Bacteriocins—A viable alternative to antibiotics?
Abstract
Solutions are urgently required for the growing number of infections caused by antibiotic-resistant bacteria. Bacteriocins, which are antimicrobial peptides produced by certain bacteria, might warrant serious consideration as alternatives to traditional antibiotics. These molecules exhibit significant potency against other bacteria (including antibiotic-resistant strains), are stable and can have narrow or broad activity spectra. Bacteriocins can even be produced in situ in the gut by probiotic bacteria to combat intestinal infections. Although the application of specific bacteriocins might be curtailed by the development of resistance, an understanding of the mechanisms by which such resistance could emerge will enable researchers to develop strategies to minimize this potential problem.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Most bacteriocins produced by LAB, especially those that inhibit Gram-positive bacteria, exert their antimicrobial effects by forming pores in the membrane of target cells, thereby depleting the transmembrane potential and/or pH gradient, which eventually leads to loss of cell contents.
“Most bacteriocins produced by LAB, especially those that inhibit Gram-positive bacteria, exert their antimicrobial effects by forming pores in the membrane of target cells, thereby depleting the transmembrane potential and/or pH gradient, which eventually leads to loss of cell contents [187,188].”
From Lactic Acid Bacteria in Raw-Milk Cheeses: From Starter Cultures to Probiotic Functions (2022) · cites this paper as [187]
Purified bacteriocins are degraded by various proteolytic enzymes during passage through the gastrointestinal tract, whereas bacteriocins produced by probiotic bacteria in the gut can interact directly with pathogens.
“This is likely due to the fact that purified bacteriocins are degraded by various proteolytic enzymes during passage through the gastrointestinal tract. However, bacteriocins produced by probiotic bacteria in the gut can interact directly with pathogens. In this way, bacteriocins can be produced by probiotic bacteria in situ in the gut to combat intestinal infections [187].”
From Lactic Acid Bacteria in Raw-Milk Cheeses: From Starter Cultures to Probiotic Functions (2022) · cites this paper as [187]
Cites
Gut flora metabolism of phosphatidylcholine promotes cardiovascular disease
Wang, Z., Klipfell, E., Bennett, B. J., Koeth, R., Levison, B. S., DuGar, B., Feldstein, A. E., Britt, E. B., Fu, X., Chung, Y.-M., et al. (2011) · Nature · doi:10.1038/nature09922 · Cited by 5,597 · see citing works
Gut microbiota in health and disease
Sekirov, I., Russell, S. L., Antunes, L. C. M., & Finlay, B. B. (2010) · Physiological Reviews · doi:10.1152/physrev.00045.2009 · Cited by 4,182 · see citing works
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 · see citing works
Self-citationArnison, P. G., Bibb, M. J., Bierbaum, G., Bowers, A. A., Bugni, T. S., Bulaj, G. W., Camarero, J. A., Campopiano, D. J., Challis, G. L., Clardy, J., et al. (2012) · Natural Product Reports · doi:10.1039/c2np20085f · Cited by 2,065 · see citing works
Self-citationRNA therapeutics: beyond RNA interference and antisense oligonucleotides
Kole, R., Krainer, A. R., & Altman, S. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3625 · Cited by 1,152 · see citing works
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 · see citing works
Self-citationThe Continuing Story of Class IIa Bacteriocins
Drider, D., Fimland, G., Héchard, Y., McMullen, L. M., & Prévost, H. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00016-05 · Cited by 750 · see citing works
Shifting the balance: antibiotic effects on host–microbiota mutualism
Willing, B. P., Russell, S. L., & Finlay, B. B. (2011) · Nature Reviews Microbiology · doi:10.1038/nrmicro2536 · Cited by 747 · see citing works
Bacteriocin Production: a Probiotic Trait?
Dobson, A., Cotter, P. D., Ross, R. P., & Hill, C. (2011) · Applied and Environmental Microbiology · doi:10.1128/aem.05576-11 · Cited by 690 · see citing works
Self-citationPlant-Derived Antimicrobial Compounds: Alternatives to Antibiotics
Savoia, D. (2012) · Future Microbiology · doi:10.2217/fmb.12.68 · Cited by 624 · see citing works
Lantibiotics: Peptides of Diverse Structure and Function
Willey, J. M., & van der Donk, W. A. (2007) · Annual Review of Microbiology · doi:10.1146/annurev.micro.61.080706.093501 · Cited by 621 · see citing works
Bagley, M. C., Dale, J. W., Merritt, E. A., & Xiong, X. (2005) · Chemical Reviews · doi:10.1021/cr0300441 · Cited by 612 · see citing works
Rea, M. C., Sit, C. S., Clayton, E., O'Connor, P. M., Whittal, R. M., Zheng, J., Vederas, J. C., Ross, R. P., & Hill, C. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913554107 · Cited by 530 · see citing works
Self-citationLantibiotics: Mode of Action, Biosynthesis and Bioengineering
Bierbaum, G., & Sahl, H. (2009) · Current Pharmaceutical Biotechnology · doi:10.2174/138920109787048616 · Cited by 524 · see citing works
Cooper, M. A., & Shlaes, D. M. (2011) · Nature · doi:10.1038/472032a · Cited by 475 · see citing works
Li, Y., Xiang, Q., Zhang, Q., Huang, Y., & Su, Z. (2012) · Peptides · doi:10.1016/j.peptides.2012.07.001 · Cited by 463 · see citing works
Microcins, gene-encoded antibacterial peptides from enterobacteria
