Bacteriocins: Perspective for the development of novel anticancer drugs

The hallmarks of cancer

Hanahan, D., & Weinberg, R. A. (2000) · Cell · doi:10.1016/s0092-8674(00)81683-9 · Cited by 29,219 · see citing works

Cancer statistics, 2015

Siegel, R. L., Miller, K. D., & Jemal, A. (2015) · CA A Cancer Journal for Clinicians · doi:10.3322/caac.21254 · Cited by 11,854 · see citing works

Cancer statistics, 2009

Jemal, A., Siegel, R., Ward, E., Hao, Y., Xu, J., & Thun, M. J. (2009) · CA: A Cancer Journal for Clinicians · doi:10.3322/caac.20006 · Cited by 9,709 · see citing works

An endotoxin-induced serum factor that causes necrosis of tumors

Carswell, E. A., Old, L. J., Kassel, R. L., Green, S., Fiore, N., & Williamson, B. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.9.3666 · Cited by 4,532 · see citing works

J Antimicrob Chemother 1994; 33: 350–351

O’Shaughnessy, E. M., & DAS, S. S. (1994) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/33.2.350 · Cited by 3,758 · see citing works

Lipid Asymmetry in Membranes

den Kamp, J. A. F. O. (1979) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.48.070179.000403 · Cited by 1,262 · see citing works

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

Bacteriocins: Evolution, Ecology, and Application

Riley, M. A., & Wertz, J. E. (2002) · Annual Review of Microbiology · doi:10.1146/annurev.micro.56.012302.161024 · Cited by 1,236 · see citing works

The asymmetric distribution of phospholipids in the human red cell membrane. A combined study using phospholipases and freeze-etch electron microscopy

Verkleij, A. J., Zwaal, R. F. A., Roelofsen, B., Comfurius, P., Kastelijn, D., & Deenen, L. L. M. V. (1973) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(73)90143-0 · Cited by 1,128 · see citing works

Non-pathogenic Escherichia coli versus mesalazine for the treatment of ulcerative colitis: a randomised trial

Rembacken, B., Snelling, A. M., Hawkey, P. M., Chalmers, D. M., & Axon, A. (1999) · The Lancet · doi:10.1016/s0140-6736(98)06343-0 · Cited by 1,100 · see citing works

Colicin Biology

Cascalès, E., Buchanan, S. K., Duché, D., Kleanthous, C., Lloubès, R., Postle, K., Riley, M. A., Slatin, S. L., & Cavard, D. (2007) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00036-06 · Cited by 1,023 · see citing works

Membrane Asymmetry

Rothman, J. E., & Lenard, J. (1977) · Science · doi:10.1126/science.402030 · Cited by 987 · see citing works

Use of the Cell Wall Precursor Lipid II by a Pore-Forming Peptide Antibiotic

Breukink, E. J., Wiedemann, I., van Kraaij, C., Kuipers, O. P., Sahl, H., & KRUIJFF, B. D. (1999) · Science · doi:10.1126/science.286.5448.2361 · Cited by 815 · 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

Class IIa bacteriocins: biosynthesis, structure and activity

Ennahar, S., Sashihara, T., Sonomoto, K., & Ishizaki, A. (2000) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2000.tb00534.x · Cited by 637 · 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

Elevated expression of phosphatidylserine in the outer membrane leaflet of human tumor cells and recognition by activated human blood monocytes.

Utsugi, T., Schroit, A. J., Connor, J., Bucana, C. D., & Fidler, I. J. (1991) · PubMed · Cited by 594 · see citing works

Novel bacteriocins from lactic acid bacteria (LAB): various structures and applications

Pérez, R., Zendo, T., & Sonomoto, K. (2014) · Microbial Cell Factories · doi:10.1186/1475-2859-13-s1-s3 · Cited by 578 · see citing works

The pyocins of Pseudomonas aeruginosa

Michel-Briand, Y., & Baysse, C. (2002) · Biochimie · doi:10.1016/s0300-9084(02)01422-0 · Cited by 565 · see citing works

Combination bacteriolytic therapy for the treatment of experimental tumors

Dang, L. H., Bettegowda, C., Huso, D. L., Kinzler, K. W., & Vogelstein, B. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251543698 · Cited by 565 · see citing works

Bacteriocins and their food applications

And, H. C., & Hoover, D. G. (2003) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/j.1541-4337.2003.tb00016.x · Cited by 550 · see citing works

Assembly of the human intestinal microbiota

Dethlefsen, L., Eckburg, P. B., Bik, E. M., & Relman, D. A. (2006) · Trends in Ecology & Evolution · doi:10.1016/j.tree.2006.06.013 · Cited by 509 · see citing works

Generation of Prothrombin‐Converting Activity and the Exposure of Phosphatidylserine at the Outer Surface of Platelets

Bevers, E. M., Comfurius, P., van Rijn, J. L. M. L., et al. (1982) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1982.tb05898.x · Cited by 479 · see citing works

BCG immunotherapy of bladder cancer: 20 years on

ALEXANDROFF, A. B., Jackson, A. M., O’Donnell, M. A., & James, K. E. (1999) · The Lancet · doi:10.1016/s0140-6736(98)07422-4 · Cited by 472 · see citing works

Coley's toxins, tumor necrosis factor and cancer research: A historical perspective

Wiemann, B., & Starnes, C. O. (1994) · Pharmacology & Therapeutics · doi:10.1016/0163-7258(94)90023-x · Cited by 466 · see citing works

The origin and early evolution of mitochondria.

Gray, M. W., Burger, G., & Lang, B. F. (2001) · Genome biology · doi:10.1186/gb-2001-2-6-reviews1018 · Cited by 460 · see citing works

Application of bacteriocins in vegetable food biopreservation

Settanni, L., & Corsetti, A. (2008) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2007.09.001 · Cited by 441 · see citing works

The Treatment of Inoperable Sarcoma by Bacterial Toxins (the Mixed Toxins of the Streptococcus erysipelas and the Bacillus prodigiosus).

