Cited by 177RNA and protein synthesis mechanismsMicrobial Natural Products and BiosynthesisChemical Synthesis and Analysis

Translation and Protein Synthesis: Macrolides

Katz, Leonard, Ashley, Gary W.·2005·Chemical Reviews

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Crossref · 10.1021/cr030107f

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217 of 217 references verified0 citation errors · 0 not checkable

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  • In the presence of erythromycin or other macrolides, the ribosome stalls during translation of the leader peptide, allowing a conformational change in ermC mRNA that unmasks its ribosomal binding site and results in efficient translation of erm(C).

    “In the presence erythromycin (but also other macrolides), the ribosome stalls due to inhibition by the antibiotic during translation of the leader peptide allowing a conformational change in the ermC mRNA that unmasks its ribosomal binding site, resulting in efficient translation of erm(C) (65).”

    From Mechanisms of Antibiotic Resistance (2016) · cites this paper as [65]

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Authors
Katz, L., & Ashley, G. W.
Affiliations
Kosan Biosciences (United States) (US)
Venue
Chemical Reviews
Published
2005-01-11
Volume
105
Issue
2
Pages
499-528
ISSN
  • 0009-2665 (ISSN-L)
  • 1520-6890
OpenAlex
W2073353107
Cited by
177
References
217
Citations by year
2026: 5 · 2025: 4 · 2024: 8 · 2023: 5 · 2022: 4 · 2021: 8 · 2020: 12 · 2019: 8 · 2018: 10 · 2017: 4 · 2016: 12 · 2015: 8 · 2014: 5 · 2013: 8 · 2012: 7
FWCI
1.13
Type
journal article
Language
en
Open access
closed
Locations
  • Chemical Reviews (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Health Sciences › Medicine › Pharmacology › Microbial Natural Products and Biosynthesis
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
Keywords
macrolides, translation (biology), protein synthesis, ribosome, antibiotic mechanism of action, protein synthesis inhibition
MeSH terms
Anti-Bacterial Agents, Bacterial Proteins, Genetic Engineering, Protein Binding, Protein Synthesis Inhibitors, RNA, Bacterial, RNA, Ribosomal, Protein Biosynthesis, Molecular Structure, Macrolides

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