Duquesne, S., Destoumieux‐Garzón, D., Péduzzi, J., & Rebuffat, S. (2007) · Natural Product Reports · doi:10.1039/b516237h · Cited by 389 · see citing works
Stop the killing of beneficial bacteria
Blaser, M. J. (2011) · Nature · doi:10.1038/476393a · Cited by 383 · see citing works
Rea, M. C., Dobson, A., O'Sullivan, O., Crispie, F., Fouhy, F., Cotter, P. D., Shanahan, F., Kiely, B., Hill, C., & Ross, R. P. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1001224107 · Cited by 377 · see citing works
Self-citationCommon mechanisms of target cell recognition and immunity for class II bacteriocins
Diep, D. B., Skaugen, M., Salehian, Z., Holo, H., & Nes, I. F. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608775104 · Cited by 374 · see citing works
Antibiotic treatment for Clostridium difficile -associated diarrhoea in adults
Nelson, R. L., Suda, K. J., & Evans, C. T. (2017) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd004610.pub5 · Cited by 368 · see citing works
Metagenome Mining Reveals Polytheonamides as Posttranslationally Modified Ribosomal Peptides
Freeman, M. F., Gurgui, C., Helf, M. J., Morinaka, B. I., Uria, A. R., Oldham, N. J., Sahl, H., Matsunaga, S., & Piel, J. (2012) · Science · doi:10.1126/science.1226121 · Cited by 351 · see citing works
Comparative Studies of Class IIa Bacteriocins of Lactic Acid Bacteria
Eijsink, V. G. H., Rødland, M. S., Middelhoven, P. H., Brurberg, M. B., & Nes, I. F. (1998) · Applied and Environmental Microbiology · doi:10.1128/aem.64.9.3275-3281.1998 · Cited by 324 · see citing works
Burton, J. P., Chilcott, C. N., Moore, C. J., Speiser, G., & Tagg, J. R. (2006) · Journal of Applied Microbiology · doi:10.1111/j.1365-2672.2006.02837.x · Cited by 307 · see citing works
O'Shea, E. F., Cotter, P. D., Stanton, C., Ross, R. P., & Hill, C. (2012) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2011.05.025 · Cited by 305 · see citing works
Cyanobactins—ribosomal cyclic peptides produced by cyanobacteria
Sivonen, K., Leikoski, N., Fewer, D. P., & Jokela, J. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2482-x · Cited by 275 · see citing works
Murphy, E. F., Cotter, P. D., Hogan, A., O’Sullivan, Ó., Joyce, A., Fouhy, F., Clarke, S. F., Marques, T. M., O’Toole, P. W., Stanton, C., et al. (2012) · Gut · doi:10.1136/gutjnl-2011-300705 · Cited by 273 · see citing works
Self-citationMaher, S., & McClean, S. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2006.01.012 · Cited by 265 · see citing works
Paik, S. H., Chakicherla, A. Y., & HANSEN, J. N. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.36.23134 · Cited by 263 · see citing works
Begley, M., Cotter, P. D., Hill, C., & Ross, R. P. (2009) · Applied and Environmental Microbiology · doi:10.1128/aem.00730-09 · Cited by 231 · see citing works
Self-citationMersacidin eradicates methicillin-resistant Staphylococcus aureus (MRSA) in a mouse rhinitis model
Kruszewska, D., Sahl, H., Bierbaum, G., Pag, U., Hynes, S. O., & Ljungh, Å. (2004) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkh387 · Cited by 231 · see citing works
Casey, P. G., Gardiner, G. E., Casey, G. D., Bradshaw, B., Lawlor, P. G., Lynch, P. B., Leonard, F. C., Stanton, C., Ross, R. P., Fitzgerald, G. F., et al. (2007) · Applied and Environmental Microbiology · doi:10.1128/aem.01840-06 · Cited by 226 · see citing works
Self-citationHåvarstein, L. S., Holo, H., & Nes, I. F. (1994) · Microbiology · doi:10.1099/13500872-140-9-2383 · Cited by 226 · see citing works
Sublancin is not a lantibiotic but an S-linked glycopeptide
Oman, T. J., Boettcher, J. M., Wang, H., Okalibe, X. N., & van der Donk, W. A. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.509 · Cited by 225 · see citing works
Bacteriophage therapy: potential uses in the control of antibiotic-resistant pathogens
Burrowes, B. H., Harper, D. R., Anderson, J., McConville, M., & Enright, M. C. (2011) · Expert Review of Anti-infective Therapy · doi:10.1586/eri.11.90 · Cited by 218 · see citing works
The spectrum of antimicrobial activity of the bacteriocin subtilosin A
Shelburne, C. E., An, F. Y., Dholpe, V., Ramamoorthy, A., Lopatin, D. E., & Lantz, M. S. (2006) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkl495 · Cited by 215 · see citing works
Meijerink, M., van Hemert, S., Taverne, N., Wels, M., de Vos, P., Bron, P. A., Savelkoul, H. F. J., van Bilsen, J. H. M., Kleerebezem, M., & Wells, J. M. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010632 · Cited by 207 · see citing works
Sutyak, K. E., Wirawan, R. E., Aroutcheva, A. A., & Chikindas, M. L. (2007) · Journal of Applied Microbiology · doi:10.1111/j.1365-2672.2007.03626.x · Cited by 207 · see citing works
van Hemert, S., Meijerink, M., Douwe Molenaar, B., Bron, P. A., de Vos, P., Kleerebezem, M., Wells, J. M., & Marco, M. L. (2010) · BMC Microbiology · doi:10.1186/1471-2180-10-293 · Cited by 196 · see citing works
Butcher, B. G., & Helmann, J. D. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05131.x · Cited by 190 · see citing works
Thirteen posttranslational modifications convert a 14-residue peptide into the antibiotic thiocillin
Brown, L. C. W., Acker, M. G., Clardy, J., Walsh, C. T., & Fischbach, M. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900008106 · Cited by 187 · see citing works
Genome mining for ribosomally synthesized natural products