COLEY, W. B. (1910) · Proceedings of the Royal Society of Medicine · doi:10.1177/003591571000301601 · Cited by 425 · see citing works

Cationic antimicrobial peptides as novel cytotoxic agents for cancer treatment

Mader, J. S., & Hoskin, D. W. (2006) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.15.8.933 · Cited by 425 · see citing works

Membrane-active host defense peptides – Challenges and perspectives for the development of novel anticancer drugs

Riedl, S., Zweytick, D., & Lohner, K. (2011) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2011.09.004 · Cited by 405 · see citing works

The ins and outs of phospholipid asymmetry in the plasma membrane: roles in health and disease

Fadeel, B., & Xue, D. (2009) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230903193307 · Cited by 391 · 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

BACTIBASE second release: a database and tool platform for bacteriocin characterization

Hammami, R., Zouhir, A., Lay, C., Hamida, J. B., & Fliss, I. (2010) · BMC Microbiology · doi:10.1186/1471-2180-10-22 · Cited by 370 · see citing works

History of Bacillus Calmette-Guerin and Bladder Cancer: An Immunotherapy Success Story

Herr, H. W., & Morales, Á. (2007) · The Journal of Urology · doi:10.1016/j.juro.2007.08.122 · Cited by 353 · see citing works

Bacteria in cancer therapy: a novel experimental strategy

Patyar, S., Joshi, R., Byrav, D. P., Prakash, A., Medhi, B., & Das, B. (2010) · Journal of Biomedical Science · doi:10.1186/1423-0127-17-21 · Cited by 343 · see citing works

Lantibiotics—Ribosomally Synthesized Biologically Active Polypeptides containing Sulfide Bridges and α,β‐Didehydroamino Acids

Jung, G. (1991) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199110513 · Cited by 333 · see citing works

Role of mitochondria as the gardens of cell death

Kim, R., Emi, M., & Tanabe, K. (2005) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-005-0111-7 · Cited by 328 · see citing works

Ribosomally synthesized peptides with antimicrobial properties: biosynthesis, structure, function, and applications

Papagianni, M. (2003) · Biotechnology Advances · doi:10.1016/s0734-9750(03)00077-6 · Cited by 311 · see citing works

Bacteriolytic therapy can generate a potent immune response against experimental tumors

Agrawal, N., Bettegowda, C., Cheong, I., Geschwind, J.-F. H., Drake, C. G., Hipkiss, E. L., Tatsumi, M., Dang, L. H., Diaz, L. A., Pomper, M. G., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406242101 · Cited by 304 · see citing works

Isolation of a Lactobacillus salivarius Strain and Purification of Its Bacteriocin, Which Is Inhibitory to Campylobacter jejuni in the Chicken Gastrointestinal System

Stern, N. J., Ea, S., Eruslanov, B. V., Perelygin, V. V., Mitsevich, E. V., Mitsevich, I. P., Pokhilenko, V. D., Levchuk, V. P., Svetoch, O. E., & Seal, B. S. (2006) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00259-06 · Cited by 297 · see citing works

Changes in electric charge and phospholipids composition in human colorectal cancer cells

Dobrzyńska, I., Szachowicz‐Petelska, B., Sulkowski, S., & Figaszewski, Z. A. (2005) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-005-3557-3 · Cited by 285 · see citing works

Nisin, an apoptogenic bacteriocin and food preservative, attenuates HNSCC tumorigenesis via CHAC 1

Joo, N. E., Ritchie, K., Kamarajan, P., Miao, D., & Kapila, Y. L. (2012) · Cancer Medicine · doi:10.1002/cam4.35 · Cited by 279 · 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

Identification of a functional role for lipid asymmetry in biological membranes: Phosphatidylserine-skeletal protein interactions modulate membrane stability

Manno, S., Takakuwa, Y., & Mohandas, N. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.042688399 · Cited by 274 · see citing works

Bacteriocins as Potential Anticancer Agents

Kaur, S., & Kaur, S. (2015) · Frontiers in Pharmacology · doi:10.3389/fphar.2015.00272 · Cited by 270 · see citing works

Investigation of the cytotoxicity of eukaryotic and prokaryotic antimicrobial peptides in intestinal epithelial cells in vitro

Maher, S., & McClean, S. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2006.01.012 · Cited by 265 · see citing works

Isolation and characterization of pediocin L50, a new bacteriocin from Pediococcus acidilactici with a broad inhibitory spectrum

Cintas, L. M., Rodríguez, J. M., Fernández, M. F., Sletten, K., Nes, I. F., Hernández, P. E., & Holo, H. (1995) · Applied and Environmental Microbiology · doi:10.1128/aem.61.7.2643-2648.1995 · Cited by 256 · see citing works

Oral microbiome and oral and gastrointestinal cancer risk

Ahn, J., Chen, C. Y., & Hayes, R. B. (2012) · Cancer Causes & Control · doi:10.1007/s10552-011-9892-7 · Cited by 242 · see citing works

Phospholipid composition of highly purified mitochondrial outer membranes of rat liver and Neurospora crassa. Is cardiolipin present in the mitochondrial outer membrane?

de Kroon, A. I. P. M., Dolis, D., Mayer, A., Lill, R., & KRUIJFF, B. D. (1997) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(96)00240-4 · Cited by 240 · see citing works

Structure of Microcin J25, a Peptide Inhibitor of Bacterial RNA Polymerase, is a Lassoed Tail

Wilson, K.-A., Kalkum, M., Ottesen, J. J., Yuzenkova, Y., Chait, B. T., Landick, R. C., Muir, T. W., Severinov, K., & Darst, S. A. (2003) · Journal of the American Chemical Society · doi:10.1021/ja036756q · Cited by 240 · see citing works

Mersacidin 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

Studies on Mechanism of Action of Anticancer Peptides by Modulation of Hydrophobicity Within a Defined Structural Framework

Huang, Y.-B., Wang, X., Wang, H.-Y., Liu, Y., & Chen, Y. (2011) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-10-0811 · Cited by 228 · see citing works

Pediocin‐like antimicrobial peptides (class IIa bacteriocins) and their immunity proteins: biosynthesis, structure, and mode of action

Fimland, G., Johnsen, L., Dalhus, B., & Nissen‐Meyer, J. (2005) · Journal of Peptide Science · doi:10.1002/psc.699 · Cited by 227 · see citing works

Oligosaccharides Expressed on MUC1 Produced by Pancreatic and Colon Tumor Cell Lines

Burdick, M. D., Harris, A., Reid, C. J., Iwamura, T., & Hollingsworth, M. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.39.24198 · Cited by 215 · 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

Determining the Structure and Mode of Action of Microbisporicin, a Potent Lantibiotic Active Against Multiresistant Pathogens

Castiglione, F., Lazzarini, A., Carrano, L., et al. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2007.11.009 · Cited by 214 · see citing works

The Enterococcus faecalis cytolysin: a novel toxin active against eukaryotic and prokaryotic cells

Coburn, P. S., & Gilmore, M. S. (2003) · Cellular Microbiology · doi:10.1046/j.1462-5822.2003.00310.x · Cited by 196 · see citing works

