RifamycinMode of Action, Resistance, and Biosynthesis
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTRifamycinMode of Action, Resistance, and BiosynthesisHeinz G. Floss and Tin-Wein YuView Author Information Department of Chemistry, Box 351700, University of Washington, Seattle, Washington 98195-1700 Cite this: Chem. Rev. 2005, 105, 2, 621–632Publication Date (Web):January 12, 2005Publication History Received10 May 2004Published online12 January 2005Published inissue 1 February 2005https://doi.org/10.1021/cr030112jCopyright © 2005 American Chemical SocietyRIGHTS & PERMISSIONSArticle Views7390Altmetric-Citations381LEARN 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 InReddit Read OnlinePDF (445 KB) Get e-AlertsSUBJECTS:Antimicrobial agents,Bacteria,Genetics,Monomers,Peptides and proteins Get e-Alerts
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These rpoB mutations result in decreased affinity of the drug for its target but usually spare the catalytic activity of the polymerase, permitting transcription to continue.
“Of note, while these mutations result in decreased affinity of the drug for its target, they usually spare the catalytic activity of the polymerase, permitting transcription to continue (58).”
From Mechanisms of Antibiotic Resistance (2016) · cites this paper as [58]
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- Authors
- Floss, H. G., & Yu, T.-W.
- Affiliations
- University of Washington (US)
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2005-01-12
- Volume
- 105
- Issue
- 2
- Pages
- 621-632
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2029869659
- Semantic Scholar
- 3fb314fdcf758438d613ea4e699c8187e7c4da3e
- Cited by
- 547
- References
- 124
- Citations by year
- 2026: 28 · 2025: 29 · 2024: 25 · 2023: 36 · 2022: 39 · 2021: 45 · 2020: 38 · 2019: 32 · 2018: 30 · 2017: 30 · 2016: 27 · 2015: 20 · 2014: 28 · 2013: 28 · 2012: 21
- FWCI
- 1.62
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Chemical Reviews (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (AI-20264, R01AI020264)
- Topics
- Health Sciences › Medicine › Pharmacology › Microbial Natural Products and Biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Medicine › Antibiotic Resistance in Bacteria
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- rifamycin, mechanism of action, antibiotic resistance, biosynthesis, rifamycin B, macrolide antibiotics, bacterial ribosome, antimicrobial agents
- MeSH terms
- Anti-Bacterial Agents, Genes, Bacterial, Models, Molecular, Mutation, Rifamycins, DNA-Directed RNA Polymerases, Molecular Structure, Drug Resistance, Bacterial, Actinobacteria
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