Velásquez, J. E., & van der Donk, W. A. (2010) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2010.10.027 · Cited by 182 · see citing works
A new family of low molecular weight antibiotics from enterobacteria
Asensio, C., Pérez-Díaz, J. C., Martínez, M. C., et al. (1976) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(76)80264-1 · Cited by 181 · see citing works
Thiazole/oxazole-modified microcins: complex natural products from ribosomal templates
Melby, J. O., Nard, N. J., & Mitchell, D. A. (2011) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2011.02.027 · Cited by 180 · see citing works
Effect of Lactobacillus salivarius Bacteriocin Abp118 on the Mouse and Pig Intestinal Microbiota
Riboulet-Bisson, E., Sturme, M. H. J., Jeffery, I. B., Donnell, M. M. O., Neville, B. A., Forde, B. M., Claesson, M. J., Harris, H. M. B., Gardiner, G. E., Casey, P. G., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031113 · Cited by 178 · see citing works
Self-citationPiper, C., Draper, L. A., Cotter, P. D., Ross, R. P., & Hill, C. (2009) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkp221 · Cited by 172 · see citing works
Self-citationBaquero, F., & Moreno, F. (1984) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1984.tb01046.x · Cited by 172 · see citing works
Desriac, F., Defer, D., Bourgougnon, N., Brillet, B., Chevalier, P. L., & Fleury, Y. (2010) · Marine Drugs · doi:10.3390/md8041153 · Cited by 167 · see citing works
Cysteine S -glycosylation, a new post-translational modification found in glycopeptide bacteriocins
Stepper, J., Shastri, S., Loo, T. S., Preston, J. C., Novák, P., Man, P., Moore, C. H., Havlı́ček, V., Patchett, M. L., & Norris, G. E. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.01.023 · Cited by 167 · see citing works
Thomas, X., Destoumieux‐Garzón, D., Péduzzi, J., Afonso, C., Blond, A., Birlirakis, N., Goulard, C., Dubost, L., Thaï, R., Tabet, J., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400228200 · Cited by 166 · see citing works
Ribosomally Synthesized Thiopeptide Antibiotics Targeting Elongation Factor Tu
Morris, R. P., Leeds, J. A., Naegeli, H., Oberer, L., Memmert, K., Weber, E., LaMarche, M. J., Parker, C. N., Burrer, N., Esterow, S., et al. (2009) · Journal of the American Chemical Society · doi:10.1021/ja900488a · Cited by 166 · see citing works
Brumfitt, W. (2002) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkf190 · Cited by 166 · see citing works
Cox, C. R., Coburn, P. S., & Gilmore, M. S. (2005) · Current Protein and Peptide Science · doi:10.2174/1389203053027557 · Cited by 159 · see citing works
Hetz, C. A., Bono, M. R., Barros, L. F., & Lagos, R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052709699 · Cited by 157 · see citing works
Millette, M., Cornut, G., Dupont, C., Shareck, F., Archambault, D., & Lacroix, M. (2008) · Applied and Environmental Microbiology · doi:10.1128/aem.02150-07 · Cited by 153 · see citing works
Collins, B., Curtis, N. J., Cotter, P. D., Hill, C., & Ross, R. P. (2010) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00503-10 · Cited by 153 · see citing works
Self-citationAspartyl-tRNA Synthetase Is the Target of Peptide Nucleotide Antibiotic Microcin C
Metlitskaya, A. Z., Kazakov, T., Kommer, A., Pavlova, O., Prætorius-Ibba, M., Ibba, M., Krasheninnikov, I. A., Kolb, V. A., Khmel, I. A., & Severinov, K. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513174200 · Cited by 151 · see citing works
To protect peptide pharmaceuticals against peptidases
Rink, R., Arkema-Meter, A., Baudoin, I., Post, E., Kuipers, A., Nelemans, S. A., Akanbi, M. H. J., & Moll, G. N. (2010) · Journal of Pharmacological and Toxicological Methods · doi:10.1016/j.vascn.2010.02.010 · Cited by 148 · see citing works
Mutations of Bacterial RNA Polymerase Leading to Resistance to Microcin J25
Yuzenkova, J., Delgado, M. A., Nechaev, S., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209425200 · Cited by 147 · see citing works
Gotteland, M., Andrews, M., Toledo, M., Muñoz, L. A., Cáceres, P., Anziani, A., Wittig, E., Speisky, H., & Salazar, G. (2008) · Nutrition · doi:10.1016/j.nut.2008.01.007 · Cited by 146 · see citing works
Mersacidin, a new antibiotic from Bacillus In vitro and in vivo antibacterial activity.
Chatterjee, S., CHATTERJEE, D. K., Jani, R. H., et al. (1992) · The Journal of Antibiotics · doi:10.7164/antibiotics.45.839 · Cited by 144 · see citing works
Activity of nisin against Streptococcus pneumoniae, in vitro, and in a mouse infection model
Goldstein, B. P. (1998) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/42.2.277 · Cited by 142 · see citing works
Lantibiotics from Geobacillus thermodenitrificans
Garg, N., Tang, W., Goto, Y., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1116815109 · Cited by 141 · see citing works
Märki, F., Hänni, E., Fredenhagen, A., & van Oostrum, J. (1991) · Biochemical Pharmacology · doi:10.1016/0006-2952(91)90604-4 · Cited by 139 · see citing works
Claesen, J., & Bibb, M. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008608107 · Cited by 139 · see citing works
Destoumieux‐Garzón, D., Duquesne, S., Péduzzi, J., et al. (2005) · Biochemical Journal · doi:10.1042/bj20042107 · Cited by 135 · see citing works
Kjos, M., Borrero, J., Opsata, M., Birri, D. J., Holo, H., Cintas, L. M., Snipen, L. G., Hernández, P. E., Nes, I. F., & Diep, D. B. (2011) · Microbiology · doi:10.1099/mic.0.052571-0 · Cited by 133 · see citing works