Antimicrobial activity of enterocins from Enterococcus faecalis SL-5 against Propionibacterium acnes, the causative agent in acne vulgaris, and its therapeutic effect

Kang, B. S., Seo, J., Lee, G.-S., Jung-Hwa, K., Kim, S. Y., Han, Y. W., Kang, H., Kim, H. O., Rhee, J. H., Chung, M.-J., et al. (2009) · The Journal of Microbiology · doi:10.1007/s12275-008-0179-y · Cited by 195 · see citing works

Bacterial redox protein azurin, tumor suppressor protein p53, and regression of cancer

Yamada, T., Goto, M., Punj, V., Zaborina, O. E., Chen, M. L., Kimbara, K., Majumdar, D., Cunningham, E. A., Gupta, T. K. D., & Chakrabarty, A. M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.222539699 · Cited by 193 · see citing works

Lysostaphin: A Staphylococcal Bacteriolysin with Potential Clinical Applications

Bastos, M. D. C. D. F., Coutinho, B. G., & Coelho, M. L. V. (2010) · Pharmaceuticals · doi:10.3390/ph3041139 · Cited by 189 · see citing works

Differentiation-dependent expression of phosphatidylserine in mammalian plasma membranes: quantitative assessment of outer-leaflet lipid by prothrombinase complex formation.

Connor, J., BUCANA, C. D., Fidler, I. J., & Schroit, A. J. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.9.3184 · Cited by 186 · see citing works

Interaction of the antimicrobial peptide pheromone Plantaricin A with model membranes: Implications for a novel mechanism of action

Zhao, H., Sood, R., Jutila, A., Bose, S., Fimland, G., Nissen-Meyer, J., & Kinnunen, P. K. J. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.03.037 · Cited by 183 · see citing works

Formation and Regulation of Mitochondrial Membranes

Schenkel, L. C., & Bakovic, M. (2014) · International Journal of Cell Biology · doi:10.1155/2014/709828 · Cited by 180 · see citing works

Bacterial cupredoxin azurin as an inducer of apoptosis and regression in human breast cancer

Punj, V., Bhattacharyya, S., Saint‐Dic, D., Vasu, C., Cunningham, E. A., Graves, J. M., Yamada, T., Constantinou, A. I., Christov, K. T., White, B. E. P., et al. (2004) · Oncogene · doi:10.1038/sj.onc.1207376 · Cited by 179 · see citing works

Production of pediocin AcH by Lactobacillus plantarum WHE 92 isolated from cheese

Ennahar, S., Werner, D., Sorokine, O., DORSSELAER, A. V., Bringel, F., Hubert, J., & HASSELMANN, C. (1996) · Applied and Environmental Microbiology · doi:10.1128/aem.62.12.4381-4387.1996 · Cited by 174 · see citing works

Colicins: structures, modes of action, transfer through membranes, and evolution

Braun, V., Pilsl, H., & Gro�, P. (1994) · Archives of Microbiology · doi:10.1007/bf00248693 · Cited by 171 · see citing works

BACTIBASE: a new web-accessible database for bacteriocin characterization

Hammami, R., Zouhir, A., Hamida, J. B., & Fliss, I. (2007) · BMC Microbiology · doi:10.1186/1471-2180-7-89 · Cited by 170 · see citing works

B acillus C almette– G uerin ( BCG ) immunotherapy for bladder cancer: Current understanding and perspectives on engineered BCG vaccine

Kawai, K., Miyazaki, J., Joraku, A., Nishiyama, H., & Akaza, H. (2012) · Cancer Science · doi:10.1111/cas.12075 · Cited by 168 · see citing works

Efficacy of Nisin in Treatment of Clinical Mastitis in Lactating Dairy Cows

Cao, L., Wu, J.-Q., Xie, F., Hu, S., & Mo, Y. (2007) · Journal of Dairy Science · doi:10.3168/jds.2007-0153 · Cited by 168 · see citing works

Membrane fluidity characteristics of human lung cancer

Sok, M., Šentjurc, M., & Schara, M. (1999) · Cancer Letters · doi:10.1016/s0304-3835(99)00044-0 · Cited by 164 · see citing works

Microcin E492, a channel-forming bacteriocin from Klebsiella pneumoniae , induces apoptosis in some human cell lines

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

Bacillus C almette‐ G uérin immunotherapy for genitourinary cancer

Gandhi, N. M., Morales, Á., & Lamm, D. L. (2013) · British Journal of Urology · doi:10.1111/j.1464-410x.2012.11754.x · Cited by 150 · see citing works

New insights into the mechanism of action of lantibiotics--diverse biological effects by binding to the same molecular target

Brötz, H. (2000) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/46.1.1 · Cited by 147 · see citing works

Efficacy of the New Lantibiotic NAI-107 in Experimental Infections Induced by Multidrug-Resistant Gram-Positive Pathogens

Jabes, D. L., Brunati, C., Candiani, G., Riva, S., Romanò, G., & Donadio, S. (2011) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01288-10 · Cited by 146 · see citing works

Toxicity of bovicin HC5 against mammalian cell lines and the role of cholesterol in bacteriocin activity

Paiva, A. D., de Oliveira, M. D., de Paula, S. O., Baracat‐Pereira, M. C., Breukink, E. J., & Mantovani, H. C. (2012) · Microbiology · doi:10.1099/mic.0.062190-0 · Cited by 146 · 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 145 · see citing works

Application of Enterocins as Biopreservatives against Listeria innocua in Meat Products

Aymerich, T., Garriga, M., Ylla, J., Vallier, J., Monfort, J. M., & Hugas, M. (2000) · Journal of Food Protection · doi:10.4315/0362-028x-63.6.721 · Cited by 143 · 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

The apoptotic impact of nisin as a potent bacteriocin on the colon cancer cells

Ahmadi, S., Ghollasi, M., & Hosseini, H. M. (2017) · Microbial Pathogenesis · doi:10.1016/j.micpath.2017.08.037 · Cited by 142 · see citing works

Purification, partial characterization and plasmid‐linkage of pediocin SJ‐1, a bacteriocin produced by Pediococcus acidilactici

SCHVED, F., Lalazar, A., Henis, Y., et al. (1993) · Journal of Applied Bacteriology · doi:10.1111/j.1365-2672.1993.tb02998.x · Cited by 140 · see citing works

Bovicin HC5, a bacteriocin from Streptococcus bovis HC5

Mantovani, H. C., Hu, H., Worobo, R. W., & Russell, J. B. (2002) · Microbiology · doi:10.1099/00221287-148-11-3347 · Cited by 139 · see citing works

