Bacteriocins: Classification, synthesis, mechanism of action and resistance development in food spoilage causing bacteria

Amphipathic, α-helical antimicrobial peptides

Tossi, A., Sandri, L., & Giangaspero, A. (2000) · Biopolymers · doi:10.1002/1097-0282(2000)55:1 · Cited by 1,245 · see citing works

Natural functions of lipopeptides from <i>Bacillus</i> and <i>Pseudomonas</i> : more than surfactants and antibiotics

Raaijmakers, J. M., De Bruijn, I., Nybroe, O., & Ongena, M. (2010) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2010.00221.x · Cited by 1,131 · see citing works

The 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

Lipopeptides as the Antifungal and Antibacterial Agents: Applications in Food Safety and Therapeutics

Meena, K. R., & Kanwar, S. S. (2015) · BioMed Research International · doi:10.1155/2015/473050 · Cited by 474 · see citing works

Lipopeptides from Bacillus and Paenibacillus spp.: A Gold Mine of Antibiotic Candidates

Cochrane, S. A., & Vederas, J. C. (2014) · Medicinal Research Reviews · doi:10.1002/med.21321 · Cited by 474 · see citing works

Bacteriocins from lactic acid bacteria: purification, properties and use as biopreservatives

Parada, J., Caron, C. R., Medeiros, A. B. P., & Soccol, C. R. (2007) · Brazilian Archives of Biology and Technology · doi:10.1590/s1516-89132007000300018 · Cited by 358 · see citing works

Production of class II bacteriocins by lactic acid bacteria; an example of biological warfare and communication

Eijsink, V. G. H., Axelsson, L. T., Diep, D. B., Håvarstein, L. S., Holo, H., & Nes, I. F. (2002) · Antonie van Leeuwenhoek · doi:10.1023/a:1020582211262 · Cited by 352 · see citing works

Mode of action of modified and unmodified bacteriocins from Gram-positive bacteria

Héchard, Y., & Sahl, H. (2002) · Biochimie · doi:10.1016/s0300-9084(02)01417-7 · Cited by 340 · see citing works

Identification of FtsW as a transporter of lipid‐linked cell wall precursors across the membrane

Mohammadi, T., van Dam, V., Sijbrandi, R., Vernet, T., Zapun, A., Bouhss, A., Bruin, M. D.-D., Nguyen‐Distèche, M., KRUIJFF, B. D., & Breukink, E. J. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.61 · Cited by 314 · see citing works

The antimicrobial effect of oregano essential oil, nisin and their combination against Salmonella Enteritidis in minced sheep meat during refrigerated storage

Govaris, A., Σολωμάκος, Ν., Pexara, A., & Chatzopoulou, P. S. (2009) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2009.12.017 · Cited by 314 · see citing works

Control of Biofilm Formation: Antibiotics and Beyond

Algburi, A., Comito, N., Kashtanov, D. O., Dicks, L. M. T., & Chikindas, M. L. (2016) · Applied and Environmental Microbiology · doi:10.1128/aem.02508-16 · Cited by 310 · see citing works

Enterolysin A, a Cell Wall-Degrading Bacteriocin from Enterococcus faecalis LMG 2333

Nilsen, T., Nes, I. F., & Holo, H. (2003) · Applied and Environmental Microbiology · doi:10.1128/aem.69.5.2975-2984.2003 · Cited by 308 · see citing works

Antibacterial activity of plant essential oils and extracts: The role of thyme essential oil, nisin, and their combination to control Listeria monocytogenes inoculated in minced fish meat

Abdollahzadeh, E., Rezaei, M., & Hosseini, H. (2013) · Food Control · doi:10.1016/j.foodcont.2013.07.004 · Cited by 298 · see citing works

The antimicrobial effect of thyme essential oil, nisin, and their combination against Listeria monocytogenes in minced beef during refrigerated storage

Σολωμάκος, Ν., Govaris, A., Koidis, P., et al. (2007) · Food Microbiology · doi:10.1016/j.fm.2007.07.002 · Cited by 286 · see citing works

Antagonistic Activity of <i>Lactobacillus plantarum</i> C11: Two New Two-Peptide Bacteriocins, Plantaricins EF and JK, and the Induction Factor Plantaricin A

Anderssen, E. L., Diep, D. B., Nes, I. F., Eijsink, V. G. H., & Nissen-Meyer, J. (1998) · Applied and Environmental Microbiology · doi:10.1128/aem.64.6.2269-2272.1998 · Cited by 280 · see citing works

Bacteriocins: mechanism of membrane insertion and pore formation

Moll, G. N., Konings, W. N., & Driessen, A. J. M. (1999) · Antonie van Leeuwenhoek · doi:10.1023/a:1002002718501 · Cited by 276 · see citing works

Characterization of the genetic locus responsible for the production of ABP-118, a novel bacteriocin produced by the probiotic bacterium Lactobacillus salivarius subsp. salivarius UCC118 The GenBank accession number for the sequence reported in this paper is AF408405.

