigmann, H., & Labischinski, H. (2004) · Current Opinion in Microbiology · doi:10.1016/j.mib.2004.08.009 · Cited by 84
Kuzin, A. P., Nukaga, M., Nukaga, Y., Hujer, A. M., Bonomo, R. A., & Knox, J. R. (2001) · Biochemistry · doi:10.1021/bi0022745 · Cited by 83
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Freiberg, C., Brötz‐Oesterhelt, H., & Labischinski, H. (2004) · Current Opinion in Microbiology · doi:10.1016/j.mib.2004.08.010 · Cited by 83
A Structure-Based Analysis of the Inhibition of Class A .beta.-Lactamases by Sulbactam
Imtiaz, U., Billings, E. M., Knox, J. R., & Mobashery, S. (1994) · Biochemistry · doi:10.1021/bi00185a009 · Cited by 83
Self-citationPenicillin Target Enzyme and the Antibiotic Binding Site
Kelly, J. A., Moews, P. C., Knox, J. R., Frère, J., & Ghuysen, J. (1982) · Science · doi:10.1126/science.7123246 · Cited by 82
Shimizu‐Ibuka, A., Ishii, Y., Galleni, M., Ishiguro, M., Yamaguchi, K., Frère, J., Matsuzawa, H., & Sakai, H. (2003) · Biochemistry · doi:10.1021/bi0342822 · Cited by 82
High-Resolution X-ray Structure of an Acyl-Enzyme Species for the Class D OXA-10 β-Lactamase
Maveyraud, L., Golemi, D., Ishiwata, A., Meroueh, O., Mobashery, S., & Samama, J. (2002) · Journal of the American Chemical Society · doi:10.1021/ja016736t · Cited by 80
Self-citationHow β-Lactamases Have Driven Pharmaceutical Drug Discovery
Bush, K., & Mobashery, S. (1998) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-4897-3_5 · Cited by 79
Self-citationVenkatesan, A. M., Gu, Y., dos Santos, O., Abé, T., Agarwal, A. K., Yang, Y., Petersen, P. J., Weiss, W. J., Mansour, T. S., Nukaga, M., et al. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm049680x · Cited by 79
Gherman, B. F., Goldberg, S. D., Cornish, V. W., & Friesner, R. A. (2004) · Journal of the American Chemical Society · doi:10.1021/ja036879a · Cited by 79
Davies, C., White, S. W., & Nicholas, R. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m004471200 · Cited by 78
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García-Castellanos, R., Mallorquí-Fernández, G., Marrero, A., Potempa, J., Coll, M., & Gomis‐Rüth, F. X. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313123200 · Cited by 78
Melano, R. G. (2003) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkg281 · Cited by 78
Diffusion-limited component of reactions catalyzed by Bacillus cereus .beta.-lactamase I
Hardy, L. W., & Kirsch, J. F. (1984) · Biochemistry · doi:10.1021/bi00301a040 · Cited by 77
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Buynak, J. D., Chen, H., Vogeti, L., Gadhachanda, V. R., Buchanan, C. A., Palzkill, T. G., Shaw, R. W., SPENCER, J. M., & Walsh, T. R. (2004) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2003.12.037 · Cited by 77
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Metadata
- Authors
- Fisher, J. F., Meroueh, S. O., & Mobashery, S.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2005-02-01
- Volume
- 105
- Issue
- 2
- Pages
- 395-424
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W1987635163
- Cited by
- 913
- References
- 281
- FWCI
- 4.36
- Type
- journal article
- Language
- en
- Open access
- closed
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