Sandiford, S. K., & Upton, M. (2011) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.05397-11 · Cited by 131 · see citing works
Dabour, N., Zihler, A., Kheadr, E., Lacroix, C., & Fliss, I. (2009) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2009.05.005 · Cited by 128 · see citing works
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 · see citing works
Fimland, G., Johnsen, L., Axelsson, L. T., Brurberg, M. B., Nes, I. F., Eijsink, V. G. H., & Nissen-Meyer, J. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.9.2643-2648.2000 · Cited by 127 · see citing works
Genetically modified Streptococcus mutans for the prevention of dental caries
Hillman, J. D. (2002) · Springer eBooks · doi:10.1007/978-94-017-2029-8_25 · Cited by 125 · see citing works
Mechanisms of Resistance to Bacteriocins Targeting the Mannose Phosphotransferase System
Kjos, M., Nes, I. F., & Diep, D. B. (2011) · Applied and Environmental Microbiology · doi:10.1128/aem.02602-10 · Cited by 122 · see citing works
Dual antibacterial mechanisms of nisin Z against Gram-positive and Gram-negative bacteria
Kuwano, K., Tanaka, N., Shimizu, T., Nagatoshi, K., Nou, S., & Sonomoto, K. (2005) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2005.08.010 · Cited by 119 · see citing works
The Escherichia coli Yej Transporter Is Required for the Uptake of Translation Inhibitor Microcin C
Новикова, М. А., Metlitskaya, A. Z., Datsenko, K. A., Kazakov, T., Kazakov, A. S., Wanner, B. L., & Severinov, K. (2007) · Journal of Bacteriology · doi:10.1128/jb.01028-07 · Cited by 118 · see citing works
Discovery of Medically Significant Lantibiotics
Piper, C., Cotter, P. D., Ross, R. P., & Hill, C. (2009) · Current Drug Discovery Technologies · doi:10.2174/157016309787581075 · Cited by 117 · see citing works
Self-citationSun, Z., Zhong, J., Liang, X., Liu, J., Chen, X., & Huan, L. (2009) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01382-08 · Cited by 117 · see citing works
Bacteriocins to control Campylobacter spp. in poultry—A review
Ea, S., & Stern, N. J. (2010) · Poultry Science · doi:10.3382/ps.2010-00659 · Cited by 116 · see citing works
Transcriptome Analysis Reveals Mechanisms by Which Lactococcus lactis Acquires Nisin Resistance
Kramer, N. E., van Hijum, S. A. F. T., Knol, J., Kok, J., & Kuipers, O. P. (2006) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.50.5.1753-1761.2006 · Cited by 116 · see citing works
Walsh, M. C., Gardiner, G. E., Hart, O. M., Lawlor, P. G., Daly, M., Lynch, B., Richert, B. T., Radcliffe, J. S., Giblin, L. M., Hill, C., et al. (2008) · FEMS Microbiology Ecology · doi:10.1111/j.1574-6941.2008.00454.x · Cited by 113 · see citing works
Self-citationNisin F in the treatment of respiratory tract infections caused byStaphylococcus aureus
de Kwaadsteniet, M., ten Doeschate, K., & Dicks, L. M. T. (2008) · Letters in Applied Microbiology · doi:10.1111/j.1472-765x.2008.02488.x · Cited by 112 · see citing works
Shanahan, F. (2010) · Gastroenterology · doi:10.1053/j.gastro.2010.10.025 · Cited by 104 · see citing works
Blay, G. L., Lacroix, C., Zihler, A., & Fliss, I. (2007) · Letters in Applied Microbiology · doi:10.1111/j.1472-765x.2007.02178.x · Cited by 104 · see citing works
Wang, H., Fewer, D. P., & Sivonen, K. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022384 · Cited by 104 · see citing works
Antibacterial and Antitumorigenic Properties of Microcin E492, a Pore- Forming Bacteriocin
Lagos, R., Tello, M., Mercado, G., Garcia, V., & Monasterio, O. (2009) · Current Pharmaceutical Biotechnology · doi:10.2174/138920109787048643 · Cited by 104 · see citing works
NATURAL ANTIMICROBIALS AND THEIR ROLE IN VAGINAL HEALTH: A SHORT REVIEW.
Dover, S. E., Aroutcheva, A. A., Faro, S., & Chikindas, M. L. (2008) · PubMed · Cited by 103 · see citing works
Recent advances in thiopeptideantibiotic biosynthesis
Li, C., & Kelly, W. L. (2009) · Natural Product Reports · doi:10.1039/b922434c · Cited by 102 · see citing works
Genetically modified Streptococcus mutans for the prevention of dental caries
Hillman, J. D. (2002) · Antonie van Leeuwenhoek · doi:10.1023/a:1020695902160 · Cited by 99 · see citing works
In Vitro Mutasynthesis of Lantibiotic Analogues Containing Nonproteinogenic Amino Acids
Levengood, M. R., Knerr, P. J., Oman, T. J., et al. (2009) · Journal of the American Chemical Society · doi:10.1021/ja903239s · Cited by 95 · see citing works
Antimycobacterial activity of bacteriocins and their complexes with liposomes
Sosunov, V. V., Mischenko, V. V., Eruslanov, B. V., et al. (2007) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkm053 · Cited by 94 · see citing works
In vivo activity of mutacin B-Ny266
Mota‐Meira, M., Morency, H., & Lavoie, M. C. (2005) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dki295 · Cited by 94 · see citing works
AS-48 bacteriocin: close to perfection
Sánchez‐Hidalgo, M., Montalbán‐López, M., Cebrián, R., Valdivia, E., Martínez‐Bueno, M., & Maqueda, M. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0724-4 · Cited by 93 · see citing works
The Vancomycin−Nisin(1−12) Hybrid Restores Activity against Vancomycin Resistant Enterococci
Arnusch, C. J., Bonvin, A. M. J. J., Verel, A., et al. (2008) · Biochemistry · doi:10.1021/bi801597b · Cited by 91 · see citing works
The impact of antibiotics on the gut microbiota as revealed by high throughput DNA sequencing.
