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Volumn 12, Issue 4, 2013, Pages 685-716

Comparative genome analysis of Bacillus spp. and its relationship with bioactive nonribosomal peptide production

Author keywords

Antibiotic; Bacillus genome; Lipopeptide; Nonribosomal; Peptide; Ribosomal; Siderophore

Indexed keywords

BACITRACIN; CEREXIN DERIVATIVE; CIRCULIN DERIVATIVE; CYCLOPEPTIDE; DECAPEPTIDE; DIPEPTIDE ANTIBIOTIC AGENT; DODECAPEPTIDE; FENGYCIN; HEPTAPEPTIDE; HEXAPEPTIDE; HOMOCEREULIDE; ITURIN DERIVATIVE; LINEAR PENTADECAPEPTIDE DERIVATIVE; LIPODECAPEPTIDE; NONAPEPTIDE; NONRIBOSOMAL BIOACTIVE PEPTIDE; NONRIBOSOMAL PEPTIDE SYNTHETASE; OCTAPEPTIDE; OCTAPEPTIN; POLYMYXIN DERIVATIVE; POLYPEPTIDE ANTIBIOTIC AGENT; POLYPEPTIN PERMETIN DERIVATIVE; RIBOSOMAL BIOACTIVE PEPTIDE; RIBOSOME PROTEIN; SIDEROPHORE; SURFACTIN; TRIDECAPEPTIDE; TRIPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG; UNDECAPEPTIDE; UNINDEXED DRUG;

EID: 84902535612     PISSN: 15687767     EISSN: 1572980X     Source Type: Journal    
DOI: 10.1007/s11101-013-9278-4     Document Type: Review
Times cited : (27)

References (289)
  • 1
    • 69849115536 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of trilactone siderophores: Where chiral recognition occurs in enterobactin and bacillibactin iron transport
    • Abergel RJ, Zawadzka AM, Hoette TM, Raymond KN (2009) Enzymatic hydrolysis of trilactone siderophores: where chiral recognition occurs in enterobactin and bacillibactin iron transport. J Am Chem Soc 131(35):12682-12692
    • (2009) J Am Chem Soc , vol.131 , Issue.35 , pp. 12682-12692
    • Abergel, R.J.1    Zawadzka, A.M.2    Hoette, T.M.3    Raymond, K.N.4
  • 2
    • 0000403532 scopus 로고
    • Production and purification of bacilysin
    • Abraham GF (1965) Production and purification of bacilysin. Biochem J 97(2):573-578
    • (1965) Biochem J , vol.97 , Issue.2 , pp. 573-578
    • Abraham, G.F.1
  • 4
    • 0028233630 scopus 로고
    • A novel dodecadepsipeptide, cereulide, isolated from Bacillus cereus causes vacuole formation in HEp-2 cells
    • DOI 10.1016/0378-1097(94)90141-4
    • Agata N, Mori M, Ohta M, Suwan S, Ohtani I, Isobe M (1994) A novel dodecadepsipeptide, cereulide, isolated from Bacillus cereus causes vacuole formation in HEp-2 cells. FEMS Microbiol Lett 121(1):31-34 (Pubitemid 24223070)
    • (1994) FEMS Microbiology Letters , vol.121 , Issue.1 , pp. 31-34
    • Agata, N.1    Mori, M.2    Ohta, M.3    Suwan, S.4    Ohtani, I.5    Isobe, M.6
  • 7
    • 84902549339 scopus 로고    scopus 로고
    • Peptide antibiotics
    • US Pat. US 2002035239 A1 20020321
    • Andersen RJ, Kelly MT, Barsby TA (2002) Peptide antibiotics. US Pat. US 2002035239 A1 20020321
    • (2002)
    • Andersen, R.J.1    Kelly, M.T.2    Barsby, T.A.3
  • 9
    • 20644458110 scopus 로고    scopus 로고
    • Further aspects on the hemolytic activity of the antibiotic lipopeptide iturin A
    • DOI 10.1016/j.bbamem.2005.05.003, PII S0005273605001240
    • Aranda FJ, Teruel JA, Ortiz A (2005) Further aspects on the hemolytic activity of the antibiotic lipopeptide iturin A. Biochim Biophys Acta Biomembr 1713(1):51-56 (Pubitemid 40835982)
    • (2005) Biochimica et Biophysica Acta - Biomembranes , vol.1713 , Issue.1 , pp. 51-56
    • Aranda, F.J.1    Teruel, J.A.2    Ortiz, A.3
  • 10
    • 71549142267 scopus 로고    scopus 로고
    • Bacillus amyloliquefaciens GA1 as a source of potent antibiotics and other secondary metabolites for biocontrol of plant pathogens
    • Argüelles-Arias A, Ongena M, Halimi B, Lara Y, Brans A, Joris B, Fickers P (2009) Bacillus amyloliquefaciens GA1 as a source of potent antibiotics and other secondary metabolites for biocontrol of plant pathogens. Microb Cell Fact 8:63
    • (2009) Microb Cell Fact , vol.8 , pp. 63
    • Argüelles-Arias, A.1    Ongena, M.2    Halimi, B.3    Lara, Y.4    Brans, A.5    Joris, B.6    Fickers, P.7
  • 11
    • 44849109513 scopus 로고    scopus 로고
    • From soil to gut: Bacillus cereus and its food poisoning toxins
    • DOI 10.1111/j.1574-6976.2008.00112.x
    • Arnesen LPS, Fagerlund A, Granum PE (2008) Fromsoil to gut: Bacillus cereus and its food poisoning toxins. FEMS Microbiol Rev 32:579-606 (Pubitemid 351799686)
    • (2008) FEMS Microbiology Reviews , vol.32 , Issue.4 , pp. 579-606
    • Stenfors, A.L.P.1    Fagerlund, A.2    Granum, P.E.3
  • 12
    • 74049119366 scopus 로고    scopus 로고
    • Iturin A is the principal inhibitor in the biocontrol activity of Bacillus amyloliquefaciens PPCB004 against postharvest fungal pathogens
    • Arrebola E, Jacobs R, Korsten L (2010) Iturin A is the principal inhibitor in the biocontrol activity of Bacillus amyloliquefaciens PPCB004 against postharvest fungal pathogens. J Appl Microbiol 108(2):386-395
    • (2010) J Appl Microbiol , vol.108 , Issue.2 , pp. 386-395
    • Arrebola, E.1    Jacobs, R.2    Korsten, L.3
  • 13
    • 0038073009 scopus 로고    scopus 로고
    • Insecticide activity of surfactins and iturins from a biopesticide Bacillus subtilis Cohn (S499 strain)
    • Assie LK, Deleu M, Arnaud L, Paquot M, Thonart P, Gaspar Ch, Haubruge E (2002) Insecticide activity of surfactins and iturins from a biopesticide Bacillus subtilis Cohn (S499 strain). Biol Wet 67(3):647-655
    • (2002) Biol Wet , vol.67 , Issue.3 , pp. 647-655
    • Assie, L.K.1    Deleu, M.2    Arnaud, L.3    Paquot, M.4    Thonart, P.5    Gaspar, C.6    Haubruge, E.7
  • 14
    • 0842328851 scopus 로고    scopus 로고
    • Biocontrol of Bacillus subtilis against Infection of Arabidopsis Roots by Pseudomonas syringae Is Facilitated by Biofilm Formation and Surfactin Production
    • DOI 10.1104/pp.103.028712
