Acedo, J. Z., M. J. van Belkum, C. T. Lohans, R. T. McKay, M. Miskolzie and J. C. Vederas (2015). “Solution Structure of Acidocin B, a Circular Bacteriocin Produced by <span class = "named-content genus-species" id = "named-content–1">Lactobacillus acidophilus</span> M46.” Applied and Environmental Microbiology 81(8): 2910.
Bartholomae, M., A. Buivydas, J. H. Viel, M. Montalbán-López and O. P. Kuipers (2017). “Major gene-regulatory mechanisms operating in ribosomally synthesized and post-translationally modified peptide (RiPP) biosynthesis.” Molecular Microbiology 106(2): 186–206.
Borrero, J., D. A. Brede, M. Skaugen, D. B. Diep, C. Herranz, I. F. Nes, L. M. Cintas and P. E. Hernández (2011). “Characterization of Garvicin ML, a Novel Circular Bacteriocin Produced by <em>Lactococcus garvieae</em> DCC43, Isolated from Mallard Ducks (<em>Anas platyrhynchos</em>).” Applied and Environmental Microbiology 77(1): 369.
Borrero, J., E. Kelly, P.M. Connor, P. Kelleher, C. Scully, P. D. Cotter, J. Mahony and D. van Sinderen (2018). “Plantaricyclin A, a Novel Circular Bacteriocin Produced by <span class = "named-content genus-species" id = "named-content–1">Lactobacillus plantarum</span> NI326: Purification, Characterization, and Heterologous Production.” Applied and Environmental Microbiology 84(1): e01801–01817.
Braun, P. and G. von Heijne (1999). “The Aromatic Residues Trp and Phe Have Different Effects on the Positioning of a Transmembrane Helix in the Microsomal Membrane.” Biochemistry 38(30): 9778–9782.
Cebrián, R., M. Maqueda, J. L. Neira, E. Valdivia, M. Martínez-Bueno and M. Montalbán-López (2010). “Insights into the Functionality of the Putative Residues Involved in Enterocin AS–48 Maturation.” Applied and Environmental Microbiology 76(21): 7268.
Ceotto, H., D. Brede, Z. Salehian, J. dos Santos Nascimento, P. C. Fagundes, I. F. Nes and M. do Carmo de Freire Bastos (2010). “Aureocins 4185, Bacteriocins Produced by Staphylococcus aureus 4185: Potential Application in Food Preservation.” Foodborne Pathogens and Disease 7(10): 1255–1262.
Ceotto, H., J. d. S. Nascimento, M. A. V. d. P. Brito and M. d. C. d. F. Bastos (2009). “Bacteriocin production by Staphylococcus aureus involved in bovine mastitis in Brazil.” Research in microbiology 160(8): 592–599.
Chojnacki, S., A. Cowley, J. Lee, A. Foix and R. Lopez (2017). “Programmatic access to bioinformatics tools from EMBL-EBI update: 2017.” Nucleic acids research 45(W1): W550-W553.
Clark, R. J., H. Fischer, L. Dempster, N. L. Daly, K. J. Rosengren, S. T. Nevin, F. A. Meunier, D. J. Adams and D. J. Craik (2005). “Engineering stable peptide toxins by means of backbone cyclization: Stabilization of the α-conotoxin MII.” Proceedings of the National Academy of Sciences of the United States of America 102(39): 13767.
Collins, F. W. J., P.M. O’Connor, O. O’Sullivan, B. Gómez-Sala, M. C. Rea, C. Hill and R. P. Ross (2017). “Bacteriocin Gene-Trait matching across the complete Lactobacillus Pan-genome.” Scientific Reports 7(1): 3481.
Cotter, P. D., C. Hill and R. P. Ross (2005). “Bacteriocins: developing innate immunity for food.” Nature Reviews Microbiology 3: 777.
Egan, K. (2018). Discovery and evaluation of novel and characterised bacteriocins for future applications, University College Cork.
Espinosa-Hernández, E., J. I. Morales-Camacho, D. A. Fernández-Velasco, C. G. Benítez-Cardoza, F. d. F. Rosas-Cárdenas and S. Luna-Suárez (2019). “The insertion of bioactive peptides at the C-terminal end of an 11S globulin changes the structural stability and improves the antihypertensive activity.” Electronic Journal of Biotechnology 37: 18–24.