Flynn, S., van Sinderen, D., Thornton, G., Holo, H., Nes, I. F., & Collins, J. K. (2002) · Microbiology · doi:10.1099/00221287-148-4-973 · Cited by 264 · see citing works

A Functional dlt Operon, Encoding Proteins Required for Incorporation of d -Alanine in Teichoic Acids in Gram-Positive Bacteria, Confers Resistance to Cationic Antimicrobial Peptides in Streptococcus pneumoniae

Kovács, M., Halfmann, A., Fedtke, I., Heintz, M., Peschel, A., Vollmer, W., Hakenbeck, R., & Brückner, R. (2006) · Journal of Bacteriology · doi:10.1128/jb.00336-06 · Cited by 235 · see citing works

The generation of nisin variants with enhanced activity against specific Gram‐positive pathogens

Field, D., Connor, P. M. O., Cotter, P. D., et al. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06279.x · Cited by 230 · see citing works

Nisin ZP, a Bacteriocin and Food Preservative, Inhibits Head and Neck Cancer Tumorigenesis and Prolongs Survival

Kamarajan, P., Hayami, T., Matte, B., Liu, Y., Danciu, T., Ramamoorthy, A., Worden, F., Kapila, S., & Kapila, Y. (2015) · PLOS ONE · doi:10.1371/journal.pone.0131008 · Cited by 214 · see citing works

Fighting biofilms with lantibiotics and other groups of bacteriocins

Mathur, H., Field, D., Rea, M. C., Cotter, P. D., Hill, C., & Ross, R. P. (2018) · npj Biofilms and Microbiomes · doi:10.1038/s41522-018-0053-6 · Cited by 213 · see citing works

The MprF protein is required for lysinylation of phospholipids in listerial membranes and confers resistance to cationic antimicrobial peptides (CAMPs) on Listeria monocytogenes

Thedieck, K., Hain, T., Mohamed, W. A., Tindall, B. J., Nimtz, M., Chakraborty, T., Wehland, J., & Jänsch, L. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05452.x · Cited by 209 · see citing works

Bioengineered Nisin A Derivatives with Enhanced Activity against Both Gram Positive and Gram Negative Pathogens

Field, D., Begley, M., O’Connor, P. M., Daly, K. M., Hugenholtz, F., Cotter, P. D., Hill, C., & Ross, R. P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046884 · Cited by 207 · see citing works

Peptide pheromone-dependent regulation of antimicrobial peptide production in Gram-positive bacteria: a case of multicellular behavior

Kleerebezem, M., & Quadri, L. E. N. (2001) · Peptides · doi:10.1016/s0196-9781(01)00493-4 · Cited by 202 · see citing works

Amino acid-containing membrane lipids in bacteria

Geiger, O., González‐Silva, N., López-Lara, I. M., & Sohlenkamp, C. (2009) · Progress in Lipid Research · doi:10.1016/j.plipres.2009.08.002 · Cited by 194 · see citing works

Resistance to bacteriocins produced by Gram-positive bacteria

Bastos, M. D. C. D. F., Coelho, M. L. V., & Santos, O. C. D. S. (2014) · Microbiology · doi:10.1099/mic.0.082289-0 · Cited by 181 · see citing works

Sensitivity and Resistance of Listeria monocytogenes ATCC 19115, Scott A, and UAL500 to Nisin

Harris, L. J., Fleming, H. P., & Klaenhammer, T. R. (1991) · Journal of Food Protection · doi:10.4315/0362-028x-54.11.836 · Cited by 181 · see citing works

Bacteriocins of Lactic Acid Bacteria in Combination Have Greater Antibacterial Activity