    • Bais HP, Fall R, Vivanco JM (2004) Biocontrol of Bacillus subtilis against infection of arabidopsis roots by Pseudomonas syringae is facilitated by biofilm formation and surfactin production. Plant Physiol 134:307-319 (Pubitemid 38178703)
    • (2004) Plant Physiology , vol.134 , Issue.1 , pp. 307-319
    • Bais, H.P.1    Fall, R.2    Vivanco, J.M.3
  • 15
    • 0342485073 scopus 로고
    • Laterosporin A and laterosporin B antibiotics produced by Bacillus laterosporus
    • Barnes EM (1949) Laterosporin A and laterosporin B antibiotics produced by Bacillus laterosporus. Br J Exp Pathol 30:100-104
    • (1949) Br J Exp Pathol , vol.30 , pp. 100-104
    • Barnes, E.M.1
  • 16
    • 0035825748 scopus 로고    scopus 로고
    • Bogorol A Produced in Culture by a Marine Bacillus sp. Reveals a Novel Template for Cationic Peptide Antibiotics
    • DOI 10.1021/ol006942q
    • Barsby T, Kelly MT, Gagne SM, Andersen RJ, Bogorol A (2001) Produced in culture by a marine Bacillus sp. reveals a novel template for cationic peptide antibiotics. Org Lett 3(3):437-440 (Pubitemid 33693014)
    • (2001) Organic Letters , vol.3 , Issue.3 , pp. 437-440
    • Barsby, T.1    Kelly, M.T.2    Gagne, S.M.3    Andersen, R.J.4
  • 17
    • 0036773509 scopus 로고    scopus 로고
    • Tupuseleiamides and basiliskamides, new acyldipeptides and antifungal polyketides produced in culture by a Bacillus laterosporus isolate obtained from a tropical marine habitat
    • DOI 10.1021/np0201321
    • Barsby T, Kelly MT, Andersen RJ (2002) Tupuseleiamides and basiliskamides, new acyldipeptides and antifungal polyketides produced in culture by a Bacillus laterosporus isolate obtained from a tropical marine habitat. J Nat Prod 65(10):1447-1451 (Pubitemid 35239631)
    • (2002) Journal of Natural Products , vol.65 , Issue.10 , pp. 1447-1451
    • Barsby, T.1    Kelly, M.T.2    Andersen, R.J.3
  • 18
    • 33746903170 scopus 로고    scopus 로고
    • The bogorol family of antibiotics: Template-based structure elucidation and a new approach to positioning enantiomeric pairs of amino acids
    • DOI 10.1021/jo060667p
    • Barsby T, Warabi K, Sorensen D, Zimmerman WT, Kelly MT, Andersen RJ (2006) The bogorol family of antibiotics: template-based structure elucidation and a new approach to positioning enantiomeric pairs of amino acids. J Org Chem 71(16):6031-6037 (Pubitemid 44200271)
    • (2006) Journal of Organic Chemistry , vol.71 , Issue.16 , pp. 6031-6037
    • Barsby, T.1    Warabi, K.2    Sorensen, D.3    Zimmerman, W.T.4    Kelly, M.T.5    Andersen, R.J.6
  • 19
    • 0023273989 scopus 로고
    • Isolation and characterization of new iturins: iturin D and iturin E
    • Besson F, Michel G (1987) Isolation and characterization of new iturins: iturin D and iturin E. J Antibiot 40(4):437-442 (Pubitemid 17115900)
    • (1987) Journal of Antibiotics , vol.40 , Issue.4 , pp. 437-442
    • Besson, F.1    Michel, G.2
  • 20
    • 0025328454 scopus 로고
    • Mycosubtilins B and C: minor antibiotics from mycosubtilin-producer Bacillus subtilis
    • Besson F, Michel G (1990) Mycosubtilins B and C: minor antibiotics from mycosubtilin-producer Bacillus subtilis. Microbios 62(251):93-99 (Pubitemid 20198151)
    • (1990) Microbios , vol.62 , Issue.251 , pp. 93-99
    • Besson, F.1    Michel, G.2
  • 21
    • 0017194446 scopus 로고
    • Characterization of iturin A in antibiotics from various strains of Bacillus subtilis
    • Besson F, Peypoux F, Michel G, Delcambe L (1976) Characterization of iturin A in antibiotics from various strains of Bacillus subtilis. J Antibiot 29(10):1043-1049
    • (1976) J Antibiot , vol.29 , Issue.10 , pp. 1043-1049
    • Besson, F.1    Peypoux, F.2    Michel, G.3    Delcambe, L.4
  • 23
    • 0024450046 scopus 로고
    • Action of mycosubtilin on erythrocytes and artificial membranes
    • Besson F, Quentin MJ, Michel G (1989) Action of mycosubtilin on erythrocytes and artificial membranes. Microbios 59(240-241):137-143 (Pubitemid 19278034)
    • (1989) Microbios , vol.59 , Issue.240-241 , pp. 137-143
    • Besson, F.1    Quentin, M.-J.2    Michel, G.3
  • 24
    • 0031106743 scopus 로고    scopus 로고
    • Polymyxin B nonapeptide: Conformations in water and in the lipopolysaccharide-bound state determined by two-dimensional NMR and molecular dynamics biopolymers
    • Bhattacharjya S, David SA, Mathan VI, Balaram P (1997) Polymyxin B nonapeptide: conformations in water and in the lipopolysaccharide-bound state determined by two-dimensional NMR and molecular dynamics biopolymers. Biopolymers 41:251-265
    • (1997) Biopolymers , vol.41 , pp. 251-265
    • Bhattacharjya, S.1    David, S.A.2    Mathan, V.I.3    Balaram, P.4
  • 25
    • 65349186325 scopus 로고    scopus 로고
    • Entomopathogenic bacteria as a source of secondary metabolites
    • Bode HB (2009) Entomopathogenic bacteria as a source of secondary metabolites. Curr Opin Chem Biol 13:224-230
    • (2009) Curr Opin Chem Biol , vol.13 , pp. 224-230
    • Bode, H.B.1
  • 26
    • 75149160998 scopus 로고    scopus 로고
    • Biosynthesis of rhizocticins, antifungal phosphonate oligopeptides produced by Bacillus subtilis ATCC6633
    • Borisova SA, Circello BT, Zhang JK, van der Donk WA, Metcalf WW (2010) Biosynthesis of rhizocticins, antifungal phosphonate oligopeptides produced by Bacillus subtilis ATCC6633. Chem Biol 17(1):28-37
    • (2010) Chem Biol , vol.17 , Issue.1 , pp. 28-37
    • Borisova, S.A.1    Circello, B.T.2    Zhang, J.K.3    Van Der Donk, W.A.4    Metcalf, W.W.5
  • 29
    • 33750070416 scopus 로고
    • Effect of various inhibitors of protein and deoxyribonucleic acid synthesis on the growth of mycoplasmas
    • Borysiewicz J (1966) Effect of various inhibitors of protein and deoxyribonucleic acid synthesis on the growth of mycoplasmas. Appl Microbiol 14:1049-1050