Fujimoto, S., H. Tomita, E. Wakamatsu, K. Tanimoto and Y. Ike (1995). Physical mapping of the conjugative bacteriocin plasmid pPD1 of Enterococcus faecalis and identification of the determinant related to the pheromon response.
Gabrielsen, C., D. A. Brede, P. E. Hernández, I. F. Nes and D. B. Diep (2012). “The Maltose ABC Transporter in <span class = "named-content genus-species" id = "named-content–1">Lactococcus lactis</span> Facilitates High-Level Sensitivity to the Circular Bacteriocin Garvicin ML.” Antimicrobial Agents and Chemotherapy 56(6): 2908.
Gabrielsen, C., D. A. Brede, I. F. Nes and D. B. Diep (2014). “Circular Bacteriocins: Biosynthesis and Mode of Action.” Applied and Environmental Microbiology 80(22): 6854.
Gálvez, A., M. Maqueda, M. Martínez-Bueno and E. Valdivia (1991). “Permeation of bacterial cells, permeation of cytoplasmic and artificial membrane vesicles, and channel formation on lipid bilayers by peptide antibiotic AS–48.” Journal of Bacteriology 173(2): 886.
Gálvez, A., M. Maqueda, E. Valdivia, A. Quesada and E. Montoya (1986). “Characterization and partial purification of a broad spectrum antibiotic AS–48 produced by Streptococcus faecalis.” Canadian Journal of Microbiology 32(10): 765–771.
Gleason, N. J., D. V. Greathouse, C. V. Grant, S. J. Opella and R. E. Koeppe (2013). “Single Tryptophan and Tyrosine Comparisons in the N-Terminal and C-Terminal Interface Regions of Transmembrane GWALP Peptides.” The Journal of Physical Chemistry B 117(44): 13786–13794.
Golneshin, A. (2014). Characterisation of bacteriocin genes and proteins from Lactobacillus plantarum B21 as potential new antimicrobial agents and natural food preservatives Doctor of Philosophy, RMIT University.
Gong, X., L. A. Martin-Visscher, D. Nahirney, J. C. Vederas and M. Duszyk (2009). “The circular bacteriocin, carnocyclin A, forms anion-selective channels in lipid bilayers.” Biochimica et Biophysica Acta (BBA) - Biomembranes 1788(9): 1797–1803.
González, C., G. M. Langdon, M. Bruix, A. Gálvez, E. Valdivia, M. Maqueda and M. Rico (2000). “Bacteriocin AS–48, a microbial cyclic polypeptide structurally and functionally related to mammalian NK-lysin.” Proceedings of the National Academy of Sciences 97(21): 11221.
Himeno, K., K. J. Rosengren, T. Inoue, R. H. Perez, M. L. Colgrave, H. S. Lee, L. Y. Chan, S. T. Henriques, K. Fujita, N. Ishibashi, T. Zendo, P. Wilaipun, J. Nakayama, V. Leelawatcharamas, H. Jikuya, D. J. Craik and K. Sonomoto (2015). “Identification, Characterization, and Three-Dimensional Structure of the Novel Circular Bacteriocin, Enterocin NKR–5–3B, from Enterococcus faecium.” Biochemistry 54(31): 4863–4876.
Ishibashi, N., K. Himeno, K. Fujita, Y. Masuda, R. H. Perez, T. Zendo, P. Wilaipun, V. Leelawatcharamas, J. Nakayama and K. Sonomoto (2012). “Purification and Characterization of Multiple Bacteriocins and an Inducing Peptide Produced by Enterococcus faecium NKR–5–3 from Thai Fermented Fish.” Bioscience, Biotechnology, and Biochemistry 76(5): 947–953.
Ito, Y., Y. Kawai, K. Arakawa, Y. Honme, T. Sasaki and T. Saito (2009). “Conjugative Plasmid from <em>Lactobacillus gasseri</em> LA39 That Carries Genes for Production of and Immunity to the Circular Bacteriocin Gassericin A.” Applied and Environmental Microbiology 75(19): 6340.
Iwai, H. and A. Plückthun (1999). “Circular β-lactamase: stability enhancement by cyclizing the backbone.” FEBS Letters 459(2): 166–172.
Jiménez, J. J., D. B. Diep, J. Borrero, L. Gútiez, S. Arbulu, I. F. Nes, C. Herranz, L. M. Cintas and P. E. Hernández (2015). “Cloning strategies for heterologous expression of the bacteriocin enterocin A by Lactobacillus sakei Lb790, Lb. plantarum NC8 and Lb. casei CECT475.” Microbial Cell Factories 14(1): 166.
