The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Antibacterial activities of bacteriocins: application in foods and pharmaceuticals
Open accessAbstract
Bacteriocins are a kind of ribosomal synthesized antimicrobial peptides produced by bacteria, which can kill or inhibit bacterial strains closely-related or non-related to produced bacteria, but will not harm the bacteria themselves by specific immunity proteins. Bacteriocins become one of the weapons against microorganisms due to the specific characteristics of large diversity of structure and function, natural resource, and being stable to heat. Many recent studies have purified and identified bacteriocins for application in food technology, which aims to extend food preservation time, treat pathogen disease and cancer therapy, and maintain human health. Therefore, bacteriocins may become a potential drug candidate for replacing antibiotics in order to treat multiple drugs resistance pathogens in the future. This review article summarizes different types of bacteriocins from bacteria. The latter half of this review focuses on the potential applications in food science and pharmaceutical industry.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Bacteriocins: Developing innate immunity for food
Cotter, P. D., Hill, C., & Ross, R. P. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1273 · Cited by 2,380
Bacteriocins: safe, natural antimicrobials for food preservation.
Cleveland, J., Montville, T. J., Nes, I. F., & Chikindas, M. L. (2001) · International Journal of Food Microbiology · doi:10.1016/s0168-1605(01)00560-8 · Cited by 1,835
Corr, S. C., Li, Y., Riedel, C. U., O'Toole, P. W., Hill, C., & Gahan, C. G. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700440104 · Cited by 853
Vassiliadis, G., Destoumieux-Garzón, D., Lombard, C., Rebuffat, S., & Peduzzi, J. (2010) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00744-09 · Cited by 128 · cited 2×
“…Linear peptides with post-translational modifications or not at C-terminal E492 7886 Klebsiella pneumoniae Pons et al., 2002 M 7284 Escherichia coli Vassiliadis et al., 2010 H47 4865 Escherichia coli Vassiliadis et al., 2010 Bacteriocins from gram-positive bacteria Unlike colicins from…”
Research works printed but not linked: 24
- Acuña, 2012, A new hybrid bacteriocin, Ent35-MccV, displays antimicrobial activity against pathogenic Gram-positive and Gram-negative bacteria, FEBS Open Bio, 2, 12, 10.1016/j.fob.2012.01.002 · DOI
- Akutsu, 1989, Molecular structure and immunity specificity of colicin E6, an evolutionary intermediate between E-group colicins and cloacin DF13, J. Bacteriol, 171, 6430, 10.1128/jb.171.12.6430-6436.1989 · DOI
- Allison, 1994, Expansion of bacteriocin activity and host range upon complementation of two peptides encoded within the lactacin F operon, J. Bacteriol, 176, 2235, 10.1128/jb.176.8.2235-2241.1994 · DOI
- Babasaki, 1985, Subtilosin A, a new antibiotic peptide produced by Bacillus subtilis 168: isolation, structural analysis, and biogenesis, J. Bacteriol, 98, 585
- Bernbom, 2006, Effects of Lactococcus lactis on composition of intestinal microbiota: role of nisin, Appl. Environ. Microbiol, 72, 239, 10.1128/AEM.72.1.239-244.2006 · DOI
- Bures, 1986, Colicinogeny in colorectal cancer, Neoplasma, 33, 233
- Burton, 2013, Persistence of the oral probiotic Streptococcus salivarius M18 is dose dependent and megaplasmid transfer can augment their bacteriocin production and adhesion characteristics, PLoS ONE, 8, e65991, 10.1371/journal.pone.0065991 · DOI
- Cascales, 2007, Colicin biology, Microbiol. Mol. Biol. Rev, 71, 158, 10.1128/MMBR.00036-06 · DOI · Paper page
- Center, 2013, Cancer Facts and Figures 2013
- Chak, 1991, Cloning and characterization of the ColE7 plasmid, J. Gen. Microbiol, 137, 91, 10.1099/00221287-137-1-91 · doi:10.1099/00221287-137-1-91
- Chatterjee, 1992, Mersacidin, a new antibiotic from Bacillus. Fermentation, isolation, purification and chemical characterization, J. Antibiot. (Tokyo), 45, 832, 10.7164/antibiotics.45.832 · DOI
- Chumchalová, 2003, Human tumor cells are selectively inhibited by colicins, Folia Microbiol. (Praha), 48, 111, 10.1007/BF02931286 · DOI