Therapeutic Effect of Nisin Z on Subclinical Mastitis in Lactating Cows

Wu, J.-Q., Hu, S., & Cao, L. (2007) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00629-07 · Cited by 139 · see citing works

Evaluation of Lacticin 3147 and a Teat Seal Containing This Bacteriocin for Inhibition of Mastitis Pathogens

Ryan, M. P., Meaney, W. J., Ross, R. P., et al. (1998) · Applied and Environmental Microbiology · doi:10.1128/aem.64.6.2287-2290.1998 · Cited by 137 · see citing works

Transdermal absorption enhancement through rat skin of gallidermin loaded in niosomes

Manosroi, A., Khanrin, P., Lohcharoenkal, W., et al. (2010) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2010.03.064 · Cited by 134 · see citing works

Automated Genome Mining of Ribosomal Peptide Natural Products

Mohimani, H., Kersten, R. D., Liu, W.-T., Wang, M., Purvine, S. O., Wu, S., Brewer, H. M., Paša‐Tolić, L., Bandeira, N., Moore, B. S., et al. (2014) · ACS Chemical Biology · doi:10.1021/cb500199h · Cited by 133 · see citing works

Inhalation of Moli1901 in Patients With Cystic Fibrosis

Grasemann, H., Stehling, F., Brunar, H., et al. (2007) · CHEST Journal · doi:10.1378/chest.06-2085 · Cited by 132 · see citing works

In vivo study on the effectiveness of pediocin PA-1 and Pediococcus acidilactici UL5 at inhibiting Listeria monocytogenes

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

Isolation and Characterization of Two Members of the Siderophore-Microcin Family, Microcins M and H47

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

The Bacteriocin Nisin, an Effective Agent for the Treatment of Staphylococcal Mastitis During Lactation

Fernández, L., Delgado, S., Herrero, H., Maldonado‐Barragán, A., & Rodríguez, J. M. (2008) · Journal of Human Lactation · doi:10.1177/0890334408317435 · Cited by 124 · see citing works

Anticancer properties of a defensin like class IId bacteriocin Laterosporulin10

Baindara, P., Gautam, A., Raghava, G. P. S., & Korpole, S. (2017) · Scientific Reports · doi:10.1038/srep46541 · Cited by 123 · see citing works

Genome mining for ribosomally synthesized and post-translationally modified peptides (RiPPs) in anaerobic bacteria

Letzel, A., Pidot, S. J., & Hertweck, C. (2014) · BMC Genomics · doi:10.1186/1471-2164-15-983 · Cited by 121 · see citing works

Renal effects of targeted anticancer therapies

Porta, C., Cosmai, L., Gallieni, M. A., Pedrazzoli, P., & Malberti, F. (2015) · Nature Reviews Nephrology · doi:10.1038/nrneph.2015.15 · Cited by 119 · see citing works

Evaluation of NVB302 versus vancomycin activity in an in vitro human gut model of Clostridium difficile infection

Crowther, G. S., Baines, S. D., Todhunter, S. L., et al. (2012) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dks359 · Cited by 116 · see citing works

A cell penetrating peptide derived from azurin inhibits angiogenesis and tumor growth by inhibiting phosphorylation of VEGFR-2, FAK and Akt

Mehta, R. R., Yamada, T., Taylor, B. N., Christov, K. T., King, M. L., Majumdar, D., Lekmine, F., Tiruppathì, C., Shilkaitis, A. L., Bratescu, L., et al. (2011) · Angiogenesis · doi:10.1007/s10456-011-9220-6 · Cited by 115 · see citing works

Human tumor cells are selectively inhibited by colicins

Chumchalová, J., & Šmarda, J. (2003) · Folia Microbiologica · doi:10.1007/bf02931286 · Cited by 114 · see citing works

A peptide fragment of azurin induces a p53-mediated cell cycle arrest in human breast cancer cells

Yamada, T., Mehta, R. R., Lekmine, F., Christov, K. T., King, M. L., Majumdar, D., Shilkaitis, A. L., Green, A., Bratescu, L., Beattie, C. W., et al. (2009) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-09-0444 · Cited by 114 · see citing works

Evaluation of antimicrobial peptide nisin as a safe vaginal contraceptive agent in rabbits: in vitro and in vivo studies

Reddy, K. V. R., Aranha, C. C., Gupta, S. M., et al. (2004) · Reproduction · doi:10.1530/rep.1.00028 · Cited by 112 · see citing works

Nisin 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

Microbiota, Oral Microbiome, and Pancreatic Cancer

Michaud, D. S., & Izard, J. (2014) · The Cancer Journal · doi:10.1097/ppo.0000000000000046 · Cited by 111 · see citing works

Characterization of the Antimicrobial Peptide Penisin, a Class Ia Novel Lantibiotic from Paenibacillus sp. Strain A3

Baindara, P., Chaudhry, V., Mittal, G., et al. (2015) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01813-15 · Cited by 111 · see citing works

Effect of O-Glycosylated Mucin on Invasion and Metastasis of HM7 Human Colon Cancer Cells

Yoon, W.-H., Park, H.-D., Lim, K., et al. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.0806 · Cited by 110 · see citing works

Inhibition of Listeria monocytogenes by enterocin 4 during the manufacture andripening of Manchego cheese

Núñez, M., Rodríguez, J. L., García, E. F., Gaya, P., & Médina, M. (1997) · Journal of Applied Microbiology · doi:10.1046/j.1365-2672.1997.00275.x · Cited by 110 · see citing works

In vitro characterization of the anticancer activity of membrane-active cationic peptides. I. Peptide-mediated cytotoxicity and peptide-enhanced cytotoxic activity of doxorubicin against wild-type and p-glycoprotein over-expressing tumor cell lines.

