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Cited by 340

The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.

Rational Design of Peptide Antibiotics by Targeted Replacement of Bacterial and Fungal Domains

Stachelhaus, Torsten, Schneider, Axel, Marahiel, Mohamed A.·1995·Science

Abstract

Peptide synthetases involved in the nonribosomal synthesis of peptide secondary metabolites possess a highly conserved domain structure. The arrangement of these domains within the multifunctional enzymes determines the number and order of the amino acid constituents of the peptide product. A general approach has been developed for targeted substitution of amino acid-activating domains within the srfA operon, which encodes the protein templates for the synthesis of the lipopeptide antibiotic surfactin in Bacillus subtilis . Exchange of domain-coding regions of bacterial and fungal origin led to the construction of hybrid genes that encoded peptide synthetases with altered amino acid specificities and the production of peptides with modified amino acid sequences.

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Crossref · 10.1126/science.7604280

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Metadata

Authors
Stachelhaus, T., Schneider, A., & Marahiel, M. A.
Venue
Science
Published
1995-07-07
Volume
269
Issue
5220
Pages
69-72
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2089475202
Cited by
340
References
23
FWCI
16.12
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Rational Design of Peptide Antibiotics by Targeted Replacement of Bacterial and Fungal Domains. https://app.cochat.ai/papers/10.1126/science.7604280
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Stachelhaus, T., Schneider, A., & Marahiel, M. A. (1995). Rational Design of Peptide Antibiotics by Targeted Replacement of Bacterial and Fungal Domains. Science. https://doi.org/10.1126/science.7604280

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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.