    • (1966) Appl Microbiol , vol.14 , pp. 1049-1050
    • Borysiewicz, J.1
  • 30
    • 0037378073 scopus 로고    scopus 로고
    • Chromosomal aadD2 encodes an aminoglycoside nucleotidyltransferase in Bacillus clausii
    • DOI 10.1128/AAC.47.4.1343-1346.2003
    • Bozdogan B, Galopin S, Gerbaud G, Courvalin P, Leclercq R (2003) Chromosomal aadD2 encodes an aminoglycoside nucleotidyltransferase in Bacillus clausii. Antimicrob Agents Chemother 47:1343-1346 (Pubitemid 36368595)
    • (2003) Antimicrobial Agents and Chemotherapy , vol.47 , Issue.4 , pp. 1343-1346
    • Bozdogan, B.1    Galopin, S.2    Gerbaud, G.3    Courvalin, P.4    Leclercq, R.5
  • 31
    • 78651007147 scopus 로고
    • Comparative biological studies of polymyxin A and D
    • Brownlee G, Bushby SRM, Short EI (1949) Comparative biological studies of polymyxin A and D. Ann N Y Acad Sci 51:891-896
    • (1949) Ann N Y Acad Sci , vol.51 , pp. 891-896
    • Brownlee, G.1    Bushby, S.R.M.2    Short, E.I.3
  • 32
    • 0014040193 scopus 로고
    • Iron-chelating hydroxamic acid (schizokinen) active in initiation of cell division in Bacillus megaterium
    • Byers BR, Powell MV, Lankford CE (1967) Iron-chelating hydroxamic acid (schizokinen) active in initiation of cell division in Bacillus megaterium. J Bacteriol 93(1):286-294
    • (1967) J Bacteriol , vol.93 , Issue.1 , pp. 286-294
    • Byers, B.R.1    Powell, M.V.2    Lankford, C.E.3
  • 36
    • 48449098635 scopus 로고    scopus 로고
    • Mining microbial genomes for new natural products and biosynthetic pathways
    • Challis GL (2008) Mining microbial genomes for new natural products and biosynthetic pathways. Microbiology 154:1555-1569
    • (2008) Microbiology , vol.154 , pp. 1555-1569
    • Challis, G.L.1
  • 37
    • 84902537568 scopus 로고    scopus 로고
    • Polymyxin A, B, C, D, or E containing compositions for the treatment of periodontal disease, plaque and breath mal-odor
    • Brit. UK Patent GB 2319726
    • Charbonneau DL, Buchanan W, Donovan-Brand RJ (1998) Polymyxin A, B, C, D, or E containing compositions for the treatment of periodontal disease, plaque and breath mal-odor. Brit. UK Patent GB 2319726
    • (1998)
    • Charbonneau, D.L.1    Buchanan, W.2    Donovan-Brand, R.J.3
  • 39
    • 55249127380 scopus 로고    scopus 로고
    • More than anticipated-production of antibiotics and other secondary metabolites by Bacillus amyloliquefaciens
    • Chen X-H, Koumoutsi A, Scholz R, Borriss R (2009a) More than anticipated-production of antibiotics and other secondary metabolites by Bacillus amyloliquefaciens. J Mol Microbiol Biotechnol 16:14-24
    • (2009) J Mol Microbiol Biotechnol , vol.16 , pp. 14-24
    • Chen, X.-H.1    Koumoutsi, A.2    Scholz, R.3    Borriss, R.4
  • 40
    • 61649127530 scopus 로고    scopus 로고
    • Difficidin and bacilysin produced by plant-associated Bacillus amyloliquefaciens are efficient in controlling fire blight disease
    • Chen X-H, Scholz R, Borriss M, Junge H, Moegel G, Kunz S, Borriss R (2009b) Difficidin and bacilysin produced by plant-associated Bacillus amyloliquefaciens are efficient in controlling fire blight disease. J Biotechnol 140:38-44
    • (2009) J Biotechnol , vol.140 , pp. 38-44
    • Chen, X.-H.1    Scholz, R.2    Borriss, M.3    Junge, H.4    Moegel, G.5    Kunz, S.6    Borriss, R.7
  • 42
    • 0014234067 scopus 로고
    • Antibiotic edeine: VII. Biological activity of edeine A and B
    • Chmara H, Borowski E (1968) Antibiotic edeine: VII. Biological activity of edeine A and B. Acta Microbiol Pol 17:59-66
    • (1968) Acta Microbiol Pol , vol.17 , pp. 59-66
    • Chmara, H.1    Borowski, E.2
  • 43
    • 0015930034 scopus 로고
    • Antibiotic tetaine, a new inhibitor of murein precursor's synthesis in Escherichia coli K-12
    • Chmara H, Borowski E (1973) Antibiotic tetaine, a new inhibitor of murein precursor's synthesis in Escherichia coli K-12. Biochem Biophys Res Commun 52(4):1381-1387
    • (1973) Biochem Biophys Res Commun , vol.52 , Issue.4 , pp. 1381-1387
    • Chmara, H.1    Borowski, E.2
  • 46
    • 33750077285 scopus 로고    scopus 로고
    • Structure activity relationship studies on the antimicrobial activity of novel edeine A and D analogues
    • DOI 10.1002/psc.775
    • Czajgucki Z, Andruszkiewicz R, Kamysz W (2006) Structure activity relationship studies on the antimicrobial activity of novel edeine A and D analogues. J Pept Sci 12:653-662 (Pubitemid 44574894)
    • (2006) Journal of Peptide Science , vol.12 , Issue.10 , pp. 653-662
    • Czajgucki, Z.1    Andruszkiewicz, R.2    Kamysz, W.3
  • 47
    • 0020422783 scopus 로고
    • Antibacterial action of gramicidin S and tyrocidines in relation to active transport, in vitro transcription, and spore outgrowth
    • Danders W, Marahiel MA, Krause M, Kosui N, Katom T, Izumiya N, Kleinkauf H (1982) Antibacterial action of gramicidin S and tyrocidines in relation to active transport, in vitro transcription, and spore outgrowth. Antimicrob Agents Chemother 22(5):785-790 (Pubitemid 13210055)
    • (1982) Antimicrobial Agents and Chemotherapy , vol.22 , Issue.5 , pp. 785-790
    • Danders, W.1    Marahiel, M.A.2    Krause, M.3
  • 48
    • 0029038652 scopus 로고
    • New dimensions in natural products research: Cultured marine microorganisms
    • Davidson B (1995) New dimensions in natural products research: cultured marine microorganisms. Curr Opin Biotechnol 6:284-291
    • (1995) Curr Opin Biotechnol , vol.6 , pp. 284-291
    • Davidson, B.1
  • 49
    • 41649113580 scopus 로고    scopus 로고
    • Effect of fengycin, a lipopeptide produced by Bacillus subtilis, on model biomembranes