Johnstone, S. A., Gelmon, K. A., Mayer, L., Hancock, R. E. W., & Bally, M. B. (2000) · PubMed · Cited by 108 · see citing works

Internalization of bacterial redox protein azurin in mammalian cells: entry domain and specificity

Yamada, T., Fialho, A. M., Punj, V., Bratescu, L., Gupta, T. K. D., & Chakrabarty, A. M. (2005) · Cellular Microbiology · doi:10.1111/j.1462-5822.2005.00567.x · Cited by 107 · 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

Purification, characterization and in vitro cytotoxicity of the bacteriocin from Pediococcus acidilactici K2a2-3 against human colon adenocarcinoma (HT29) and human cervical carcinoma (HeLa) cells

Villarante, K. I., Elegado, F. B., Iwatani, S., Zendo, T., Sonomoto, K., & de Guzman, E. E. (2010) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-010-0541-1 · Cited by 103 · see citing works

The Bacterial Redox Protein Azurin Induces Apoptosis in J774 Macrophages through Complex Formation and Stabilization of the Tumor Suppressor Protein p53

Yamada, T., Goto, M., Punj, V., Zaborina, O. E., Kimbara, K., Gupta, T. K. D., & Chakrabarty, A. M. (2002) · Infection and Immunity · doi:10.1128/iai.70.12.7054-7062.2002 · Cited by 103 · see citing works

Isolation and characterization of microcin E 492 fromKlebsiella pneumoniae

de Lorenzo, V. (1984) · Archives of Microbiology · doi:10.1007/bf00692715 · Cited by 102 · see citing works

Application of proteomics to determine the mechanism of action of traditional Chinese medicine remedies

Lao, Y., Wang, X., Xu, N., et al. (2014) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2014.05.022 · Cited by 101 · see citing works

Contraceptive efficacy of antimicrobial peptide Nisin: in vitro and in vivo studies

Aranha, C. C., Gupta, S. M., & Reddy, K. V. R. (2004) · Contraception · doi:10.1016/j.contraception.2003.11.002 · Cited by 101 · see citing works

Bioengineering of a Nisin A‐producing Lactococcus lactis to create isogenic strains producing the natural variants Nisin F, Q and Z

Piper, C., Hill, C., Cotter, P. D., et al. (2010) · Microbial Biotechnology · doi:10.1111/j.1751-7915.2010.00207.x · Cited by 100 · see citing works

Laterosporulin10: a novel defensin like Class IId bacteriocin from Brevibacillus sp. strain SKDU10 with inhibitory activity against microbial pathogens

Baindara, P., Singh, N., Ranjan, M., et al. (2016) · Microbiology · doi:10.1099/mic.0.000316 · Cited by 100 · see citing works

Evaluation of safety and human tolerance of the oral probiotic Streptococcus salivarius K12: A randomized, placebo-controlled, double-blind study

Burton, J. P., Cowley, S., Simon, R. R., McKinney, J., Wescombe, P. A., & Tagg, J. R. (2011) · Food and Chemical Toxicology · doi:10.1016/j.fct.2011.06.038 · Cited by 95 · see citing works

The bacterial colicin active against tumor cells in vitro and in vivo is verotoxin 1.

Farkas-Himsley, H., Hill, R. P., Rosen, B. P., Arab, S., & Lingwood, C. A. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.15.6996 · 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

Escherichia coli Nissle 1917 Facilitates Tumor Detection by Positron Emission Tomography and Optical Imaging

Brader, P., Stritzker, J., Riedl, C. C., ZANZONICO, P. B., Cai, S., Burnazi, E. M., Ghani, E. R., Hricak, H., Szalay, A. A., Fong, Y., et al. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-4254 · Cited by 91 · see citing works

Control of Listeria monocytogenes in ground beef by ‘Lactocin 705’, a bacteriocin produced by Lactobacillus casei CRL 705

Vignolo, G. M., Fadda, S., de Kairúz, M. S. N., Holgado, A. A. P. D. R., & Oliver, G. (1996) · International Journal of Food Microbiology · doi:10.1016/0168-1605(95)00038-0 · Cited by 91 · see citing works

Novel Antimicrobial Peptides with High Anticancer Activity and Selectivity

Chu, H., Yip, B., Chen, K., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0126390 · Cited by 91 · see citing works

STUDIES OF A PYOCIN. I. PHYSICAL AND CHEMICAL PROPERTIES.

KAGEYAMA, M. (1964) · PubMed · doi:10.1093/oxfordjournals.jbchem.a127839 · Cited by 90 · see citing works

Spermicidal Activity of the Safe Natural Antimicrobial Peptide Subtilosin

Sutyak, K. E., Anderson, R. A., Dover, S. E., Feathergill, K. A., Aroutcheva, A. A., Faro, S., & Chikindas, M. L. (2008) · Infectious Diseases in Obstetrics and Gynecology · doi:10.1155/2008/540758 · Cited by 88 · see citing works

Microcin E492, a low-molecular-weight peptide antibiotic which causes depolarization of the Escherichia coli cytoplasmic membrane

de Lorenzo, V., & Pugsley, A. P. (1985) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.27.4.666 · Cited by 88 · see citing works

Exoproducts of the Escherichia coli strain H22 inhibiting some enteric pathogens both in vitro and in vivo

Cursino, L., Šmajs, D., Šmarda, J., Nardi, R. M. D., Nicoli, J. R., Chartone‐Souza, E., & Nascimento, A. M. A. (2006) · Journal of Applied Microbiology · doi:10.1111/j.1365-2672.2006.02834.x · Cited by 86 · see citing works

Rapid purification, partial characterization, and antimicrobial spectrum of the bacteriocin, Pediocin AcM, from Pediococcus acidilactici M

Elegado, F. B., Kim, W. J., & Kwon, D. Y. (1997) · International Journal of Food Microbiology · doi:10.1016/s0168-1605(97)00037-8 · 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

Secreted products of a nonmucoid Pseudomonas aeruginosa strain induce two modes of macrophage killing: external-ATP-dependent, P2Z-receptor-mediated necrosis and ATP-independent, caspase-mediated apoptosis

Zaborina, O. E., Dhiman, N., Chen, M. L., et al. (2000) · Microbiology · doi:10.1099/00221287-146-10-2521 · Cited by 83 · see citing works

Structure and Mode of Action of the Membrane-permeabilizing Antimicrobial Peptide Pheromone Plantaricin A

Kristiansen, P. E., Fimland, G., Mantzilas, D., & Nissen-Meyer, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501620200 · 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

Modification of an effector strain for replacement therapy of dental caries to enable clinical safety trials

Hillman, 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

Antibiotics and probiotics in inflammatory bowel disease

Kruis, W. (2004) · Alimentary Pharmacology & Therapeutics · doi:10.1111/j.1365-2036.2004.02051.x · Cited by 80 · see citing works

Colicins—Exocellular lethal proteins ofEscherichia coli

Šmarda, J., & Šmajs, D. (1998) · Folia Microbiologica · doi:10.1007/bf02816372 · Cited by 80 · see citing works

Rapid Cytotoxicity of Antimicrobial Peptide Tempoprin-1CEa in Breast Cancer Cells through Membrane Destruction and Intracellular Calcium Mechanism

