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Bacterial Resistance to β-Lactam Antibiotics: Compelling Opportunism, Compelling Opportunity

Fisher, Jed F., Meroueh, Samy O., Mobashery, Shahriar·2005·Chemical Reviews

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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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Zhu, Y. F., Curran, I. H. A., Joris, B., Ghuysen, J., & Lampen, J. O. (1990) · Journal of Bacteriology · doi:10.1128/jb.172.2.1137-1141.1990 · Cited by 54
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Self-citation
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Yang, Y., Janota, K., Tabei, K., Huang, N., Siegel, M. M., Lin, Y., Rasmussen, B. A., & Shlaes, D. M. (2000) · PubMed · doi:10.1074/jbc.m002369200 · Cited by 43
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Hanique, S., Colombo, M.-L., Goormaghtigh, E., Soumillion, P., Frère, J., & Joris, B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313488200 · Cited by 35
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Williams, D. H., Stephens, E., & Zhou, M. (2003) · Chemical Communications · doi:10.1039/b305544m · Cited by 35
Acylating Agents as Enzyme Inhibitors and Understanding Their Reactivity for Drug Design
Sykes, N. O., Macdonald, S. J. F., & Page, M. I. (2002) · Journal of Medicinal Chemistry · doi:10.1021/jm0111245 · Cited by 32
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Rice, L. B. (2003) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2003.05.001 · Cited by 31
Roots: Selective reminiscences of β‐lactam antibiotics: Early research on penicillin and cephalosporins
Abraham, E. P. (1990) · BioEssays · doi:10.1002/bies.950121208 · Cited by 31
Reduced Outer Membrane Permeability of Escherichia coli O157:H7: Suggested Role of Modified Outer Membrane Porins and Theoretical Function in Resistance to Antimicrobial Agents
Martinez, M. B., Flickinger, M. C., Higgins, L., Krick, T. P., & Nelsestuen, G. L. (2001) · Biochemistry · doi:10.1021/bi0109515 · Cited by 30
Solution Structural Study of BlaI: Implications for the Repression of Genes Involved in β-Lactam Antibiotic Resistance
Melckebeke, H. V., Vreuls, C., Gans, P., Filée, P., Llabrès, G., Joris, B., & Simorre, J. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.09.005 · Cited by 29
Evidence of dimerisation among class D β-lactamases: kinetics of OXA-14 β-lactamase
Danel, F., Frère, J., & Livermore, D. M. (2001) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(01)00133-9 · Cited by 29
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Lakaye, B., Dubus, A., Joris, B., & Frère, J. (2002) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.46.9.2901-2907.2002 · Cited by 29
High-Throughput Screen for Inhibitors of Transglycosylase and/or Transpeptidase Activities of Escherichia coli Penicillin Binding Protein 1b
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Role of Ser-237 in the substrate specificity of the carbapenem-hydrolyzing class A β-lactamase Sme-1
Sougakoff, W., Naas, T., Nordmann, P., Collatz, E., & Jarlier, V. (1999) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00138-7 · Cited by 24
Is resistance futile?
McGeer, A., & Low, D. E. (2003) · Nature Medicine · doi:10.1038/nm0403-390 · Cited by 21
Structure of the First-Shell Active Site in Metallolactamase: Effect of Water Ligands
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Antibacterial Agents: Solutions for the Evolving Problems of Resistance
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Catalytic Mechanism of the Streptomyces K15 dd -Transpeptidase/Penicillin-Binding Protein Probed by Site-Directed Mutagenesis and Structural Analysis,
Rhazi, N., Charlier, P., Dehareng, D., Engher, D., Vermeire, M., Frère, J., Nguyen‐Distèche, M., & Fonzé, E. (2003) · Biochemistry · doi:10.1021/bi027256x · Cited by 18

Three Decades of β-Lactamase Inhibitors
Drawz, S. M., & Bonomo, R. A. (2010) · Clinical Microbiology Reviews · doi:10.1128/cmr.00037-09 · Cited by 1,709
Drug combinations: a strategy to extend the life of antibiotics in the 21st century
Tyers, M., & Wright, G. D. (2019) · Nature Reviews Microbiology · doi:10.1038/s41579-018-0141-x · Cited by 820
Antibiotic resistance is prevalent in an isolated cave microbiome
Bhullar, K., Waglechner, N., Pawlowski, A., Koteva, K., Banks, E. D., Johnston, M. D., Barton, H. A., & Wright, G. D. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034953 · Cited by 736
β-Lactam antibiotic resistance: a current structural perspective
Wilke, M. S., Lovering, A. L., & Strynadka, N. C. (2005) · Current Opinion in Microbiology · doi:10.1016/j.mib.2005.08.016 · Cited by 383
Covalent inhibitors design and discovery.
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See all 913

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
DOI: 10.1021/cr030102i
OpenAlex: W1987635163
Cited by: 913
References: 281
FWCI: 4.36
Type: journal article
Language: en
Open access: closed

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Bacterial Resistance to β-Lactam Antibiotics: Compelling Opportunism, Compelling Opportunity

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