    • Deleu M, Paquot M, Nylander T (2008) Effect of fengycin, a lipopeptide produced by Bacillus subtilis, on model biomembranes. Biophys J 94:2667-2679
    • (2008) Biophys J , vol.94 , pp. 2667-2679
    • Deleu, M.1    Paquot, M.2    Nylander, T.3
  • 50
    • 79651472963 scopus 로고    scopus 로고
    • Transcriptional kinetic analyses of cereulide synthetase genes with respect to growth, sporulation and emetic toxin production in Bacillus cereus
    • Dommel MK, Lücking G, Scherer S, Ehling-Schulz M (2011) Transcriptional kinetic analyses of cereulide synthetase genes with respect to growth, sporulation and emetic toxin production in Bacillus cereus. Food Microbiol 28:284-290
    • (2011) Food Microbiol , vol.28 , pp. 284-290
    • Dommel, M.K.1    Lücking, G.2    Scherer, S.3    Ehling-Schulz, M.4
  • 51
    • 0027517868 scopus 로고
    • Bacillus cereus and related species
    • Drobniewsk FA (1993) Bacillus cereus and related species. Clin Microbiol Rev 6:324-338
    • (1993) Clin Microbiol Rev , vol.6 , pp. 324-338
    • Drobniewsk, F.A.1
  • 52
    • 10444239437 scopus 로고    scopus 로고
    • Bacillus cereus, the causative agent of an emetic type of food-borne illness
    • DOI 10.1002/mnfr.200400055
    • Ehling-Schulz M, Fricker M, Scherer S (2004) Bacillus cereus, the causative agent of an emetic type of food-borne illness. Mol Nutr Food Res 48:479-487 (Pubitemid 39643690)
    • (2004) Molecular Nutrition and Food Research , vol.48 , Issue.7 , pp. 479-487
    • Ehling-Schulz, M.1    Fricker, M.2    Scherer, S.3
  • 53
    • 33646699589 scopus 로고    scopus 로고
    • Cereulide synthetase gene cluster from emetic Bacillus cereus: Structure and location on a mega virulence plasmid related to Bacillus anthracis toxin plasmid pXO1
    • Ehling-Schulz M, Fricker M, Grallert H, Rieck P, Wagner M, Scherer S (2006) Cereulide synthetase gene cluster from emetic Bacillus cereus: structure and location on a mega virulence plasmid related to Bacillus anthracis toxin plasmid pXO1. BMC Microbiol 6:20
    • (2006) BMC Microbiol , vol.6 , pp. 20
    • Ehling-Schulz, M.1    Fricker, M.2    Grallert, H.3    Rieck, P.4    Wagner, M.5    Scherer, S.6
  • 54
    • 33444455640 scopus 로고
    • Industrial applications of the bacilli: A review and prospectus
    • Schlesinger D (ed) ASM Press, Washington, DC
    • Erickson RJ (1976) Industrial applications of the bacilli: a review and prospectus. In: Schlesinger D (ed) Microbiology. ASM Press, Washington, DC, pp 406-419
    • (1976) Microbiology , pp. 406-419
    • Erickson, R.J.1
  • 55
    • 0028970606 scopus 로고
    • Bacillomycin Lc, a new antibiotic of the iturin group: Isolations, structures, and antifungal activities of the congeners
    • Eshita SM, Roberto NH, Beale JM, Mamiya BM, Workman RF (1995) Bacillomycin Lc, a new antibiotic of the iturin group: isolations, structures, and antifungal activities of the congeners. J Antibiot 48(11):1240-1247 (Pubitemid 3015929)
    • (1995) Journal of Antibiotics , vol.48 , Issue.11 , pp. 1240-1247
    • Eshita, S.M.1    Roberto, N.H.2    Beale, J.M.3    Mamiya, B.M.4    Workman, R.F.5
  • 56
    • 9244234513 scopus 로고    scopus 로고
    • Biosynthesis of nonribosomal peptides
    • DOI 10.1146/annurev.micro.58.030603.123615
    • Finking R, Marahiel MA (2004) Biosynthesis of nonribosomal peptides. Annu Rev Microbiol 58:453-488 (Pubitemid 39551994)
    • (2004) Annual Review of Microbiology , vol.58 , pp. 453-488
    • Finking, R.1    Marahiel, M.A.2
  • 57
    • 33748631825 scopus 로고    scopus 로고
    • Assembly-line enzymology for polyketide and nonribosomal peptide antibiotics: Logic, machinery, and mechanisms
    • and references therein cited
    • Fischbach MA, Walsh CT (2006) Assembly-line enzymology for polyketide and nonribosomal peptide antibiotics: logic, machinery, and mechanisms. Chem Rev 106:3468-3496 and references therein cited
    • (2006) Chem Rev , vol.106 , pp. 3468-3496
    • Fischbach, M.A.1    Walsh, C.T.2
  • 58
    • 24944575227 scopus 로고    scopus 로고
    • Commercialization and implementation of biocontrol
    • Fravel DR (2005) Commercialization and implementation of biocontrol. Ann Rev Phytopathol 43:A337-A359
    • (2005) Ann Rev Phytopathol , vol.43
    • Fravel, D.R.1
  • 59
    • 33947113822 scopus 로고    scopus 로고
    • Food poisoning associated with pumilacidin-producing Bacillus pumilus in rice
    • DOI 10.1016/j.ijfoodmicro.2006.11.005, PII S0168160507000359
    • From C, Hormazabal V, Granum PE (2007) Food poisoning associated with pumilacidin-producing Bacillus pumilus in rice. Int J Food Microbiol 115(3):319-324 (Pubitemid 46400880)
    • (2007) International Journal of Food Microbiology , vol.115 , Issue.3 , pp. 319-324
    • From, C.1    Hormazabal, V.2    Granum, P.E.3
  • 62
    • 3242754298 scopus 로고    scopus 로고
    • Temperature control of a 3,4-dihydroxybenzoate (protocatechuate)-based siderophore in Bacillus anthracis
    • Garner BL, Arceneaux JEL, Byers BR (2004) Temperature control of a 3,4-dihydroxybenzoate (protocatechuate)-based siderophore in Bacillus anthracis. Curr Microbiol 49(2):89-94 (Pubitemid 38970712)
    • (2004) Current Microbiology , vol.49 , Issue.2 , pp. 89-94
    • Garner, B.L.1    Arceneaux, J.E.L.2    Byers, B.R.3
  • 63
    • 0032909767 scopus 로고    scopus 로고
    • Loloatins A-D, cyclic decapeptide antibiotics produced in culture by a tropical marine bacterium
    • DOI 10.1021/np980219f
    • Gerard JM, Haden P, Kelly MT, Andersen RJ (1999) Loloatins A-D, cyclic decapeptide antibiotics produced in culture by a tropical marine bacterium. J Nat Prod 62(1):80-85 (Pubitemid 29071381)
    • (1999) Journal of Natural Products , vol.62 , Issue.1 , pp. 80-85