Hanlin, M. B., Kalchayanand, N., Ray, P., et al. (1993) · Journal of Food Protection · doi:10.4315/0362-028x-56.3.252 · Cited by 174 · see citing works

A comparison of the activities of lacticin 3147 and nisin against drug-resistant Staphylococcus aureus and Enterococcus species

Piper, 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

The Potential of Antimicrobial Peptides as Biocides

Laverty, G., Gorman, S. P., & Gilmore, B. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12106566 · Cited by 171 · see citing works

The Two-Peptide Class II Bacteriocins: Structure, Production, and Mode of Action

Oppegård, C., Rogne, P., Emanuelsen, L., Kristiansen, P. E., Fimland, G., & Nissen-Meyer, J. (2007) · Microbial Physiology · doi:10.1159/000104750 · Cited by 170 · see citing works

Virulence Factors of Enterococcus faecalis and Enterococcus faecium Blood Culture Isolates

Elsner, H. ‐., Sobottka, I., Mack, D., Laufs, R., Claussen, M., & Wirth, R. (2000) · European Journal of Clinical Microbiology & Infectious Diseases · doi:10.1007/s100960050007 · Cited by 168 · see citing works

The Lantibiotic Peptide Labyrinthopeptin A1 Demonstrates Broad Anti-HIV and Anti-HSV Activity with Potential for Microbicidal Applications

Férir, G., Petrova, M., Andreï, G., Huskens, D., Hoorelbeke, B., Snoeck, R., Vanderleyden, J., Balzarini, J. M., Bartoschek, S., Brönstrup, M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0064010 · Cited by 167 · see citing works

The dlt operon confers resistance to cationic antimicrobial peptides in Clostridium difficile

McBride, S. M., & Sonenshein, A. L. (2011) · Microbiology · doi:10.1099/mic.0.045997-0 · Cited by 160 · see citing works

The Cyclic Antibacterial Peptide Enterocin AS-48: Isolation, Mode of Action, and Possible Food Applications

Burgos, M. J. G., Pulido, R. P., Aguayo, M. D. C. L., Gálvez, A., & Lucas, R. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms151222706 · Cited by 154 · see citing works

Prokaryotic Antimicrobial Peptides

(2011) · Springer eBooks · doi:10.1007/978-1-4419-7692-5 · Cited by 153 · see citing works

Antiadhesive activity of the biosurfactant pseudofactin II secreted by the Arctic bacterium Pseudomonas fluorescensBD5

Janek, T., Łukaszewicz, M., & Krasowska, A. (2012) · BMC Microbiology · doi:10.1186/1471-2180-12-24 · Cited by 149 · see citing works

In silico identification of bacteriocin gene clusters in the gastrointestinal tract, based on the Human Microbiome Project’s reference genome database

Walsh, C. J., Guinane, C. M., Hill, C., Ross, R. P., O’Toole, P. W., & Cotter, P. D. (2015) · BMC Microbiology · doi:10.1186/s12866-015-0515-4 · Cited by 146 · see citing works

Bacterial lipid diversity

López-Lara, I. M., & Geiger, O. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.10.007 · Cited by 141 · see citing works

Nisin Resistance of Streptococcus bovis

Mantovani, H. C., & Russell, J. B. (2001) · Applied and Environmental Microbiology · doi:10.1128/aem.67.2.808-813.2001 · Cited by 140 · see citing works

Classification of Bacteriocins from Gram-Positive Bacteria

Rea, M. C., Ross, R. P., Cotter, P. D., & Hill, C. (2011) · Springer eBooks · doi:10.1007/978-1-4419-7692-5_3 · Cited by 129 · see citing works

Correlation of Daptomycin Resistance in a Clinical Staphylococcus aureus Strain with Increased Cell Wall Teichoic Acid Production and d -Alanylation

Bertsche, U., Weidenmaier, C., Kuehner, D., et al. (2011) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01226-10 · Cited by 128 · see citing works

Characterization of Garvicin ML, a Novel Circular Bacteriocin Produced by Lactococcus garvieae DCC43, Isolated from Mallard Ducks ( Anas platyrhynchos )

Borrero, J., Brede, D. A., Skaugen, M., et al. (2010) · Applied and Environmental Microbiology · doi:10.1128/aem.01173-10 · Cited by 122 · see citing works

Cell-surface alterations in class IIa bacteriocin-resistant Listeria monocytogenes strains