Jiménez, M. A., A. C Barrachi-Saccilotto, E. Valdivia, M. Maqueda and M. Rico (2005). Design, NMR characterization and activity of a 21‐residue peptide fragment of bacteriocin AS‐48 containing its putative membrane interacting region.
Kalmokoff, M. L., T. D. Cyr, M. A. Hefford, M. F. Whitford and R. M. Teather (2003). “Butyrivibriocin AR10, a new cyclic bacteriocin produced by the ruminal anaerobe Butyrivibrio fibrisolvens AR10: characterization of the gene and peptide.” Canadian Journal of Microbiology 49(12): 763–773.
Kalmokoff, M. L. and R. M. Teather (1997). “Isolation and characterization of a bacteriocin (Butyrivibriocin AR10) from the ruminal anaerobe Butyrivibrio fibrisolvens AR10: evidence in support of the widespread occurrence of bacteriocin-like activity among ruminal isolates of B. fibrisolvens.” Applied and Environmental Microbiology 63: 394–402.
Kawai, Y., Y. Ishii, K. Arakawa, K. Uemura, B. Saitoh, J. Nishimura, H. Kitazawa, Y. Yamazaki, Y. Tateno, T. Itoh and T. Saito (2004). “Structural and Functional Differences in Two Cyclic Bacteriocins with the Same Sequences Produced by Lactobacilli.” Applied and Environmental Microbiology 70(5): 2906.
Kawai, Y., R. Kemperman, J. Kok and T. Saito (2004). “The Circular Bacteriocins Gassericin A and Circularin A.” Current protein & peptide science 5: 393–398.
Kawai, Y., T. Saito, H. Kitazawa and T. Itoh (1998). “Gassericin A; an Uncommon Cyclic Bacteriocin Produced by <i>Lactobacillus gasseri</i> LA39 Linked at <i>N</i>- and <i>C</i>-Terminal Ends.” Bioscience, Biotechnology, and Biochemistry 62(12): 2438–2440.
Kemperman, R., A. Kuipers, H. Karsens, A. Nauta, O. Kuipers and J. Kok (2003). “Identification and Characterization of Two Novel Clostridial Bacteriocins, Circularin A and Closticin 574.” Applied and Environmental Microbiology 69(3): 1589.
Kim, J., M. Mosior, L. A. Chung, H. Wu and S. McLaughlin (1991). “Binding of peptides with basic residues to membranes containing acidic phospholipids.” Biophysical Journal 60(1): 135–148.
Krogh, A., E. L. L. Sonnhammer and L. Käll (2007). “Advantages of combined transmembrane topology and signal peptide prediction—the Phobius web server.” Nucleic Acids Research 35(suppl_2): W429-W432.
Kurata, A., T. Yamaguchi, M. Kira and N. Kishimoto (2019). “Characterization and heterologous expression of an antimicrobial peptide from Bacillus amyloliquefaciens CMW1.” Biotechnology & Biotechnological Equipment 33(1): 886–893.
Kyte, J. and R. F. Doolittle (1982). “A simple method for displaying the hydropathic character of a protein.” Journal of Molecular Biology 157(1): 105–132.
Logan, N. A., O. Berge, A. H. Bishop, H.-J. Busse, P. De Vos, D. Fritze, M. Heyndrickx, P. Kämpfer, L. Rabinovitch, M. S. Salkinoja-Salonen, L. Seldin and A. Ventosa (2009). “Proposed minimal standards for describing new taxa of aerobic, endospore-forming bacteria.” International Journal of Systematic and Evolutionary Microbiology 59(8): 2114–2121.
Luciani, A., R. Lopez, S. C. Potter, Y. Park, R. D. Finn and S. R. Eddy (2018). “HMMER web server: 2018 update.” Nucleic Acids Research 46(W1): W200-W204.
Maqueda, M., M. Sánchez-Hidalgo, M. Fernández, M. Montalbán-López, E. Valdivia and M. Martínez-Bueno (2008). “Genetic features of circular bacteriocins produced by Gram-positive bacteria.” FEMS Microbiology Reviews 32(1): 2–22.