Cotter, P. D., Stanton, C., Ross, R. P., & Hill, C. (2012) · PubMed · Cited by 90 · see citing works
Self-citationDevelopment of Class IIa Bacteriocins as Therapeutic Agents
Lohans, C. T., & Vederas, J. C. (2011) · International Journal of Microbiology · doi:10.1155/2012/386410 · Cited by 89 · see citing works
Tagg, J. R. (2004) · PubMed · Cited by 86 · see citing works
Highly Diverse Cyanobactins in Strains of the Genus Anabaena
Leikoski, N., Fewer, D. P., Jokela, J., Wahlsten, M., Rouhiainen, L., & Sivonen, K. (2009) · Applied and Environmental Microbiology · doi:10.1128/aem.01061-09 · Cited by 86 · see citing works
The dawning of a ‘Golden era’ in lantibiotic bioengineering
Field, D., Hill, C., Cotter, P. D., et al. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07406.x · Cited by 86 · see citing works
Self-citationCastiglione, F., Cavaletti, L., Losi, D., et al. (2007) · Biochemistry · doi:10.1021/bi700131x · Cited by 85 · see citing works
Structure and Biosynthesis of the Antibiotic Bottromycin D
Hou, Y., Tianero, M. D. B., Kwan, J. C., et al. (2012) · Organic Letters · doi:10.1021/ol3022758 · Cited by 85 · see citing works
Efficacy of microcin J25 in biomatrices and in a mouse model of Salmonella infection
López, F. E., Vincent, P. A., Zenoff, A. M., Salomón, R. A., & Farı́as, R. N. (2007) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkm009 · Cited by 84 · see citing works
Haste, N. M., Thienphrapa, W., Tran, D. N., et al. (2012) · The Journal of Antibiotics · doi:10.1038/ja.2012.77 · Cited by 83 · see citing works
Zschüttig, A., Zimmermann, K., Blom, J., Goesmann, A., Pöhlmann, C., & Gunzer, F. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033351 · Cited by 81 · see citing works
Marsh, A. J., O’Sullivan, Ó., Ross, R. P., Cotter, P. D., & Hill, C. (2010) · BMC Genomics · doi:10.1186/1471-2164-11-679 · Cited by 81 · see citing works
Self-citationHillman, J. D., Mo, J., McDonell, E., Cvitkovitch, D. G., & Hillman, C. H. (2007) · Journal of Applied Microbiology · doi:10.1111/j.1365-2672.2007.03316.x · Cited by 80 · see citing works
The glucagon receptor antagonist BI‐32169 constitutes a new class of lasso peptides
Knappe, T. A., Linne, U., Xie, X., & Marahiel, M. A. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.12.046 · Cited by 78 · see citing works
Giacometti, A., Cirioni, O., Barchiesi, F., & Scalise, G. (2000) · Diagnostic Microbiology and Infectious Disease · doi:10.1016/s0732-8893(00)00175-9 · Cited by 77 · see citing works
Su, P., Henriksson, A., & Mitchell, H. M. (2007) · Journal of Applied Microbiology · doi:10.1111/j.1365-2672.2007.03469.x · Cited by 75 · see citing works
Escherichia coli Peptidase A, B, or N Can Process Translation Inhibitor Microcin C
Kazakov, T., Vondenhoff, G. H. M., Datsenko, K. A., et al. (2008) · Journal of Bacteriology · doi:10.1128/jb.01956-07 · Cited by 75 · see citing works
The action of the bacterial toxin, microcin B17, on DNA gyrase
Parks, W. M., Bottrill, A. R., Pierrat, O. A., Durrant, M. C., & Maxwell, A. (2007) · Biochimie · doi:10.1016/j.biochi.2006.12.005 · Cited by 75 · see citing works
Kazazić, M., Nissen-Meyer, J., & Fimland, G. (2002) · Microbiology · doi:10.1099/00221287-148-7-2019 · Cited by 75 · see citing works
Genome Mining for Radical SAM Protein Determinants Reveals Multiple Sactibiotic-Like Gene Clusters
Murphy, K., O’Sullivan, Ó., Rea, M. C., Cotter, P. D., Ross, R. P., & Hill, C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020852 · Cited by 74 · see citing works
Self-citationMajchrzykiewicz, J. A., Lubelski, J., Moll, G. N., et al. (2010) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00883-09 · Cited by 73 · see citing works
Murinda, S. E., Rashid, K. A., & Roberts, R. (2003) · Journal of Food Protection · doi:10.4315/0362-028x-66.5.847 · Cited by 72 · see citing works
Molecular Determinants of Microbial Resistance to Thiopeptide Antibiotics
Baumann, S., Schoof, S., Bolten, M., Haering, C., Takagi, M., Shin‐ya, K., & Arndt, H. (2010) · Journal of the American Chemical Society · doi:10.1021/ja909317n · Cited by 70 · see citing works
The Expanding Role of Lipid II as a Target for Lantibiotics
Martin, N. I., & Breukink, E. J. (2007) · Future Microbiology · doi:10.2217/17460913.2.5.513 · Cited by 70 · see citing works
Microcin C: Biosynthesis and Mechanisms of Bacterial Resistance
Severinov, K., & Nair, S. K. (2012) · Future Microbiology · doi:10.2217/fmb.11.148 · Cited by 70 · see citing works
McCormick, B. A., Franklin, D. P., Laux, D. C., et al. (1989) · Infection and Immunity · doi:10.1128/iai.57.10.3022-3029.1989 · Cited by 69 · see citing works
Structure and mode of action of microcin 7, an antibacterial peptide produced by Escherichia coli
Garcia-Bustos, J., Pezzi, N., & Méndez, E. (1985) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.27.5.791 · Cited by 69 · see citing works
Noll, K. S., Sinko, P. J., & Chikindas, M. L. (2010) · Probiotics and Antimicrobial Proteins · doi:10.1007/s12602-010-9061-4 · Cited by 68 · see citing works
Effective antibacterials: at what cost? The economics of antibacterial resistance and its control
White, A. R., Development, O. B. O. T. B. W. P. O. T. U. N. R. A. D. D. A., Blaser, M. J., et al. (2011) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkr260 · Cited by 68 · see citing works
Brand, A. M., de Kwaadsteniet, M., & Dicks, L. M. T. (2010) · Letters in Applied Microbiology · doi:10.1111/j.1472-765x.2010.02948.x · Cited by 65 · see citing works