Vadyvaloo, V., Arous, S., Gravesen, A., Héchard, Y., Chauhan-Haubrock, R., Hastings, J. W., & Rautenbach, M. (2004) · Microbiology · doi:10.1099/mic.0.27059-0 · Cited by 120 · see citing works

Membranes of Class IIa Bacteriocin-Resistant Listeria monocytogenes Cells Contain Increased Levels of Desaturated and Short-Acyl-Chain Phosphatidylglycerols

Vadyvaloo, V., Hastings, J. W., van der Merwe, M. J., & Rautenbach, M. (2002) · Applied and Environmental Microbiology · doi:10.1128/aem.68.11.5223-5230.2002 · Cited by 119 · see citing works

Biodiversity of Lactic Acid Bacteria

Liu, W., Pang, H., Zhang, H., & Cai, Y. (2014) · Springer eBooks · doi:10.1007/978-94-017-8841-0_2 · Cited by 119 · see citing works

Nisin Resistance in Clostridium botulinum Spores and Vegetative Cells

Mazzotta, A. S., Crandall, A. D., & Montville, T. J. (1997) · Applied and Environmental Microbiology · doi:10.1128/aem.63.7.2654-2659.1997 · Cited by 114 · see citing works

Teichoic Acid Is an Essential Polymer in Bacillus subtilis That Is Functionally Distinct from Teichuronic Acid

Bhavsar, A. P., Erdman, L. K., Schertzer, J. W., & Brown, E. D. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.23.7865-7873.2004 · Cited by 111 · see citing works

Increased membrane surface positive charge and altered membrane fluidity leads to cationic antimicrobial peptide resistance in Enterococcus faecalis

Kumariya, R., Sood, S. K., Rajput, Y. S., Saini, N. K., & Garsa, A. K. (2015) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2015.03.007 · Cited by 99 · see citing works

Class III bacteriocin Helveticin-M causes sublethal damage on target cells through impairment of cell wall and membrane

Sun, Z., Wang, X., Zhang, X., Wu, H., Zou, Y., Li, P., Sun, C., Xu, W., Liu, F., & Wang, D. (2018) · Journal of Industrial Microbiology & Biotechnology · doi:10.1007/s10295-018-2008-6 · Cited by 98 · see citing works

Class I/Class IIa bacteriocin cross-resistance phenomenon in Listeria monocytogenes

Naghmouchi, K., Kheadr, E., Lacroix, C., et al. (2007) · Food Microbiology · doi:10.1016/j.fm.2007.03.012 · Cited by 96 · see citing works

Plant essential oils and allied volatile fractions as multifunctional additives in meat and fish-based food products: a review

Patel, S. V. (2015) · Food Additives & Contaminants Part A · doi:10.1080/19440049.2015.1040081 · Cited by 94 · see citing works

Nisin is an effective inhibitor of Clostridium difficile vegetative cells and spore germination

Lay, C., Dridi, L., Bergeron, M. G., Ouellette, M., & Fliss, I. (2015) · Journal of Medical Microbiology · doi:10.1099/jmm.0.000202 · Cited by 94 · see citing works

The Maltose ABC Transporter in Lactococcus lactis Facilitates High-Level Sensitivity to the Circular Bacteriocin Garvicin ML

Gabrielsen, C., Brede, D. A., Hernández, P. E., Nes, I. F., & Diep, D. B. (2012) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00314-12 · Cited by 92 · see citing works

Nisin–curvaticin 13 combinations for avoiding the regrowth of bacteriocin resistant cells of Listeria monocytogenes ATCC 15313

Bouttefroy, A., & Millière, J.-B. (2000) · International Journal of Food Microbiology · doi:10.1016/s0168-1605(00)00372-x · Cited by 90 · see citing works

Interactions between Pairs of Bacteriocins From Lactic Bacteria

Mulet-Powell, N., Lacoste-Armynot, A.-M., Viñas, M., et al. (1998) · Journal of Food Protection · doi:10.4315/0362-028x-61.9.1210 · Cited by 83 · see citing works

Synergistic effect of gamma (γ)-irradiation and microencapsulated antimicrobials against Listeria monocytogenes on ready-to-eat (RTE) meat

Huq, T., Vu, K. D., Riedl, B., Bouchard, J., & Lacroix, M. (2014) · Food Microbiology · doi:10.1016/j.fm.2014.09.013 · Cited by 82 · see citing works

