The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Magainins and the disruption of membrane-linked free-energy transduction.
Open accessAbstract
Magainins, a family of positively charged peptides, are partly if not wholly responsible for antimicrobial activity in skin extracts of Xenopus laevis. We report here that members of the magainin family--i.e., the 21-amino acid peptide PGLa and the 23-amino acid peptide magainin 2 amide (PGSa)--dissipate the electric potential across various energy-transducing membranes and thus uncouple respiration from other free-energy-requiring processes. We propose that this is a likely mechanism for the antimicrobial effects of these compounds.
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Cites
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Cited by
Antimicrobial peptides of multicellular organisms
Zasloff, M. (2002) · Nature · doi:10.1038/415389a · Cited by 8,457
Self-citationAntimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
Brogden, K. A. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1098 · Cited by 5,829
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Mode of action of linear amphipathic α-helical antimicrobial peptides
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Metadata
- Authors
- Westerhoff, H. V., Juretić, D., Hendler, R. W., & Zasloff, M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1989-09
- Volume
- 86
- Issue
- 17
- Pages
- 6597-6601
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2014035436
- Cited by
- 290
- References
- 26
- FWCI
- 6.29
- Type
- journal article
- Language
- en
- Open access
- green
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- Westerhoff, H. V., Juretić, D., Hendler, R. W., & Zasloff, M. (1989). Magainins and the disruption of membrane-linked free-energy transduction. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.86.17.6597
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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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