del Castillo, F. J., del Castillo, I., & Moreno, F. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.6.2137-2140.2001 · Cited by 65 · see citing works
Niu, W.-W., & Neu, H. C. (1991) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.35.5.998 · Cited by 64 · see citing works
Zhang, C., Occi, J., Masurekar, P. S., Barrett, J. F., Zink, D. L., Smith, S. K., Onishi, R., Ha, S., Salazar, Ó., Genilloud, O., et al. (2008) · Journal of the American Chemical Society · doi:10.1021/ja803183u · Cited by 64 · see citing works
Nisin F-loaded brushite bone cement prevented the growth of Staphylococcus aureus in vivo
Staden, A. D. P. V., Brand, A. M., & Dicks, L. M. T. (2012) · Journal of Applied Microbiology · doi:10.1111/j.1365-2672.2012.05241.x · Cited by 64 · see citing works
The Structure and Biological Aspects of Peptide Antibiotic Microcin J25
Vincent, P. A., & Morero, R. D. (2009) · Current Medicinal Chemistry · doi:10.2174/092986709787458461 · Cited by 64 · see citing works
Morency, H., Mota‐Meira, M., LaPointe, G., et al. (2001) · Canadian Journal of Microbiology · doi:10.1139/cjm-47-4-322 · Cited by 63 · see citing works
Cross‐immunity and immune mimicry as mechanisms of resistance to the lantibiotic lacticin 3147
Draper, L. A., Grainger, K., Deegan, L. H., Cotter, P. D., Hill, C., & Ross, R. P. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06590.x · Cited by 63 · see citing works
Self-citationThe Synthesis of Active and Stable Diaminopimelate Analogues of the Lantibiotic Peptide Lactocin S
Ross, A. C., McKinnie, S. M. K., & Vederas, J. C. (2012) · Journal of the American Chemical Society · doi:10.1021/ja211088m · Cited by 63 · see citing works
Efficacy of LFF571 in a Hamster Model of Clostridium difficile Infection
Trzasko, A., Leeds, J. A., Præstgaard, J., LaMarche, M. J., & McKenney, D. (2012) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.06355-11 · Cited by 62 · see citing works
Kobayashi, Y., Ichioka, M., Hirose, T., et al. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.08.037 · Cited by 59 · see citing works
Leeds, J. A., Sachdeva, M., Mullin, S., et al. (2012) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.06354-11 · Cited by 58 · see citing works
Citron, D. M., Tyrrell, K. L., Merriam, C. V., & Goldstein, E. J. C. (2012) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.06305-11 · Cited by 57 · see citing works
Synthetic Microcin C Analogs Targeting Different Aminoacyl-tRNA Synthetases
de Vijver, P. V., Vondenhoff, G. H. M., Kazakov, T., et al. (2009) · Journal of Bacteriology · doi:10.1128/jb.00829-09 · Cited by 57 · see citing works
Bacteriocins Pep5 and Epidermin Inhibit Staphylococcus epidermidis Adhesion to Catheters
Fontana, M. B. C., Bastos, M. D. C. D. F., & Brandelli, A. (2006) · Current Microbiology · doi:10.1007/s00284-005-0152-5 · Cited by 56 · see citing works
ThioFinder: A Web-Based Tool for the Identification of Thiopeptide Gene Clusters in DNA Sequences
Li, J., Qu, X., He, X., Duan, L., Wu, G. G., Bi, D., Deng, Z., Liu, W., & Ou, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045878 · Cited by 56 · see citing works
Thiazomycins, Thiazolyl Peptide Antibiotics from Amycolatopsis fastidiosa
Zhang, C., Herath, K. B., Jayasuriya, H., Ondeyka, J. G., Zink, D. L., Occi, J., Birdsall, G., Venugopal, J., Ushio, M., Burgess, B., et al. (2009) · Journal of Natural Products · doi:10.1021/np800783b · Cited by 56 · see citing works
Destoumieux‐Garzón, D., Péduzzi, J., Thomas, X., Djédiat, C., & Rebuffat, S. (2006) · BioMetals · doi:10.1007/s10534-005-4452-9 · Cited by 55 · see citing works
O’Callaghan, J., Buttó, L. F., MacSharry, J. A., Nally, K., & O’Toole, P. W. (2012) · Applied and Environmental Microbiology · doi:10.1128/aem.00507-12 · Cited by 53 · see citing works
Morency, H., Mota‐Meira, M., LaPointe, G., et al. (2001) · Canadian Journal of Microbiology · doi:10.1139/w01-013 · Cited by 53 · see citing works
Genetic Analysis and Complete Primary Structure of Microcin L
Pons, A., Delalande, F., Duarte, M., Benoît, S., Lanneluc, I., Sablé, S., DORSSELAER, A. V., & Cottenceau, G. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.2.505-513.2004 · Cited by 52 · see citing works
Antibacterial Evaluations of Thiazomycin
Singh, S. B., Occi, J., Jayasuriya, H., et al. (2007) · The Journal of Antibiotics · doi:10.1038/ja.2007.71 · Cited by 51 · see citing works
Kouwen, T. R. H. M., Trip, E. N., Denham, E. L., et al. (2009) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00439-09 · Cited by 51 · see citing works
Synthesis of the Bacteriocin Glycopeptide Sublancin 168 and S-Glycosylated Variants
Hsieh, Y. S. Y., Wilkinson, B. L., O’Connell, M. R., et al. (2012) · Organic Letters · doi:10.1021/ol300557g · Cited by 49 · see citing works
Noll, K. S., Prichard, M. N., Khaykin, A., Sinko, P. J., & Chikindas, M. L. (2012) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.05861-11 · Cited by 48 · see citing works
Soudy, R., Wang, L., & Kaur, K. (2012) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.12.061 · Cited by 48 · see citing works
Generation of an actagardine A variant library through saturation mutagenesis
Boakes, S., Ayala, T., Herman, M., et al. (2012) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-012-4041-0 · Cited by 46 · see citing works
Enterocin CRL35 Inhibits Listeria monocytogenes in a Murine Model
Salvucci, E., Saavedra, L., Hebert, E. M., Haro, C., & Sesma, F. J. M. (2011) · Foodborne Pathogens and Disease · doi:10.1089/fpd.2011.0972 · Cited by 45 · see citing works
In vitro and in vivo antibacterial activity of cefoperazone.