In vivo activity of Nisin A and Nisin V against Listeria monocytogenesin mice

Campion, A., Casey, P. G., Field, D., Cotter, P. D., Hill, C., & Ross, R. P. (2013) · BMC Microbiology · doi:10.1186/1471-2180-13-23 · Cited by 82 · see citing works

A large scale prediction of bacteriocin gene blocks suggests a wide functional spectrum for bacteriocins

Morton, J. T., Freed, S. D., Lee, S. W., & Friedberg, I. (2015) · BMC Bioinformatics · doi:10.1186/s12859-015-0792-9 · Cited by 80 · see citing works

Focal Targeting of the Bacterial Envelope by Antimicrobial Peptides

Rashid, R., Veleba, M., & Kline, K. A. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2016.00055 · Cited by 80 · see citing works

The combined effect of nisin, leucocin F10, pH, NaCl and EDTA on the survival of Listeria monocytogenes in broth

Parente, E., Giglio, M. A., Ricciardi, A., & Clementi, F. (1998) · International Journal of Food Microbiology · doi:10.1016/s0168-1605(98)00021-x · Cited by 79 · see citing works

Class IIa bacteriocin resistance in Enterococcus faecalis V583: The mannose PTS operon mediates global transcriptional responses

Opsata, M., Nes, I. F., & Holo, H. (2010) · BMC Microbiology · doi:10.1186/1471-2180-10-224 · Cited by 76 · see citing works

Three Distinct Two-Component Systems Are Involved in Resistance to the Class I Bacteriocins, Nukacin ISK-1 and Nisin A, in Staphylococcus aureus

Kawada‐Matsuo, M., Yoshida, Y., Zendo, T., Nagao, J.-I., Oogai, Y., Nakamura, Y., Sonomoto, K., Nakamura, N., & Komatsuzawa, H. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069455 · Cited by 75 · see citing works

Microcin Amyloid Fibrils A Are Reservoir of Toxic Oligomeric Species

Shahnawaz, M., & Soto, C. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.282533 · Cited by 75 · see citing works

Biosynthesis of Lipoteichoic Acid in Lactobacillus rhamnosus : Role of DltD in d -Alanylation

Debabov, D. V., Kiriukhin, M. Y., & Neuhaus, F. C. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.10.2855-2864.2000 · Cited by 75 · see citing works

The Bactericidal Activity of Pediocin PA-1 Is Specifically Inhibited by a 15-mer Fragment That Spans the Bacteriocin from the Center toward the C Terminus

Fimland, G., Jack, R. W., Jung, G., et al. (1998) · Applied and Environmental Microbiology · doi:10.1128/aem.64.12.5057-5060.1998 · Cited by 75 · see citing works

Functional analysis of promoters involved in quorum sensing‐based regulation of bacteriocin production in Lactobacillus

Risøen, P. A., Brurberg, M. B., Eijsink, V. G. H., et al. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.02029.x · Cited by 74 · see citing works

Evaluation of the probiotic potential and effect of encapsulation on survival for Lactobacillus plantarum ST16Pa isolated from papaya

Todorov, S. D., LeBlanc, J. G., & Franco, B. D. G. D. M. (2011) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-011-0895-z · Cited by 74 · see citing works

Alanyl-Phosphatidylglycerol and Lysyl-Phosphatidylglycerol Are Translocated by the Same MprF Flippases and Have Similar Capacities To Protect against the Antibiotic Daptomycin in Staphylococcus aureus

Slavetinsky, C. J., Peschel, A., & Ernst, C. M. (2012) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00370-12 · Cited by 74 · see citing works

The Lipid-Modifying Multiple Peptide Resistance Factor Is an Oligomer Consisting of Distinct Interacting Synthase and Flippase Subunits

Ernst, C. M., Kuhn, S., Slavetinsky, C. J., Krismer, B., Heilbronner, S., Gekeler, C., Kraus, D., Wagner, S., & Peschel, A. (2015) · mBio · doi:10.1128/mbio.02340-14 · Cited by 71 · see citing works

Gassericin A: a circular bacteriocin produced by Lactic acid bacteria Lactobacillus gasseri

Pandey, N., Malik, R. K., Kaushik, J. K., et al. (2013) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-013-1368-3 · Cited by 69 · see citing works

Bacterial spores in food: how phenotypic variability complicates prediction of spore properties and bacterial behavior

