The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils.
Open accessAbstract
Cytoplasmic granules of neutrophils store a variety of cationic polypeptides, which exert in vitro a potent antibacterial action and are potentially involved in host defense mechanisms. From an acid extract of bovine neutrophil granules we have purified over 2,000-fold a dodecapeptide exhibiting bactericidal activity against both Escherichia coli and Staphylococcus aureus at 10(-7)-10(-5) M concentration. The purification procedure involved only two steps of ion-exchange and reversed-phase chromatography. The peptide, named bactenecin, has the amino acid sequence, Arg-Leu-Cys-Arg-Ile-Val-Val-Ile-Arg-Val-Cys-Arg, maintained in a cyclic structure by a disulfide bond between the two cysteine residues. Computer modeling of the dodecapeptide resulted in a conformation in which the chain adopts an antiparallel extended structure forming a gamma turn at residue 7.
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Cited by
Antimicrobial peptides of multicellular organisms
Zasloff, M. (2002) · Nature · doi:10.1038/415389a · Cited by 8,457
Anti-microbial peptides: from invertebrates to vertebrates
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High-throughput generation of small antibacterial peptides with improved activity
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Metadata
- Authors
- Romeo, D., Skerlavaj, B., Bolognesi, M., & Gennaro, R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1988-07
- Volume
- 263
- Issue
- 20
- Pages
- 9573-9575
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1489585221
- Cited by
- 277
- References
- 13
- FWCI
- 5.20
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Romeo, D., Skerlavaj, B., Bolognesi, M., & Gennaro, R. (1988). Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)81553-3
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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