The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
Interactions of Bacterial Cationic Peptide Antibiotics with Outer and Cytoplasmic Membranes of Pseudomonas aeruginosa
Open accessAbstract
Polymyxins B and E1 and gramicidin S are bacterium-derived cationic antimicrobial peptides. The polymyxins were more potent than gramicidin S against Pseudomonas aeruginosa , with MICs of 0.125 to 0.25 and 8 μg/ml, respectively. These peptides differed in their affinities for binding to lipopolysaccharide, but all were able to permeabilize the outer membrane of wild-type P. aeruginosa PAO1 strain H103, suggesting differences in their mechanisms of self-promoted uptake. Gramicidin S caused rapid depolarization of the bacterial cytoplasmic membrane at concentrations at which no killing was observed within 30 min, whereas, conversely, the concentrations of the polymyxins that resulted in rapid killing resulted in minimal depolarization. These data indicate that the depolarization of the cytoplasmic membrane by these peptides did not correlate with bacterial cell lethality.
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Polymyxin and Related Peptide Antibiotics
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Self-citationInteraction of human defensins with Escherichia coli. Mechanism of bactericidal activity.
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Self-citationOuter membrane of Pseudomonas aeruginosa: heat- 2-mercaptoethanol-modifiable proteins
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Self-citationTHE PROPERTIES AND MODE OF ACTION OF THE POLYMYXINS
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Cited by
Mechanisms of Antimicrobial Peptide Action and Resistance
Yeaman, M. R., & Yount, N. Y. (2003) · Pharmacological Reviews · doi:10.1124/pr.55.1.2 · Cited by 3,001
Horcajada, J. P., Montero, M., Oliver, A., Sorlí, L., Luque, S., Gómez-Zorrilla, S., Benito, N., & Grau, S. (2019) · Clinical Microbiology Reviews · doi:10.1128/cmr.00031-19 · Cited by 961
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Metadata
- Authors
- Zhang, L., Dhillon, P., Yan, H., Farmer, S., & Hancock, R. E. W.
- Venue
- Antimicrobial Agents and Chemotherapy
- Publisher
- American Society for Microbiology
- Published
- 2000-12
- Volume
- 44
- Issue
- 12
- Pages
- 3317-3321
- ISSN
- 0066-4804 (ISSN-L)
- 1098-6596
- OpenAlex
- W2149623513
- Cited by
- 349
- References
- 16
- FWCI
- 4.43
- Type
- journal article
- Language
- en
- Open access
- green
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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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