- Collin, 2013, Fragments of the bacterial toxin microcin B17 as gyrase poisons, PLoS ONE, 8, e61459, 10.1371/journal.pone.0061459 · doi:10.1371/journal.pone.0061459
- Corsini, 2010, Purification and characterization of the antimicrobial peptide microcin N, FEMS Microbiol. Lett, 312, 119, 10.1111/j.1574-6968.2010.02106.x · DOI
- Cotter, 2013, Bacteriocins—a viable alternative to antibiotics?, Nat. Rev. Microbiol, 11, 95, 10.1038/nrmicro2937 · DOI · Paper page
- Cursino, 2002, Recent updated aspects of colicins of Enterobacteriaceae, Braz. J. Microbiol, 33, 185, 10.1590/S1517-83822002000300001 · DOI
- Cursino, 2006, Exoproducts of the Escherichia coli strain H22 inhibiting some enteric pathogens both in vitro and in vivo, J. Appl. Microbiol, 100, 821, 10.1111/j.1365-2672.2006.02834.x · DOI
- Cutler, 2007, Dietary inclusion of colicin e1 is effective in preventing postweaning diarrhea caused by F18-positive Escherichia coli in pigs, Antimicrob. Agents Chemother, 51, 3830, 10.1128/AAC.00360-07 · doi:10.1128/aac.00360-07
- Dabour, 2009, In vivo study on the effectiveness of pediocin PA-1 and Pediococcus acidilactici UL5 at inhibiting Listeria monocytogenes, Int. J. Food Microbiol, 133, 225, 10.1016/j.ijfoodmicro.2009.05.005 · DOI
- Deegan, 2006, Bacteriocins: biological tools for bio-preservation and shelf-life extension, Int. Dairy J, 16, 1058, 10.1016/j.idairyj.2005.10.026 · DOI · Paper page
- de Lorenzo, 1985, Microcin E492, a low-molecular-weight peptide antibiotic which causes depolarization of the Escherichia coli cytoplasmic membrane, Antimicrob. Agents Chemother, 27, 666, 10.1128/AAC.27.4.666 · DOI
- Dimov, 2005, Bioactive peptides used by bacteria in the concurrence for the ecological niche: eneral classification and mode of action (overview), Biotechnol. Biotechnol. Eq, 3, 3, 10.1080/13102818.2005.10817185 · doi:10.1080/13102818.2005.10817185
- Dobson, 2012, Bacteriocin production: a probiotic trait?, Appl. Environ. Microbiol, 78, 1, 10.1128/AEM.05576-11 · DOI · Paper page
- Duquesne, 2007, Structural and functional diversity of microcins, gene-encoded antibacterial peptides from enterobacteria, J. Mol. Microbiol. Biotechnol, 13, 200, 10.1159/000104748 · DOI
Cited by
Biomedical applications of nisin
Shin, J. M., Gwak, J. W., Kamarajan, P., Fenno, J. C., Rickard, A. H., & Kapila, Y. L. (2016) · Journal of Applied Microbiology · doi:10.1111/jam.13033 · Cited by 607
The Genus Enterococcus: Between Probiotic Potential and Safety Concerns—An Update
Hanchi, H., Mottawea, W., Sebei, K., & Hammami, R. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.01791 · Cited by 569
Microcins mediate competition among Enterobacteriaceae in the inflamed gut
Sassone-Corsi, M., Nuccio, S.-P., Liu, H., Hernandez, D., Vu, C. T., Takahashi, A. A., Edwards, R. A., & Raffatellu, M. (2016) · Nature · doi:10.1038/nature20557 · Cited by 549
Bacteriocins as a new generation of antimicrobials: toxicity aspects and regulations
Soltani, S., Hammami, R., Cotter, P. D., Rebuffat, S., Said, L. B., Gaudreau, H., Bédard, F., Biron, E., Drider, D., & Fliss, I. (2021) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuaa039 · Cited by 544
Lactic Acid Bacteria: Food Safety and Human Health Applications
Ayivi, R. D., Gyawali, R., Krastanov, A., Aljaloud, S. O., Worku, M., Tahergorabi, R., Silva, R. C. D., & Ibrahim, S. A. (2020) · Dairy · doi:10.3390/dairy1030015 · Cited by 367
Metadata
- Authors
- Yang, S.-C., Lin, C.-H., Sung, C. T., & Fang, J.-Y.
- Venue
- Frontiers in Microbiology
- Publisher
- Frontiers Media SA
- Published
- 2014-05-26
- Volume
- 5
- Pages
- 241-241
- ISSN
- 1664-302X (ISSN-L)
- OpenAlex
- W2072465905
- Cited by
- 726
- References
- 4
- FWCI
- 23.64
- Type
- journal article
- Language
- en
- Open access
- gold
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Antibacterial activities of bacteriocins: application in foods and pharmaceuticals. https://app.cochat.ai/papers/10.3389/fmicb.2014.00241
- The paper
- Yang, S.-C., Lin, C.-H., Sung, C. T., & Fang, J.-Y. (2014). Antibacterial activities of bacteriocins: application in foods and pharmaceuticals. Frontiers in Microbiology. https://doi.org/10.3389/fmicb.2014.00241
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