Wang, C., Tian, L., Li, S., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060462 · Cited by 79 · see citing works

p28, A first in class peptide inhibitor of cop1 binding to p53

Yamada, T., Christov, K. T., Shilkaitis, A. L., Bratescu, L., Green, A., Santini, S., Bizzarri, A. R., Cannistraro, S., Gupta, T. K. D., & Beattie, C. W. (2013) · British Journal of Cancer · doi:10.1038/bjc.2013.266 · Cited by 78 · see citing works

Lactocin 160, a Bacteriocin Produced by Vaginal Lactobacillus rhamnosus, Targets Cytoplasmic Membranes of the Vaginal Pathogen, Gardnerella vaginalis

Turovskiy, Y., Ludescher, R. D., Aroutcheva, A. A., Faro, S., & Chikindas, M. L. (2009) · Probiotics and Antimicrobial Proteins · doi:10.1007/s12602-008-9003-6 · Cited by 75 · see citing works

Cupredoxin−Cancer Interrelationship: Azurin Binding with EphB2, Interference in EphB2 Tyrosine Phosphorylation, and Inhibition of Cancer Growth

Chaudhari, A., Mahfouz, M. M., Fialho, A. M., Yamada, T., Granja, A. T., Zhu, Y., Hashimoto, W., Schlarb‐Ridley, B. G., Cho, W., Gupta, T. K. D., et al. (2007) · Biochemistry · doi:10.1021/bi061661x · Cited by 74 · see citing works

Therapeutic potential of type A (I) lantibiotics, a group of cationic peptide antibiotics

Smith, L., & Hillman, J. D. (2008) · Current Opinion in Microbiology · doi:10.1016/j.mib.2008.09.008 · Cited by 74 · see citing works

In Vitro Assessment of the Cytotoxicity of Nisin, Pediocin, and Selected Colicins on Simian Virus 40–Transfected Human Colon and Vero Monkey Kidney Cells with Trypan Blue Staining Viability Assays

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

Increase in fluidity in the membrane of MT3 breast cancer cells correlates with enhanced cell adhesion in vitro and increased lung metastasis in NOD/SCID mice

Zeisig, R., Koklič, T., Wiesner, B., et al. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2006.09.030 · Cited by 71 · see citing works

Microcin E492 forms ion channels in phospholipid bilayer membranes

Lagos, R., Wilkens, M., Vergara, C., Cecchi, X., & Monasterio, O. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80096-d · Cited by 70 · see citing works

Bacteriocins: exploring alternatives to antibiotics in mastitis treatment

Pieterse, R., & Todorov, S. D. (2010) · Brazilian Journal of Microbiology · doi:10.1590/s1517-83822010000300003 · Cited by 70 · see citing works

Induction of apoptosis in macrophages by Pseudomonas aeruginosa azurin: tumour‐suppressor protein p53 and reactive oxygen species, but not redox activity, as critical elements in cytotoxicity

Goto, M., Yamada, T., Kimbara, K., Horner, J., Newcomb, M., Gupta, T. K. D., & Chakrabarty, A. M. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03317.x · Cited by 69 · see citing works

Preclinical pharmacokinetics, metabolism, and toxicity of azurin-p28 (NSC745104) a peptide inhibitor of p53 ubiquitination

Jia, L., Gorman, G. S., Coward, L. U., et al. (2010) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-010-1518-3 · Cited by 69 · see citing works

The role of mucin in colon‐cancer metastasis

Schwartz, B., Bresalier, R. S., & Kim, Y. S. (1992) · International Journal of Cancer · doi:10.1002/ijc.2910520113 · Cited by 67 · see citing works

The ability of nisin F to control Staphylococcus aureus infection in the peritoneal cavity, as studied in mice

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

Cytotoxic effects of pyocin S2 produced by Pseudomonas aeruginosa on the growth of three human cell lines

Ali, A. A., Worobec, E. A., Deezagi, A., & Malekzadeh, F. (2004) · Canadian Journal of Microbiology · doi:10.1139/w04-019 · Cited by 65 · 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

Functional and structural characteristics of anticancer peptide Pep27 analogues.

Lee, D. W., Hahm, K., Park, Y., Kim, H., Lee, W., Lim, S., Seo, Y.-K., & Choi, C.-H. (2005) · Cancer Cell International · doi:10.1186/1475-2867-5-21 · Cited by 62 · see citing works

Incorporation of nisin into a meat binding system to inhibit bacteria on beef surfaces

Cutter, & Siragusa (1998) · Letters in Applied Microbiology · doi:10.1046/j.1472-765x.1998.00381.x · Cited by 62 · see citing works

Control of beef spoilage by a sulfide-producing Lactobacillus sake strain with bacteriocinogenic Leuconostoc gelidum UAL187 during anaerobic storage at 2 degrees C

Leisner, J. J., GREER, G. G., & Stiles, M. E. (1996) · Applied and Environmental Microbiology · doi:10.1128/aem.62.7.2610-2614.1996 · Cited by 62 · 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

Spermicidal bacteriocins: Lacticin 3147 and subtilosin A

Silkin, L., Hamza, S., Kaufman, S., et al. (2007) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2007.11.024 · Cited by 56 · see citing works

Targeting the Eph System with Peptides and Peptide Conjugates

Riedl, S. J., & Pasquale, E. B. (2015) · Current Drug Targets · doi:10.2174/1389450116666150727115934 · Cited by 54 · see citing works

The Novel Biological Action of Antimicrobial Peptides via Apoptosis Induction

Cho, J. (2012) · Journal of Microbiology and Biotechnology · doi:10.4014/jmb.1205.05041 · Cited by 53 · see citing works

Investigation of the Cytotoxicity of Antimicrobial Peptide P40 on Eukaryotic Cells

Vaucher, R. D. A., Teixeira, M. L., & Brandelli, A. (2009) · Current Microbiology · doi:10.1007/s00284-009-9490-z · Cited by 53 · see citing works

The Lantibiotic Lacticin 3147 Prevents Systemic Spread ofStaphylococcus aureusin a Murine Infection Model

Piper, C., Casey, P. G., Hill, C., Cotter, P. D., & Ross, R. P. (2012) · International Journal of Microbiology · doi:10.1155/2012/806230 · Cited by 52 · 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

Interaction of an anticancer peptide fragment of azurin with p53 and its isolated domains studied by atomic force spectroscopy

Bizzarri, A. R., Santini, V., Bucciantini, Agostino, D., Yamada, T., Beattie, R. M., & Cannistraro, S. (2011) · International Journal of Nanomedicine · doi:10.2147/ijn.s26155 · Cited by 51 · see citing works

A role of the cancer cell membrane fluidity in the cancer metastases: An ESR study.