    • Gerard, J.M.1    Haden, P.2    Kelly, M.T.3    Andersen, R.J.4
  • 64
    • 0032937687 scopus 로고    scopus 로고
    • Lichenysins G, a novel family of lipopeptide biosurfactants from Bacillus licheniformis IM 1307: Production, isolation and structural evaluation by NMR and mass spectrometry
    • Grangemard I, Bonmatin JM, Bernillon J, Das BC, Peypoux F (1999) Lichenysin G, novel family of lipopeptide biosurfactants from Bacillus licheniformis IM 1307: production, isolation and structural evaluation by NMR and mass spectrometry. J Antibiot 52:363-373 (Pubitemid 29213528)
    • (1999) Journal of Antibiotics , vol.52 , Issue.4 , pp. 363-373
    • Grangemard, I.1    Bonmatin, J.-M.2    Bernillon, J.3    Das, B.C.4    Peypoux, F.5
  • 66
    • 18344389724 scopus 로고    scopus 로고
    • Structure investigation of maltacine B1a, B1b, B2a and B2b: Cyclic peptide lactones of the maltacine complex from Bacillus subtilis
    • Hagelin G (2005a) Structure investigation of maltacine B1a, B1b, B2a and B2b: cyclic peptide lactones of the maltacine complex from Bacillus subtilis. J Mass Spectrom 40(4):527-538
    • (2005) J Mass Spectrom , vol.40 , Issue.4 , pp. 527-538
    • Hagelin, G.1
  • 67
    • 27644477396 scopus 로고    scopus 로고
    • Structure investigation of maltacine C1a, C1b, C2a and C2b: Cyclic peptide lactones of the maltacine complex from Bacillus subtilis
    • Hagelin G (2005b) Structure investigation of maltacine C1a, C1b, C2a and C2b: cyclic peptide lactones of the maltacine complex from Bacillus subtilis. J Mass Spectrom 40(10):1276-1286
    • (2005) J Mass Spectrom , vol.40 , Issue.10 , pp. 1276-1286
    • Hagelin, G.1
  • 68
    • 27644554179 scopus 로고    scopus 로고
    • Structure investigation of maltacine D1a, D1b and D1c: Cyclic peptide lactones of the maltacine complex from Bacillus subtilis
    • Hagelin G (2005c) Structure investigation of maltacine D1a, D1b and D1c: cyclic peptide lactones of the maltacine complex from Bacillus subtilis. J Mass Spectrom 40(10):1287-1299
    • (2005) J Mass Spectrom , vol.40 , Issue.10 , pp. 1287-1299
    • Hagelin, G.1
  • 69
    • 29144516713 scopus 로고    scopus 로고
    • Mass spectrometric investigation of maltacines E1a and E1b - 2 members of the maltacine family of peptide antibiotics
    • Hagelin G (2005d) Mass spectrometric investigation of maltacines E1a and E1b - 2 members of the maltacine family of peptide antibiotics. Rapid Commun Mass Spectrom 19(24):3633-3642
    • (2005) Rapid Commun Mass Spectrom , vol.19 , Issue.24 , pp. 3633-3642
    • Hagelin, G.1
  • 70
    • 35748956433 scopus 로고    scopus 로고
    • Use of synthetic analogues in confirmation of structure of the peptide antibiotics maltacines
    • Hagelin G, Indrevoll B, Hoeg-Jensen T (2007) Use of synthetic analogues in confirmation of structure of the peptide antibiotics maltacines. Int J Mass Spectrom 268:254-264
    • (2007) Int J Mass Spectrom , vol.268 , pp. 254-264
    • Hagelin, G.1    Indrevoll, B.2    Hoeg-Jensen, T.3
  • 73
    • 0024501479 scopus 로고
    • Methylation of the antifungal lipopeptide iturin A modifies its interaction with lipids
    • Harnois I, Maget-Dana R, Ptak M (1989) Methylation of the antifungal lipopeptide iturin A modifies its interaction with lipids. Biochimie 71(1):111-116 (Pubitemid 19065452)
    • (1989) Biochimie , vol.71 , Issue.1 , pp. 111-116
    • Harnois, I.1    Maget-Dana, R.2    Ptak, M.3
  • 74
    • 0026752273 scopus 로고
    • Bacillus subtilis and its relatives: Molecular biological and industrial workhorses
    • Harwood CR (1992) Bacillus subtilis and its relatives: molecular biological and industrial workhorses. Trends Biotechnol 10:247-256
    • (1992) Trends Biotechnol , vol.10 , pp. 247-256
    • Harwood, C.R.1
  • 75
    • 39049125071 scopus 로고    scopus 로고
    • Bacillus protein secretion: An unfolding story
    • Harwood CR, Cranenburgh R (2008) Bacillus protein secretion: an unfolding story. Trends Microbiol 16:73-79
    • (2008) Trends Microbiol , vol.16 , pp. 73-79
    • Harwood, C.R.1    Cranenburgh, R.2
  • 76
    • 0029610597 scopus 로고
    • Inhibition of acyl-CoA:cholesterol acyltransferase by isohalobacillin, a complex of novel cyclic acylpeptides produced by Bacillus sp. A1238
    • Hasumi K, Takizawa K, Takahashi F, Park JK, Endo A (1995) Inhibition of Acyl-CoA: cholesterol acyltransferase by isohalobacillin, a complex of novel cyclic acylpeptides produced by Bacillus sp. A1238. J Antibiot 48(12):1419-1424 (Pubitemid 26016900)
    • (1995) Journal of Antibiotics , vol.48 , Issue.12 , pp. 1419-1424
    • Hasumi, K.1    Takizawa, K.2    Takahashi, F.3    Park, J.K.4    Endo, A.5
  • 77
    • 0033709514 scopus 로고    scopus 로고
    • Kurstakins: A new class of lipopeptides isolated from Bacillus thuringiensis
    • Hathout Y, Ho Y-P, Ryzhov V, Demirev P, Fenselau C (2000) Kurstakins: a new class of lipopeptides isolated from Bacillus thuringiensis. J Nat Prod 63(11):1492-1496
    • (2000) J Nat Prod , vol.63 , Issue.11 , pp. 1492-1496
    • Hathout, Y.1    Ho, Y.-P.2    Ryzhov, V.3    Demirev, P.4    Fenselau, C.5
  • 79
    • 10644274361 scopus 로고    scopus 로고
    • Towards a comprehensive understanding of Bacillus subtilis cell physiology by physiological proteomics
    • DOI 10.1002/pmic.200401017
    • Hecker M, Voelker U (2004) Towards a comprehensive understanding of Bacillus subtilis cell physiology by physiological proteomics. Proteomics 4:3727-3750 (Pubitemid 39657451)
    • (2004) Proteomics , vol.4 , Issue.12 , pp. 3727-3750
    • Hecker, M.1    Volker, U.2
  • 80
    • 0034000835 scopus 로고    scopus 로고
    • Genetic structure of population of Bacillus cereus and B. thuringiensis Isolates associated with periodontitis and other human infections