Martin-Visscher, L. A., X. Gong, M. Duszyk and J. C. Vederas (2009). “The Three-dimensional Structure of Carnocyclin A Reveals That Many Circular Bacteriocins Share a Common Structural Motif.” Journal of Biological Chemistry 284(42): 28674–28681.
Martin-Visscher, L. A., M. J. van Belkum, S. Garneau-Tsodikova, R. M. Whittal, J. Zheng, L. M. McMullen and J. C. Vederas (2008). “Isolation and characterization of carnocyclin a, a novel circular bacteriocin produced by Carnobacterium maltaromaticum UAL307.” Applied and environmental microbiology 74(15): 4756–4763.
Martínez-Bueno, M., A. Gálvez, E. Valdivia and M. Maqueda (1990). “A transferable plasmid associated with AS–48 production in Enterococcus faecalis.” Journal of Bacteriology 172(5): 2817.
Martínez-Bueno, M., E. Valdivia, A. Gálvez, J. Coyette and M. Maqueda (1998). “Analysis of the gene cluster involved in production and immunity of the peptide antibiotic AS–48 in Enterococcus faecalis.” Molecular Microbiology 27(2): 347–358.
Masuda, Y., H. Ono, H. Kitagawa, H. Ito, F. Mu, N. Sawa, T. Zendo and K. Sonomoto (2011). “Identification and Characterization of Leucocyclicin Q, a Novel Cyclic Bacteriocin Produced by <span class = "named-content genus-species" id = "named-content–1">Leuconostoc mesenteroides</span> TK41401.” Applied and Environmental Microbiology 77(22): 8164.
Mercedes, M., G. Antonio, B. Manuel Martinez, S.-B. Maria Jose, G. Carlos, A. Armando, R. Manuel and V. Eva (2004). “Peptide AS–48: Prototype of a New Class of Cyclic Bacteriocins.” Current Protein & Peptide Science 5(5): 399–416.
Montalbán-López, M., B. Spolaore, O. Pinato, M. Martínez-Bueno, E. Valdivia, M. Maqueda and A. Fontana (2008). “Characterization of linear forms of the circular enterocin AS–48 obtained by limited proteolysis.” FEBS Letters 582(21–22): 3237–3242.
Mu, F., Y. Masuda, T. Zendo, H. Ono, H. Kitagawa, H. Ito, J. Nakayama and K. Sonomoto (2014). “Biological function of a DUF95 superfamily protein involved in the biosynthesis of a circular bacteriocin, leucocyclicin Q.” Journal of Bioscience and Bioengineering 117(2): 158–164.
Nazina, T. N., T. P. Tourova, A. B. Poltaraus, E. V. Novikova, A. A. Grigoryan, A. E. Ivanova, A.M. Lysenko, V. V. Petrunyaka, G. A. Osipov, S. S. Belyaev and M. V. Ivanov (2001). “Taxonomic study of aerobic thermophilic bacilli: descriptions of Geobacillus subterraneus gen. nov., sp. nov. and Geobacillus uzenensis sp. nov. from petroleum reservoirs and transfer of Bacillus stearothermophilus, Bacillus thermocatenulatus, Bacillus thermoleovorans, Bacillus kaustophilus, Bacillus thermodenitrificans to Geobacillus as the new combinations G. stearothermophilus, G. th.” International Journal of Systematic and Evolutionary Microbiology 51(2): 433–446.
NCBI (2017). “Database resources of the National Center for Biotechnology Information.” Nucleic Acids Research 46(D1): D8-D13.
Perez, R. H., N. Ishibashi, T. Inoue, K. Himeno, Y. Masuda, N. Sawa, T. Zendo, P. Wilaipun, V. Leelawatcharamas, J. Nakayama and K. Sonomoto (2016). “Functional Analysis of Genes Involved in the Biosynthesis of Enterocin NKR–5–3B, a Novel Circular Bacteriocin.” Journal of Bacteriology 198(2): 291.
Perez, R. H., H. Sugino, N. Ishibashi, T. Zendo, P. Wilaipun, V. Leelawatcharamas, J. Nakayama and K. Sonomoto (2017). “Mutations near the cleavage site of enterocin NKR–5–3B prepeptide reveal new insights into its biosynthesis.” Microbiology 163(4): 431–441.
Perez, R. H., T. Zendo and K. Sonomoto (2014). “Novel bacteriocins from lactic acid bacteria (LAB): various structures and applications.” Microbial Cell Factories 13(1): S3.