Nakazawa, I., & Iwaizumi, M. (1989) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.157.193 · Cited by 50 · see citing works

THE PHENOTYPIC AND FITNESS EFFECTS OF COLICIN RESISTANCE IN ESCHERICHIA COLI K‐12

Feldgarden, M., & Riley, M. A. (1999) · Evolution · doi:10.1111/j.1558-5646.1999.tb04517.x · Cited by 50 · see citing works

Bacterial proteinaceous products (bacteriocins) as cytotoxic agents of neoplasia.

Farkas-Himsley, H., & Cheung, R. (1976) · PubMed · Cited by 49 · see citing works

Plantaricin A, a cationic peptide produced by Lactobacillus plantarum, permeabilizes eukaryotic cell membranes by a mechanism dependent on negative surface charge linked to glycosylated membrane proteins

Sand, S. L., Nissen-Meyer, J., Sand, O., & Haug, T. M. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2012.11.001 · Cited by 49 · see citing works

Mechanisms of Colonisation and Colonisation Resistance of the Digestive Tract Part 2: Bacteria/Bacteria Interactions

Michel Fons, A. G. (2000) · Microbial Ecology in Health and Disease · doi:10.1080/089106000750060495 · Cited by 49 · see citing works

The bacteriocin piscicolin 126 retains antilisterial activity in vivo

Ingham, A. B. (2003) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkg229 · 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

Antineoplastic Properties of Bacteriocins

Cornut, G., Fortin, C., & Soulières, D. (2008) · American Journal of Clinical Oncology · doi:10.1097/coc.0b013e31815e456d · Cited by 44 · see citing works

Scanning electron microscopic analysis of breast aspirates

CHAUDHARY, J., & Munshi, M. M. (1995) · Cytopathology · doi:10.1111/j.1365-2303.1995.tb00469.x · Cited by 43 · see citing works

Analysis of the Two-Peptide Bacteriocins Lactococcin G and Enterocin 1071 by Site-Directed Mutagenesis

Oppegård, C., Fimland, G., Thorbæk, L., & Nissen-Meyer, J. (2007) · Applied and Environmental Microbiology · doi:10.1128/aem.02718-06 · Cited by 43 · see citing works

The intramolecular disulfide‐stapled structure of laterosporulin, a class II d bacteriocin, conceals a human defensin‐like structural module

Singh, P. K., Solanki, V., Sharma, S., Thakur, K. G., Krishnan, B., & Korpole, S. (2014) · FEBS Journal · doi:10.1111/febs.13129 · Cited by 43 · see citing works

Plantaricin A, a peptide pheromone produced by Lactobacillus plantarum, permeabilizes the cell membrane of both normal and cancerous lymphocytes and neuronal cells

Sand, S. L., Oppegård, C., Ohara, S., Iijima, T., Naderi, S., Blomhoff, H. K., Nissen-Meyer, J., & Sand, O. (2010) · Peptides · doi:10.1016/j.peptides.2010.04.010 · Cited by 42 · see citing works

Lipid analysis of mitochondrial membranes from the yeast Pichia pastoris

Wriessnegger, T., Leitner, E., Belegratis, M. R., Ingolić, E., & Daum, G. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2008.12.017 · Cited by 42 · see citing works

Cationic Antimicrobial Peptide Cytotoxicity

Laverty, G. (2014) · SOJ Microbiology & Infectious Diseases · doi:10.15226/sojmid.2013.00112 · Cited by 41 · see citing works

Discovery of Azurin-Like Anticancer Bacteriocins from Human Gut Microbiome through Homology Modeling and Molecular Docking against the Tumor Suppressor p53

Nguyen, C., & Nguyễn, V. D. (2016) · BioMed Research International · doi:10.1155/2016/8490482 · Cited by 41 · see citing works

Correlation between the Presence of Microvilli and the Growth or Metastatic Potential of Tumor Cells

Ren, J., Hamada, J., Okada, F., et al. (1990) · Japanese Journal of Cancer Research · doi:10.1111/j.1349-7006.1990.tb02668.x · Cited by 40 · see citing works

ESR study of plasmatic membrane of the transplantable melanoma cells in relation to their biological properties

Kozłowska, K., Nowak, J., Kwiatkowski, B., et al. (1999) · Experimental and Toxicologic Pathology · doi:10.1016/s0940-2993(99)80074-8 · Cited by 40 · 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

Structure and Function of Colicin S4, a Colicin with a Duplicated Receptor-binding Domain

Arnold, T., Zeth, K., & Linke, D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m808504200 · Cited by 38 · see citing works

Evolution of Microcin V and Colicin Ia Plasmids in Escherichia coli

Jeziorowski, A., & Gordon, D. M. (2007) · Journal of Bacteriology · doi:10.1128/jb.00243-07 · Cited by 37 · see citing works

Bacterial proteins as potential drugs in the treatment of leukemia

Kwan, J. M., Fialho, A. M., Kundu, M., Thomas, J., Hong, C. S., Gupta, T. K. D., & Chakrabarty, A. M. (2009) · Leukemia Research · doi:10.1016/j.leukres.2009.01.024 · Cited by 36 · see citing works

Novel cationic antimicrobial peptide GW-H1 induced caspase-dependent apoptosis of hepatocellular carcinoma cell lines

Chen, Y. S., Li, J., Yu, C., Lin, C., Chiu, P.-H., Chen, P., Lin, C.-C., & Chen, W. (2012) · Peptides · doi:10.1016/j.peptides.2012.05.011 · Cited by 36 · see citing works

Interactions between two carnobacteriocins Cbn BM1 and Cbn B2 from Carnobacterium maltaromaticum CP5 on target bacteria and Caco-2 cells

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

Structure analysis of the two-peptide bacteriocin lactococcin G by introducing d-amino acid residues

Oppegård, C., Rogne, P., Kristiansen, P. E., et al. (2010) · Microbiology · doi:10.1099/mic.0.038430-0 · Cited by 35 · see citing works

Bacterial redox protein azurin induce apoptosis in human osteosarcoma U2OS cells

YANG, D., MIAO, X., Ye, Z., FENG, J., XU, R., Huang, X. H., & Ge, F. (2005) · Pharmacological Research · doi:10.1016/j.phrs.2005.06.002 · Cited by 34 · see citing works

Recent updated aspects of colicins of Enterobacteriaceae

Cursino, L., Šmarda, J., Chartone‐Souza, E., et al. (2002) · Brazilian Journal of Microbiology · doi:10.1590/s1517-83822002000300001 · Cited by 34 · see citing works

The structural role of the copper-coordinating and surface-exposed histidine residue in the blue copper protein azurin

