The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Alpha-helical cationic antimicrobial peptides: relationships of structure and function
Open accessAbstract
Antimicrobial peptides (AMPs), with their extraordinary properties, such as broad-spectrum activity, rapid action and difficult development of resistance, have become promising molecules as new antibiotics. Despite their various mechanisms of action, the interaction of AMPs with the bacterial cell membrane is the key step for their mode of action. Moreover, it is generally accepted that the membrane is the primary target of most AMPs, and the interaction between AMPs and eukaryotic cell membranes (causing toxicity to host cells) limits their clinical application. Therefore, researchers are engaged in reforming or de novo designing AMPs as a 'single-edged sword' that contains high antimicrobial activity yet low cytotoxicity against eukaryotic cells. To improve the antimicrobial activity of AMPs, the relationship between the structure and function of AMPs has been rigorously pursued. In this review, we focus on the current knowledge of α-helical cationic antimicrobial peptides, one of the most common types of AMPs in nature.
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Citations
Cites
Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
Brogden, K. A. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1098 · Cited by 5,829
The crisis in antibiotic resistance
Neu, H. C. (1992) · Science · doi:10.1126/science.257.5073.1064 · Cited by 2,834 · cited 2×
“(Neu, 1992); however, due to mutations and adaptation in bacteria, the traditional antibiotics eventually become inefficient (Bryan, 1988).”
Background
Cited by
Designing antimicrobial peptides: form follows function
Fjell, C. D., Hiss, J. A., Hancock, R. E. W., & Schneider, G. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3591 · Cited by 2,035
Bahar, A., & Ren, D. (2013) · Pharmaceuticals · doi:10.3390/ph6121543 · Cited by 1,351
Antimicrobial peptides for combating drug-resistant bacterial infections
Xuan, J., Feng, W., Wang, J., Wang, R., Zhang, B., Bo, L., Chen, Z.-S., Yang, H., & Sun, L. (2023) · Drug Resistance Updates · doi:10.1016/j.drup.2023.100954 · Cited by 665
Antimicrobial peptides (AMPs): A promising class of antimicrobial compounds
Erdem Büyükkiraz, M., & Kesmen, Z. (2022) · Journal of Applied Microbiology · doi:10.1111/jam.15314 · Cited by 454
Antimicrobial Peptides: An Update on Classifications and Databases
Bin Hafeez, A., Jiang, X., Bergen, P. J., & Zhu, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111691 · Cited by 341
Metadata
- Authors
- Huang, Y., Huang, J., & Chen, Y.
- Venue
- Protein & Cell
- Publisher
- Oxford University Press (OUP)
- Published
- 2010-02
- Volume
- 1
- Issue
- 2
- Pages
- 143-152
- ISSN
- 1674-800X (ISSN-L)
- 1674-8018
- OpenAlex
- W1973742248
- Cited by
- 575
- References
- 2
- FWCI
- 16.42
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Huang, Y., Huang, J., & Chen, Y. (2010). Alpha-helical cationic antimicrobial peptides: relationships of structure and function. Protein & Cell. https://doi.org/10.1007/s13238-010-0004-3
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