    • Helgason E, Caugant DA, Olsen I, Kolsto A-B (2000) Genetic structure of population of Bacillus cereus and B. thuringiensis isolates associated with periodontitis and other human infections. J Clin Microbiol 38:1615-1622 (Pubitemid 30216698)
    • (2000) Journal of Clinical Microbiology , vol.38 , Issue.4 , pp. 1615-1622
    • Helgason, E.1    Caugant, D.A.2    Olsen, I.3    Kolsto, A.-B.4
  • 81
    • 0019131638 scopus 로고
    • Phospholipid methylation and biological signal transmission
    • Hirata F, Axelrod J (1980) Phospholipid methylation and biological signal transmission. Science 209:1082-1090 (Pubitemid 11235466)
    • (1980) Science , vol.209 , Issue.4461 , pp. 1082-1090
    • Hirata, F.1    Axelrod, J.2
  • 83
    • 23844544940 scopus 로고    scopus 로고
    • The use of bacterial spore formers as probiotics
    • DOI 10.1016/j.femsre.2004.12.001, PII S0168644504000890
    • Hong HA, Duc L-H, Cutting SM (2005) The use of bacterial spore formers as probiotics. FEMS Microbiol Rev 29:813-835 (Pubitemid 41149050)
    • (2005) FEMS Microbiology Reviews , vol.29 , Issue.4 , pp. 813-835
    • Hong, H.A.1    Le, H.D.2    Cutting, S.M.3
  • 84
    • 0028876159 scopus 로고
    • Isolation and characterization of the siderophore N-deoxyschizokinen from Bacillus megaterium ATCC 19213
    • Hu X, Boyer GL (1995) Isolation and characterization of the siderophore N-deoxyschizokinen from Bacillus megaterium ATCC 19213. Biometals 8(4):357-364
    • (1995) Biometals , vol.8 , Issue.4 , pp. 357-364
    • Hu, X.1    Boyer, G.L.2
  • 85
    • 0029805914 scopus 로고    scopus 로고
    • Siderophore-mediated aluminum uptake by Bacillus megaterium ATCC 19213
    • Hu X, Boyer GL (1996) Siderophore-mediated aluminum uptake by Bacillus megaterium ATCC 19213. Appl Environ Microbiol 62(11):4044-4048 (Pubitemid 26371504)
    • (1996) Applied and Environmental Microbiology , vol.62 , Issue.11 , pp. 4044-4048
    • Hu, X.1    Boyer, G.L.2
  • 86
    • 33749645818 scopus 로고    scopus 로고
    • Functional analysis of 11 putative essential genes in Bacillus subtilis
    • DOI 10.1099/mic.0.29152-0
    • Hunt A, Rawlins JP, Thomaides HB, Errington J (2006) Functional analysis of 11 putative essential genes in Bacillus subtilis. Microbiology 152:2895-2907 (Pubitemid 44542371)
    • (2006) Microbiology , vol.152 , Issue.10 , pp. 2895-2907
    • Hunt, A.1    Rawlins, J.P.2    Thomaides, H.B.3    Errington, J.4
  • 87
    • 0036064383 scopus 로고    scopus 로고
    • Extracellular phytase activity of Bacillus amyloliquefaciens FZB45 contributes to its plant-growth-promoting effect
    • Idriss EE, Makarewicz O, Farouk A, Rosner K, Greiner R, Bochow H, Richter T, Borriss R (2002) Extracellular phytase activity of Bacillus amyloliquefaciens FZB45 contributes to its plant-growth-promoting effect. Microbiology 148:2097-2109 (Pubitemid 34785294)
    • (2002) Microbiology , vol.148 , Issue.7 , pp. 2097-2109
    • Idriss, E.E.1    Makarewicz, O.2    Farouk, A.3    Rosner, K.4    Greiner, R.5    Bochow, H.6    Richter, T.7    Borriss, R.8
  • 88
    • 0027194703 scopus 로고
    • Enzymatic determination of itoic acid, a Bacillus subtilis siderophore, and 2,3-dihydroxybenzoic acid
    • Ito T (1993) Enzymatic determination of itoic acid, a Bacillus subtilis siderophore, and 2,3-dihydroxybenzoic acid. Appl Environ Microbiol 59(7):2343-2345
    • (1993) Appl Environ Microbiol , vol.59 , Issue.7 , pp. 2343-2345
    • Ito, T.1
  • 90
    • 0037483046 scopus 로고    scopus 로고
    • Bacillus species proteins involved in spore formation and degradation: From identification in the genome, to sequence analysis, and determination of function and structure
    • Jedrzejas MJ, Huang WJM (2003) Bacillus species proteins involved in spore formation and degradation: from identification in the genome, to sequence analysis, and determination of function and structure. Crit Rev Biochem Mol Biol 38:173-198 (Pubitemid 36798099)
    • (2003) Critical Reviews in Biochemistry and Molecular Biology , vol.38 , Issue.3 , pp. 173-198
    • Jedrzejas, M.J.1    Huang, W.J.M.2
  • 91
    • 0000439339 scopus 로고
    • Lipopeptide production by Bacillus licheniformis
    • Kosaric N (ed) Dekker, Inc, New York
    • Jenny K, Deltrieu V, Kappeli O (1993) Lipopeptide production by Bacillus licheniformis. In: Kosaric N (ed) Biosurfactants. Dekker, Inc, New York, pp 135-156
    • (1993) Biosurfactants , pp. 135-156
    • Jenny, K.1    Deltrieu, V.2    Kappeli, O.3
  • 92
    • 64749112297 scopus 로고    scopus 로고
    • Insights into the defense-related events occurring in plant cells following perception of surfactin-type lipopeptide from Bacillus subtilis
    • Jourdan E, Henry G, Duby F, Dommes J, Barthelemy JP, Thonart P, Ongena M (2009) Insights into the defense-related events occurring in plant cells following perception of surfactin-type lipopeptide from Bacillus subtilis. Mol Plant Microbe Interact 22:456-468
    • (2009) Mol Plant Microbe Interact , vol.22 , pp. 456-468
    • Jourdan, E.1    Henry, G.2    Duby, F.3    Dommes, J.4    Barthelemy, J.P.5    Thonart, P.6    Ongena, M.7
  • 93
    • 0030994849 scopus 로고    scopus 로고
    • Fusaricidins B, C and D, new depsipeptide antibiotics produced by Bacillus polymyxa KT-8: Isolation, structure elucidation and biological activity
    • Kajimura Y, Kaneda M (1997) Fusaricidins B, C and D, new depsipeptide antibiotics produced by Bacillus polymyxa KT-8: isolation, structure elucidation and biological activity. J Antibiot 50(3):220-228 (Pubitemid 27170588)
    • (1997) Journal of Antibiotics , vol.50 , Issue.3 , pp. 220-228
    • Kajimura, Y.1    Kaneda, M.2
  • 94
    • 0028845111 scopus 로고