Mitsuhashi, S., Minami, S., Matsubara, N., et al. (1980) · PubMed · Cited by 44 · see citing works
Antibiotic treatment forClostridium difficile-associated diarrhea in adults
Nelson, R. L., Kelsey, P., Leeman, H., Meardon, N., Patel, H., Paul, K., Rees, R. N., Taylor, B., Wood, E., & Malakun, R. (2011) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd004610.pub4 · Cited by 43 · see citing works
Synthesis of Trypsin-Resistant Variants of the Listeria -Active Bacteriocin Salivaricin P
O'Shea, E. F., O’Connor, P. M., Cotter, P. D., Ross, R. P., & Hill, C. (2010) · Applied and Environmental Microbiology · doi:10.1128/aem.00523-10 · Cited by 40 · see citing works
Self-citationSources of novel antibiotics—aside the common roads
Donadio, S., Maffioli, S. I., Monciardini, P., et al. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2877-8 · Cited by 39 · see citing works
Zamble, D. B., Miller, D. A., Heddle, J. G., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.141225698 · Cited by 38 · see citing works
Jasniewski, J., Cailliez‐Grimal, C., Chevalot, I., et al. (2009) · Food and Chemical Toxicology · doi:10.1016/j.fct.2009.01.025 · Cited by 35 · see citing works
Development of Innovative Pediocin PA-1 by DNA Shuffling among Class IIa Bacteriocins
Tominaga, T., & Hatakeyama, Y. (2007) · Applied and Environmental Microbiology · doi:10.1128/aem.00558-07 · Cited by 35 · see citing works
Nocathiacin analogs: Synthesis and antibacterial activity of novel water-soluble amides
Xu, L., Farthing, A. K., Dropinski, J. F., et al. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.04.144 · Cited by 33 · see citing works
Bernbom, N., Jelle, B., Brogren, C., et al. (2009) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2009.02.003 · Cited by 31 · see citing works
Řihakova, J., Cappelier, J.-M., Hue, I., et al. (2009) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00765-09 · Cited by 28 · see citing works
Nocek, B. P., Tikhonov, A., Babnigg, G., Gu, M., Zhou, M., Makarova, K. S., Vondenhoff, G. H. M., Aerschot, A. A. V., Kwon, K., Anderson, W. F., et al. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.04.011 · Cited by 26 · see citing works
Ea, S., Levchuk, V. P., Pokhilenko, V. D., et al. (2008) · Journal of Clinical Microbiology · doi:10.1128/jcm.01081-08 · Cited by 22 · see citing works
Su, P., Henriksson, A., & Mitchell, H. M. (2006) · Letters in Applied Microbiology · doi:10.1111/j.1472-765x.2006.02063.x · Cited by 21 · see citing works
Sensitization of Microcin J25-Resistant Strains by a Membrane-Permeabilizing Peptide
Pomares, M. F., Delgado, M. A., Corbalán, N. S., et al. (2010) · Applied and Environmental Microbiology · doi:10.1128/aem.00307-10 · Cited by 21 · see citing works
Salvucci, E., Hebert, E. M., Sesma, F. J. M., & Saavedra, L. (2010) · Letters in Applied Microbiology · doi:10.1111/j.1472-765x.2010.02879.x · Cited by 15 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Suez, J., Zmora, N., Zilberman-Schapira, G., Mor, U., Dori-Bachash, M., Bashiardes, S., Zur, M., Regev-Lehavi, D., Ben-Zeev Brik, R., Federici, S., et al. (2018) · Cell · doi:10.1016/j.cell.2018.08.047 · Cited by 1,184 · see citing works
The intestinal microbiota: Antibiotics, colonization resistance, and enteric pathogens
Kim, S., Covington, A., & Pamer, E. G. (2017) · Immunological Reviews · doi:10.1111/imr.12563 · Cited by 741 · see citing works
Bacteriocins of lactic acid bacteria: Extending the family
Alvarez-Sieiro, P., Montalbán-López, M., Mu, D., & Kuipers, O. P. (2016) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-016-7343-9 · Cited by 729 · see citing works
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 · see citing works
Application of bacteriocins and protective cultures in dairy food preservation
Silva, C. C. G., Silva, S. P. M., & Ribeiro, S. C. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.00594 · Cited by 601 · see citing works
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 · see citing works
Gut Microbiota and Colonization Resistance against Bacterial Enteric Infection
Ducarmon, Q. R., Zwittink, R. D., Hornung, B. V. H., van Schaik, W., Young, V. B., & Kuijper, E. J. (2019) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00007-19 · Cited by 566 · see citing works
The rumen microbiome: balancing food security and environmental impacts
Mizrahi, I., Wallace, R. J., & Moraïs, S. (2021) · Nature Reviews Microbiology · doi:10.1038/s41579-021-00543-6 · Cited by 490 · see citing works
Linares, D. M., Gómez, C., Renes, E., Fresno, J. M., Tornadijo, M. E., Ross, R. P., & Stanton, C. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.00846 · Cited by 335 · see citing works
Self-citationLactic Acid Bacteria in Raw-Milk Cheeses: From Starter Cultures to Probiotic Functions
Coelho, M. C., Malcata, F. X., & Silva, C. C. G. (2022) · Foods · doi:10.3390/foods11152276 · Cited by 276 · see citing works
“Most bacteriocins produced by LAB, especially those that inhibit Gram-positive bacteria, exert their antimicrobial effects by forming pores in the membrane of target cells, thereby depleting the transmembrane potential and/or pH gradient, which eventually leads to loss of cell contents [187,188].”
Large-Scale Analyses of Human Microbiomes Reveal Thousands of Small, Novel Genes
Sberro, H., Fremin, B. J., Zlitni, S., Edfors, F., Greenfield, N., Snyder, M. P., Pavlopoulos, G. A., Kyrpides, N. C., & Bhatt, A. S. (2019) · Cell · doi:10.1016/j.cell.2019.07.016 · Cited by 237 · see citing works
Pediococcus spp.: An important genus of lactic acid bacteria and pediocin producers
Porto, M. C. W., Kuniyoshi, T. M., Azevedo, P. O. S., Vitolo, M., & Oliveira, R. P. S. (2017) · Biotechnology Advances · doi:10.1016/j.biotechadv.2017.03.004 · Cited by 262 · see citing works
George, F., Daniel, C., Thomas, M., Singer, E., Guilbaud, A., Tessier, F. J., Revol-Junelles, A.-M., Borges, F., & Foligné, B. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02899 · Cited by 198 · see citing works
Effects of metabolites derived from gut microbiota and hosts on pathogens
Li, Z., Quan, G., Jiang, X., Yang, Y., Ding, X., Zhang, D., Wang, X., Hardwidge, P. R., Ren, W., & Zhu, G. (2018) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2018.00314 · Cited by 157 · see citing works
Linking microbiota to human diseases: a systems biology perspective
Wu, H., Tremaroli, V., & Bäckhed, F. (2015) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2015.09.011 · Cited by 150 · see citing works
Palmer, J. D., Piattelli, E., McCormick, B. A., Silby, M. W., Brigham, C. J., & Bucci, V. (2018) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.7b00114 · Cited by 133 · see citing works
Bacteriocin production: A relatively unharnessed probiotic trait?