Perez, R. H., T. Zendo and K. Sonomoto (2018). “Circular and Leaderless Bacteriocins: Biosynthesis, Mode of Action, Applications, and Prospects.” Frontiers in Microbiology 9(2085).
Potter, A., H. Ceotto, M. L. V. Coelho, A. J. Guimarães and M. d. C. d. F. Bastos (2014). “The gene cluster of aureocyclicin 4185: the first cyclic bacteriocin of Staphylococcus aureus.” Microbiology 160(5): 917–928.
Samyn, B., M. Martinez-Bueno, B. Devreese, M. Maqueda, A. Gálvez, E. Valdivia, J. Coyette and J. Van Beeumen (1994). “The cyclic structure of the enterococcal peptide antibiotic AS–48.” FEBS Letters 352(1): 87–90.
Sanchez-Hidalgo, M., A.M. Fernández-Escamilla, M. Martínez-Bueno, E. Valdivia, L. Serrano and M. Maqueda (2010). Conformational Stability and Activity of Circular Enterocin AS–48 Derivatives.
Sánchez-Hidalgo, M., M. Montalbán-López, R. Cebrián, E. Valdivia, M. Martínez-Bueno and M. Maqueda (2011). “AS–48 bacteriocin: close to perfection.” Cellular and Molecular Life Sciences 68(17): 2845–2857.
Sawa, N., T. Zendo, J. Kiyofuji, K. Fujita, K. Himeno, J. Nakayama and K. Sonomoto (2009). “Identification and Characterization of Lactocyclicin Q, a Novel Cyclic Bacteriocin Produced by Lactococcus sp. Strain QU 12
" Applied and Environmental Microbiology 75: 1552–1558.
Scholz, R., J. Vater, A. Budiharjo, Z. Wang, Y. He, K. Dietel, T. Schwecke, S. Herfort, P. Lasch and R. Borriss (2014). “Amylocyclicin, a Novel Circular Bacteriocin Produced by <span class = "named-content genus-species" id = "named-content–1">Bacillus amyloliquefaciens</span> FZB42.” Journal of Bacteriology 196(10): 1842.
Stamatakis, A. (2014). “RAxML version 8: a tool for phylogenetic analysis and post-analysis of large phylogenies.” Bioinformatics 30(9): 1312–1313.
Sullivan, M. J., N. K. Petty and S. A. Beatson (2011). “Easyfig: a genome comparison visualizer.” Bioinformatics 27(7): 1009–1010.
Thage, B. V., F. P. Rattray, M. W. Laustsen, Y. Ardö, V. Barkholt and U. Houlberg (2004). “Purification and characterization of a branched-chain amino acid aminotransferase from Lactobacillus paracasei subsp. paracasei CHCC 2115.” Journal of Applied Microbiology 96(3): 593–602.
Tomita, H., S. Fujimoto, K. Tanimoto and Y. Ike (1997). “Cloning and genetic and sequence analyses of the bacteriocin 21 determinant encoded on the Enterococcus faecalis pheromone-responsive conjugative plasmid pPD1.” Journal of Bacteriology 179(24): 7843.
van de Guchte, M., J. Kok and G. Venema (1991). “Distance-dependent translational coupling and interference in Lactococcus lactis."” Molecular and General Genetics MGG 227(1): 65–71.
von Heijne, G. and L. Abrahmsèn (1989). “Species-specific variation in signal peptide design Implications for protein secretion in foreign hosts.” FEBS Letters 244(2): 439–446.
Wheeler, T. J., J. Clements and R. D. Finn (2014). “Skylign: a tool for creating informative, interactive logos representing sequence alignments and profile hidden Markov models.” BMC Bioinformatics 15(1): 7.
WHO (2017). WHO priority pathogens list for R&D of new antibiotics. W. H. Organisation. https://www.who.int, Organisation.
Wirawan, R. E., K. M. Swanson, T. Kleffmann, R. W. Jack and J. R. Tagg (2007). “Uberolysin: a novel cyclic bacteriocin produced by Streptococcus uberis.” Microbiology 153(5): 1619–1630.
Zamfir, M., R. Callewaert, P. C. Cornea, L. Savu, I. Vatafu and L. De Vuyst (1999). “Purification and characterization of a bacteriocin produced by Lactobacillus acidophilus IBB 801.” Journal of Applied Microbiology 87(6): 923–931.