    • Bacillopeptins, new cyclic lipopeptide antibiotics from Bacillus subtilis FR-2
    • Kajimura Y, Sugiyama M, Kaneda M (1995) Bacillopeptins, new cyclic lipopeptide antibiotics from Bacillus subtilis FR-2. J Antibiot 48(10):1095-1103
    • (1995) J Antibiot , vol.48 , Issue.10 , pp. 1095-1103
    • Kajimura, Y.1    Sugiyama, M.2    Kaneda, M.3
  • 95
    • 0016159471 scopus 로고
    • Antitumor activity of Bacillus natto V. Isolation and characterization of surfactin in the culture medium of Bacillus natto KMD 2311
    • Kameda Y, Oira S, Matsui K, Kanatomo S, Hase T (1974) Antitumor activity of Bacillus natto V. Isolation and characterization of surfactin in the culture medium of Bacillus natto KMD 2311. Chem Pharm Bull 22:938-944
    • (1974) Chem Pharm Bull , vol.22 , pp. 938-944
    • Kameda, Y.1    Oira, S.2    Matsui, K.3    Kanatomo, S.4    Hase, T.5
  • 96
    • 0015601324 scopus 로고
    • Probable identity of bacilysin and tetaine
    • Kaminski K, Sokolowska T (1973) Probable identity of bacilysin and tetaine. J Antibiot 26(3):184-185
    • (1973) J Antibiot , vol.26 , Issue.3 , pp. 184-185
    • Kaminski, K.1    Sokolowska, T.2
  • 97
    • 0036728060 scopus 로고    scopus 로고
    • New antifungal antibiotics, bacillopeptins and fusaricidins
    • DOI 10.1248/yakushi.122.651
    • Kaneda M, Kajimura Y (2002) New antifungal antibiotics, bacillopeptins and fusaricidins. Yakugaku Zasshi-J Pharm Soc Jpn 122(9):651-671 (Pubitemid 41320981)
    • (2002) Yakugaku Zasshi , vol.122 , Issue.9 , pp. 651-671
    • Kaneda, M.1    Kajimura, Y.2
  • 98
    • 0017055251 scopus 로고
    • 1 (333-25): studies on antibiotics from the genus Bacillus, XIX
    • Kato T, Shoji J (1976) Studies on antibiotics from the genus Bacillus. XIX. The amino acid sequence of octapeptin C1 (333-25). J Antibiot 29(12):1339-1340 (Pubitemid 8018020)
    • (1976) Journal of Antibiotics , vol.29 , Issue.12 , pp. 1339-1340
    • Kato, T.1    Shoji, J.2
  • 99
    • 0018860737 scopus 로고
    • The structure of octapeptin D. (Studies on antibiotics from the genus Bacillus. XXVIII)
    • Kato T, Shoji J (1980) Studies on antibiotics from the genus Bacillus. XXVIII. The structure of octapeptin D. J Antibiot 33(2):186-191 (Pubitemid 10066234)
    • (1980) Journal of Antibiotics , vol.33 , Issue.2 , pp. 186-191
    • Kato, T.1    Shoji, J.2
  • 100
    • 0018076714 scopus 로고
    • The structure of tridecaptin A (Studies on antibiotics from the genus Bacillus. XXIV)
    • Kato T, Hinoo H, Shoji J (1978) Studies on antibiotics from the genus Bacillus. XXIV. The structure of tridecaptin A. J Antibiot 31(7):652-661 (Pubitemid 9002298)
    • (1978) Journal of Antibiotics , vol.31 , Issue.7 , pp. 652-661
    • Kato, T.1    Hinoo, H.2    Shoji, J.3
  • 101
    • 0018363557 scopus 로고
    • The structures of tridecaptins B and C. (Studies on antibiotics from the genus Bacillus. XXV)
    • Kato T, Sakazaki R, Hinoo H, Shoji J (1979) Studies on antibiotics from the genus Bacillus. XXV. The structures of tridecaptins B and C. J Antibiot 32(4):305-312 (Pubitemid 9189891)
    • (1979) Journal of Antibiotics , vol.32 , Issue.4 , pp. 305-312
    • Kato, T.1    Sakazaki, R.2    Hinoo, H.3    Shoji, J.4
  • 103
    • 34548481061 scopus 로고    scopus 로고
    • The gramicidin ion channel: A model membrane protein
    • DOI 10.1016/j.bbamem.2007.05.011, PII S0005273607001848
    • Kelkar DA, Chattopadhyay A (2007) The gramicidin ion channel: a model membrane protein. Biochim Biophys Acta 1768:2011-2025 (Pubitemid 47379614)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.9 , pp. 2011-2025
    • Kelkar, D.A.1    Chattopadhyay, A.2
  • 104
    • 59949101152 scopus 로고    scopus 로고
    • Characterization of the complete zwittermicin A biosynthesis gene cluster from Bacillus cereus
    • Kevany BM, Rasko DA, Thomas MG (2009) Characterization of the complete zwittermicin A biosynthesis gene cluster from Bacillus cereus. Appl Environ Microbiol 75(4):1144-1155
    • (2009) Appl Environ Microbiol , vol.75 , Issue.4 , pp. 1144-1155
    • Kevany, B.M.1    Rasko, D.A.2    Thomas, M.G.3
  • 105
    • 0016016280 scopus 로고
    • Optimization of the medium for the biosynthesis of esein and bresein using a mathematical experiment design
    • Kherat DM, Maksimov VN, Zharikova GG (1974) Optimization of the medium for the biosynthesis of esein and bresein using a mathematical experiment design. Biol Nauki 17(1):90-94
    • (1974) Biol Nauki , vol.17 , Issue.1 , pp. 90-94
    • Kherat, D.M.1    Maksimov, V.N.2    Zharikova, G.G.3
  • 106
    • 0037193181 scopus 로고    scopus 로고
    • Enhancement of plasminogen activation by surfactin C: Augmentation of fibrinolysis in vitro and in vivo
    • DOI 10.1016/S0167-4838(02)00221-2, PII S0167483802002212
    • Kikuchi T, Hasumi K (2002) Enhancement of plasminogen activation by surfactin C: augmentation of fibrinolysis in vitro and in vivo. Biochim Biophys Acta 1596(2):234-245 (Pubitemid 34455050)
    • (2002) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1596 , Issue.2 , pp. 234-245
    • Kikuchi, T.1    Hasumi, K.2
  • 108
  • 109
    • 0038408202 scopus 로고
    • The chemistry of tyrocidine. V. The amino acid sequence of tyrocidine B
    • King TP, Craig LC (1955) The chemistry of tyrocidine. V. The amino acid sequence of tyrocidine B. J Am Chem Soc 77:6627-6631
    • (1955) J Am Chem Soc , vol.77 , pp. 6627-6631
    • King, T.P.1    Craig, L.C.2
  • 110
    • 67149125327 scopus 로고    scopus 로고
    • A novel L-amino acid ligase from Bacillus subtilis NBRC3134, a microorganism producing peptide-antibiotic rhizocticin
