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Cited by 189

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Thirteen posttranslational modifications convert a 14-residue peptide into the antibiotic thiocillin

Open access
Wieland Brown, Laura C., Acker, Michael G., Clardy, Jon, Walsh, Christopher T., Fischbach, Michael A·2009·Proceedings of the National Academy of Sciences

Abstract

The thiazolylpeptides are a family of >50 bactericidal antibiotics that block the initial steps of bacterial protein synthesis. Here, we report a biosynthetic gene cluster for thiocillin and establish that it, and by extension the whole class, is ribosomally synthesized. Remarkably, the C-terminal 14 residues of a 52-residue peptide precursor undergo 13 posttranslational modifications to give rise to thiocillin, making this antibiotic the most heavily posttranslationally-modified peptide known to date.

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Crossref · 10.1073/pnas.0900008106

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Metadata

Authors
Wieland Brown, L. C., Acker, M. G., Clardy, J., Walsh, C. T., & Fischbach, M. A.
Venue
Proceedings of the National Academy of Sciences
Published
2009-02-24
Volume
106
Issue
8
Pages
2549-2553
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2146630893
Cited by
189
References
2
FWCI
14.51
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Thirteen posttranslational modifications convert a 14-residue peptide into the antibiotic thiocillin. https://app.cochat.ai/papers/10.1073/pnas.0900008106
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Wieland Brown, L. C., Acker, M. G., Clardy, J., Walsh, C. T., & Fischbach, M. A. (2009). Thirteen posttranslational modifications convert a 14-residue peptide into the antibiotic thiocillin. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0900008106

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.