Jeuken, L. J. C., Ubbink, M., Bitter, J. H., et al. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3754 · Cited by 33 · see citing works

Mode of antibacterial action of a signal peptide, Pep27 from Streptococcus pneumoniae

Sung, W. S., Park, Y., Choi, C.-H., et al. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.09.041 · Cited by 33 · see citing works

Anticancer effects of CAMEL peptide

Smolarczyk, R., Cichoń, T., Kamysz, W., Głowala‐Kosińska, M., Szydło, A., Szultka, Ł., Sieroń, A. L., & Szala, S. (2010) · Laboratory Investigation · doi:10.1038/labinvest.2010.58 · Cited by 32 · see citing works

Mapping Functional Domains of Colicin M

Helbig, S., & Braun, V. (2010) · Journal of Bacteriology · doi:10.1128/jb.01206-10 · Cited by 32 · see citing works

Structural Basis for Microcin C7 Inactivation by the MccE Acetyltransferase

Agarwal, V., Metlitskaya, A., Severinov, K., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.226282 · Cited by 30 · see citing works

Induction of Transient Ion Channel-Like Pores in a Cancer Cell by Antibiotic Peptide

Ye, J. (2004) · The Journal of Biochemistry · doi:10.1093/jb/mvh114 · Cited by 30 · see citing works

Structure of microcin C51, a new antibiotic with a broad spectrum of activity

Metlitskaya, A. Z., Katrukha, G. S., Shashkov, A. S., Zaitsev, D. A., Egorov, T. A., & Khmel, I. A. (1995) · FEBS Letters · doi:10.1016/0014-5793(94)01345-2 · Cited by 29 · see citing works

Pulmonary pharmacokinetics and safety of nebulized duramycin in healthy male volunteers

Steiner, I., Errhalt, P., Kubesch, K., et al. (2008) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-008-0293-8 · Cited by 29 · see citing works

Effect of colicin E3 on leukemia cells P 388 in vitro

Fuska, J., Fusková, A., Šmarda, J., et al. (1979) · Cellular and Molecular Life Sciences · doi:10.1007/bf01964380 · Cited by 29 · see citing works

Bacteriolytic therapy of experimental pancreatic carcinoma

Maletzki, C. (2010) · World Journal of Gastroenterology · doi:10.3748/wjg.v16.i28.3546 · Cited by 28 · see citing works

Cysteine-rich low molecular weight antimicrobial peptides from Brevibacillus and related genera for biotechnological applications

Baindara, P., Kapoor, A., Korpole, S., & Grover, V. (2017) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-017-2291-9 · Cited by 23 · see citing works

Mutational Analysis of the Class IIa Bacteriocin Curvacin A and Its Orientation in Target Cell Membranes

Haugen, H. S., Kristiansen, P. E., Fimland, G., & Nissen-Meyer, J. (2008) · Applied and Environmental Microbiology · doi:10.1128/aem.01068-08 · Cited by 22 · see citing works

Effect of a bacteriocin produced by Mycobacterium smegmatis on growth of cultured tumor and normal cells.

Saito, H., & Watanabe, T. (1979) · PubMed · Cited by 21 · see citing works

Development of a Homologous Expression System for and Systematic Site-Directed Mutagenesis Analysis of Thurincin H, a Bacteriocin Produced by Bacillus thuringiensis SF361

Wang, G., Manns, D. C., Churey, J. J., & Worobo, R. W. (2014) · Applied and Environmental Microbiology · doi:10.1128/aem.00433-14 · Cited by 21 · see citing works

The cytotoxic and cytocidal effect of colicin E3 on mammalian tissue cells

Šmarda, J., Obdržálek, V., Taborsky, I., et al. (1978) · Folia Microbiologica · doi:10.1007/bf02876680 · Cited by 21 · see citing works

Cloning and expression of bacteriocins of Pediococcus spp.: A review

Kumar, B., Balgir, P. P., Kaur, B., & Garg, N. (2011) · Archives of Clinical Microbiology · Cited by 20 · see citing works

Identification & Characterization of lactobacillus salavarius bacteriocins and its relevance in cancer therapeutics

Shaikh, F., Abhinand, P. A., & Ragunath, P. (2012) · Bioinformation · doi:10.6026/97320630008589 · Cited by 20 · see citing works

Cytotoxic Effects of Colicins E1 and E3 on v-myb-Transformed Chicken Monoblasts

Šmarda, J., Fialová, M., & Šmarda, J. (2001) · Folia Biologica · doi:10.14712/fb2001047010011 · Cited by 20 · see citing works

Lactic 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

Periodontal pathogens promote cancer aggressivity via TLR/MyD88 triggered activation of Integrin/FAK signaling that is therapeutically reversible by a probiotic bacteriocin

Kamarajan, P., Ateia, I., Shin, J. M., Fenno, J. C., Le, C., Zhan, L., Chang, A., Darveau, R., & Kapila, Y. L. (2020) · PLOS Pathogens · doi:10.1371/journal.ppat.1008881 · Cited by 134 · 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

Bacteriocin diversity and the frequency of multiple bacteriocin production in Escherichia coli

Gordon, D. M., & O'Brien, C. L. (2006) · Microbiology · doi:10.1099/mic.0.28690-0 · Cited by 148 · see citing works

Purification, amino acid sequence, and characterization of bacteriocin GA15, a novel class IIa bacteriocin secreted by Lactiplantibacillus plantarum GCNRC_GA15

Daba, G. M., Mostafa, F. A., Saleh, S. A. A., Elkhateeb, W. A., Awad, G. E. A., Nomiyama, T., Zendo, T., & El-Dein, A. N. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.06.003 · Cited by 35 · see citing works

Antineoplastic Properties of Bacteriocins

Cornut, G., Fortin, C., & Soulières, D. (2008) · American Journal of Clinical Oncology · doi:10.1097/coc.0b013e31815e456d · Cited by 44 · see citing works

The role of ‘soaking’ in spiteful toxin production in Pseudomonas aeruginosa

Inglis, R. F., Hall, A. R., & Buckling, A. (2012) · Biology Letters · doi:10.1098/rsbl.2012.0569 · Cited by 12 · see citing works

Identification and production of a bacteriocin from Enterococcus mundtii QU 2 isolated from soybean

Zendo, T., Eungruttanagorn, N., Fujioka, S., Tashiro, Y., Nomura, K., Sera, Y., Kobayashi, G., Nakayama, J., Ishizaki, A., & Sonomoto, K. (2005) · Journal of Applied Microbiology · doi:10.1111/j.1365-2672.2005.02704.x · Cited by 105 · see citing works