Hegarty, J. W., Guinane, C. M., Ross, R. P., Hill, C., & Cotter, P. D. (2016) · F1000Research · doi:10.12688/f1000research.9615.1 · Cited by 141 · see citing works
Community Interactions of Oral Streptococci
Jakubovics, N. S., Yassin, S. A., & Rickard, A. H. (2014) · Advances in Applied Microbiology · doi:10.1016/b978-0-12-800261-2.00002-5 · Cited by 107 · see citing works
Pettigrew, M. M., Marks, L. R., Kong, Y., Gent, J. F., Roche-Hakansson, H., & Hakansson, A. P. (2014) · Infection and Immunity · doi:10.1128/iai.02225-14 · Cited by 110 · see citing works
Kaškonienė, V., Stankevičius, M., Bimbiraitė-Survilienė, K., Naujokaitytė, G., Šernienė, L., Mulkytė, K., Malakauskas, M., & Maruška, A. (2017) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-017-8088-9 · Cited by 99 · see citing works
Geldart, K. G., Kommineni, S., Forbes, M., Hayward, M., Dunny, G. M., Salzman, N. H., & Kaznessis, Y. N. (2018) · Bioengineering & Translational Medicine · doi:10.1002/btm2.10107 · Cited by 93 · see citing works
Antimicrobial antagonists against food pathogens: A bacteriocin perspective
O’Connor, P. M., Ross, R. P., Hill, C., & Cotter, P. D. (2015) · Current Opinion in Food Science · doi:10.1016/j.cofs.2015.01.004 · Cited by 88 · see citing works
Self-citationEnterocins: Classification, Synthesis, Antibacterial Mechanisms and Food Applications
Wu, Y., Pang, X., Wu, Y., Liu, X., & Zhang, X. (2022) · Molecules · doi:10.3390/molecules27072258 · Cited by 82 · see citing works
Jia, F.-F., Zhang, L.-J., Pang, X.-H., Gu, X.-X., Abdelazez, A., Liang, Y., Sun, S.-R., & Meng, X.-C. (2017) · Genomics · doi:10.1016/j.ygeno.2017.06.008 · Cited by 82 · see citing works
Zhang, D., Zhang, J., Kalimuthu, S., Liu, J., Song, Z.-M., He, B.-B., Cai, P., Zhong, Z., Feng, C., Neelakantan, P., et al. (2023) · Microbiome · doi:10.1186/s40168-023-01540-y · Cited by 72 · see citing works
“…peptides with antibacterial potential and are generally divided into three classes [class I, post ‐ translationally modified peptides (e.g., nisin and lactocillin); class II, small unmodified peptides (e.g., amylovorin L and crispacin A); class III, large, heat-labile peptides] [12, 13].”
Roles of the intestinal microbiota and microbial metabolites in acute GVHD
Lin, D., Hu, B., Li, P., Zhao, Y., Xu, Y., & Wu, D. (2021) · Experimental Hematology & Oncology · doi:10.1186/s40164-021-00240-3 · Cited by 71 · see citing works
Natural bacterial isolates as an inexhaustible source of new bacteriocins
Lozo, J., Topisirovic, L., & Kojic, M. (2021) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-020-11063-3 · Cited by 63 · see citing works
Vandera, E., Lianou, A., Kakouri, A., Feng, J., Koukkou, A.-I., & Samelis, J. (2017) · Journal of Food Protection · doi:10.4315/0362-028x.jfp-16-082 · Cited by 44 · see citing works
A Review of Research Conducted with Probiotic<i> E. coli</i> Marketed as Symbioflor
Beimfohr, C. (2016) · International Journal of Bacteriology · doi:10.1155/2016/3535621 · Cited by 30 · see citing works
Host Factors in Dysregulation of the Gut Barrier Function during Alcohol-Associated Liver Disease
Maccioni, L., Leclercq, I. A., Schnabl, B., & Stärkel, P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222312687 · Cited by 31 · see citing works
Angelescu, I.-R., Grosu-Tudor, S.-S., Cojoc, L.-R., Maria, G.-M., Chirițoiu, G. N., Munteanu, C. V. A., & Zamfir, M. (2022) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-022-03408-z · Cited by 26 · see citing works
Do Bacteria Provide an Alternative to Cancer Treatment and What Role Does Lactic Acid Bacteria Play?
Dicks, L. M. T., & Vermeulen, W. (2022) · Microorganisms · doi:10.3390/microorganisms10091733 · Cited by 25 · see citing works
- Authors
- Cotter, P. D., Ross, R. P., & Hill, C.
- Affiliations
- Teagasc - The Irish Agriculture and Food Development Authority (IE)
- University College Cork (IE)
- Corresponding author
- Cotter, Paul D.
- Ross, R. Paul
- Hill, Colin
- Venue
- Nature Reviews Microbiology
- Published
- 2012-12-24
- Volume
- 11
- Issue
- 2
- Pages
- 95-105
- ISSN
- 1740-1526 (ISSN-L)
- 1740-1534
- OpenAlex
- W1544835748
- Cited by
- 1,793
- References
- 164
- Citations by year
- 2026: 119 · 2025: 141 · 2024: 168 · 2023: 167 · 2022: 174 · 2021: 192 · 2020: 167 · 2019: 139 · 2018: 116 · 2017: 126 · 2016: 99 · 2015: 72 · 2014: 79 · 2013: 33
- FWCI
- 7.74
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Science Foundation Ireland
- Irish Research Council
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Physical Sciences › Environmental Science › Ecology › Bacteriophages and microbial interactions
- Keywords
- bacteriocins, antimicrobial peptides, antibiotic resistance, antibiotic alternatives, probiotic bacteria, gut microbiota, intestinal infection, resistance mechanisms
- MeSH terms
- Anti-Bacterial Agents, Bacteria, Bacteriocins, Drug Resistance, Bacterial
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