Eijlander, R. T., Abee, T., & Kuipers, O. P. (2010) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2010.11.009 · Cited by 69 · see citing works

Bactofencin A, a New Type of Cationic Bacteriocin with Unusual Immunity

O'Shea, E. F., O’Connor, P. M., O’Sullivan, Ó., Cotter, P. D., Ross, R. P., & Hill, C. (2013) · mBio · doi:10.1128/mbio.00498-13 · Cited by 69 · see citing works

Nisin and ALTATM 2341 inhibit the growth ofListeria monocytogeneson smoked salmon packaged under vacuum or 100% CO2

Szabó, É., & Cahill, M. E. (1999) · Letters in Applied Microbiology · doi:10.1046/j.1365-2672.1999.00547.x · Cited by 69 · see citing works

Structure–Function Analysis of the Two-Peptide Bacteriocin Plantaricin EF

Ekblad, B., Kyriakou, P. K., Oppegård, C., Nissen-Meyer, J., Kaznessis, Y. N., & Kristiansen, P. E. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00588 · Cited by 69 · see citing works

Collapse of the proton motive force in Listeria monocytogenes caused by a bacteriocin produced by Pediococcus acidilactici

Christensen, D. P., & Hutkins, R. W. (1992) · Applied and Environmental Microbiology · doi:10.1128/aem.58.10.3312-3315.1992 · Cited by 67 · see citing works

Saturation Mutagenesis of Lysine 12 Leads to the Identification of Derivatives of Nisin A with Enhanced Antimicrobial Activity

Molloy, E. M., Field, D., Connor, P. M. O., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0058530 · Cited by 64 · see citing works

Effect of prebiotics on bacteriocin production and cholesterol lowering activity of Pediococcus acidilactici LAB 5

Mandal, V., Sen, S. K., & Mandal, N. C. (2009) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-009-0085-4 · Cited by 58 · see citing works

Effect of Enterocin CRL35 on Listeria monocytogenes cell membrane

Minahk, C. J., Farías, M. E., Sesma, F. J. M., et al. (2000) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2000.tb09362.x · Cited by 57 · see citing works

Botulism, where are we now?

Zhang, J.-C., Sun, L., & Nie, Q. (2010) · Clinical Toxicology · doi:10.3109/15563650.2010.535003 · Cited by 55 · see citing works

Insights into the Mode of Action of the Sactibiotic Thuricin CD

Mathur, H., Fallico, V., O’Connor, P. M., Rea, M. C., Cotter, P. D., Hill, C., & Ross, R. P. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.00696 · Cited by 55 · see citing works

Identification of genes essential for anaerobic growth of Listeria monocytogenes

Müller-Herbst, S., Wüstner, S., Mühlig, A., et al. (2014) · Microbiology · doi:10.1099/mic.0.075242-0 · Cited by 53 · see citing works

Characterization of Enterococcus faecium mutants resistant to mundticin KS, a class IIa bacteriocin

Sakayori, Y., Muramatsu, M., Hanada, S., et al. (2003) · Microbiology · doi:10.1099/mic.0.26435-0 · Cited by 48 · see citing works

LAB Bacteriocins Controlling the Food Isolated (Drug-Resistant) Staphylococci

Perales-Adán, J., Rubiño, S., Martínez‐Bueno, M., et al. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.01143 · Cited by 47 · see citing works

Purification of leucocin A for use on wieners to inhibit Listeria monocytogenes in the presence of spoilage organisms

Balay, D. R., Dangeti, R. V., Kaur, K., & McMullen, L. M. (2017) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2017.05.016 · Cited by 46 · see citing works

Structures of two bacterial resistance factors mediating tRNA-dependent aminoacylation of phosphatidylglycerol with lysine or alanine

Hebecker, S., Krausze, J., Hasenkampf, T., Schneider, J. R., Groenewold, M. K., Reichelt, J., Jahn, D., Heinz, D. W., & Moser, J. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1511167112 · Cited by 45 · see citing works

Anti-staphylococcal activities of lysostaphin and LytM catalytic domain

Sabała, I., Jonsson, I., Tarkowski, A., et al. (2012) · BMC Microbiology · doi:10.1186/1471-2180-12-97 · Cited by 44 · see citing works

LysPGS formation inListeria monocytogeneshas broad roles in maintaining membrane integrity beyond antimicrobial peptide resistance

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