    • Kino K, Kotanaka Y, Arai T, Yagasaki M (2009) A novel L-amino acid ligase from Bacillus subtilis NBRC3134, a microorganism producing peptide-antibiotic rhizocticin. Biosci Biotechnol Biochem 73(4):901-907
    • (2009) Biosci Biotechnol Biochem , vol.73 , Issue.4 , pp. 901-907
    • Kino, K.1    Kotanaka, Y.2    Arai, T.3    Yagasaki, M.4
  • 111
    • 0035083897 scopus 로고    scopus 로고
    • Synthesis and characterization of the colistin peptide polymyxin E1 and related antimicrobial peptides
    • DOI 10.1046/j.1397-002X.2,000.00000.x
    • Kline T, Holub D, Therrien J, Leung T, Ryckman D (2001) Synthesis and characterization of the colistin peptide polymixin E1 and related antimicrobial peptides. J Pept Res 57:175-187 (Pubitemid 32232059)
    • (2001) Journal of Peptide Research , vol.57 , Issue.3 , pp. 175-187
    • Kline, T.1    Holub, D.2    Therrien, J.3    Leung, T.4    Ryckman, D.5
  • 112
    • 33847599810 scopus 로고
    • Enhanced plant growth by siderophores produced by plant growth-promoting rhizobacteria
    • Kloepper JW, Leong J, Teintze M, Schroth MN (1980) Enhanced plant growth by siderophores produced by plant growth-promoting rhizobacteria. Nature 286:885-886
    • (1980) Nature , vol.286 , pp. 885-886
    • Kloepper, J.W.1    Leong, J.2    Teintze, M.3    Schroth, M.N.4
  • 113
    • 0021854185 scopus 로고
    • Gramicidin K, a new linear channel-forming gramicidin from Bacillus brevis
    • DOI 10.1021/bi00333a002
    • Koeppe RE, Paczkowski JA, Whaley WL (1985) Gramicidin K, a new linear channel-forming gramicidin from Bacillus brevis. Biochemistry 24(12):2822-2826 (Pubitemid 15004427)
    • (1985) Biochemistry , vol.24 , Issue.12 , pp. 2822-2826
    • Koeppe II, R.E.1    Paczkowski, J.A.2    Whaley, W.L.3
  • 114
  • 115
    • 0033080078 scopus 로고    scopus 로고
    • How do peptide synthetases generate structural diversity?
    • Konz D, Marahiel MA (1999) How do peptide synthetases generate structural diversity? Chem Biol 6:39-48
    • (1999) Chem Biol , vol.6 , pp. 39-48
    • Konz, D.1    Marahiel, M.A.2
  • 116
    • 0032955583 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of the protein template controlling biosynthesis of the lipopeptide lichenysin
    • Konz D, Doekel S, Marahiel AM (1999) Molecular and biochemical characterization of the protein template controlling biosynthesis of the lipopeptide lichenysin. J Bacteriol 181:133-140 (Pubitemid 29013663)
    • (1999) Journal of Bacteriology , vol.181 , Issue.1 , pp. 133-140
    • Konz, D.1    Doekel, S.2    Marahiel, M.A.3
  • 117
    • 29744459466 scopus 로고    scopus 로고
    • Petrobactin is the primary siderophore synthesized by Bacillus anthracis str. Sterne under conditions of iron starvation
    • DOI 10.1007/s10534-005-1782-6
    • Koppisch AT, Browder CC, Moe AL, Shelley JT, Kinkel BA, Hersman LE, Iyer S, Ruggiero CE (2005) Petrobactin is the primary siderophore synthesized by Bacillus anthracis str. Sterne under conditions of iron starvation. Biometals 18:577-585 (Pubitemid 43030279)
    • (2005) BioMetals , vol.18 , Issue.6 , pp. 577-585
    • Koppisch, A.T.1    Browder, C.C.2    Moe, A.L.3    Shelley, J.T.4    Kinkel, B.A.5    Hersman, L.E.6    Iyer, S.7    Ruggiero, C.E.8
  • 118
    • 59649107763 scopus 로고    scopus 로고
    • Biological control of post harvest disease caused by Aspergillus flavus on stored lemon fruits
    • Kotan R, Dikbas N, Bostan H (2009) Biological control of post harvest disease caused by Aspergillus flavus on stored lemon fruits. Afr J Biotechnol 8:209-214
    • (2009) Afr J Biotechnol , vol.8 , pp. 209-214
    • Kotan, R.1    Dikbas, N.2    Bostan, H.3
  • 119
    • 1142298587 scopus 로고    scopus 로고
    • Structural and Functional Characterization of Gene Clusters Directing Nonribosomal Synthesis of Bioactive Cyclic Lipopeptides in Bacillus amyloliquefaciens Strain FZB42
    • DOI 10.1128/JB.186.4.1084-1096.2004
    • Koumoutsi A, Chen X-H, Henne A, Liesegang H, Hitzeroth G, Franke P, Vater J, Borriss R (2004) Structural and functional characterization of gene clusters directing nonribosomal synthesis of bioactive cyclic lipopeptides in Bacillus amyloliquefaciens strain FZB42. J Bacteriol 186:1084-1096 (Pubitemid 38209468)
    • (2004) Journal of Bacteriology , vol.186 , Issue.4 , pp. 1084-1096
    • Koumoutsi, A.1    Chen, X.-H.2    Henne, A.3    Liesegang, H.4    Hitzeroth, G.5    Franke, P.6    Vater, J.7    Borriss, R.8
  • 120
    • 35948941266 scopus 로고    scopus 로고
    • DegU and YczE positively regulate the synthesis of bacillomycin D by Bacillus amyloliquefaciens strain FZB42
    • DOI 10.1128/AEM.00565-07
    • Koumoutsi A, Chen X-H, Vater J, Borriss R (2007) DegU and YczE positively regulate the synthesis of bacillomycin D by Bacillus amyloliquefaciens strain FZB42. Appl Environ Microbiol 73:6953-6964 (Pubitemid 350076816)
    • (2007) Applied and Environmental Microbiology , vol.73 , Issue.21 , pp. 6953-6964
    • Koumoutsi, A.1    Chen, X.-H.2    Vater, J.3    Borriss, R.4
  • 121
    • 0032767622 scopus 로고    scopus 로고
    • Antiviral and hemolytic activities of surfactin isoforms and their methyl ester derivatives
    • Kracht M, Rokos H, Ozel M, Kowall M, Pauli G, Vater J (1999) Antiviral and hemolytic activities of surfactin isoforms and their methyl ester derivatives. J Antibiot 52:613-619 (Pubitemid 29378218)
    • (1999) Journal of Antibiotics , vol.52 , Issue.7 , pp. 613-619
    • Kracht, M.1    Rokos, H.2    Ozel, M.3    Kowall, M.4    Pauli, G.5    Vater, J.6
  • 122
    • 0025190444 scopus 로고
    • Rhizocticin A, an antifungal phosphono-oligopeptide of Bacillus subtilis ATCC 6633: Biological properties
    • Kugler M, Loeffler W, Rapp C, Kern A, Jung G (1990) Rhizocticin A, an antifungal phosphono-oligopeptide of Bacillus subtilis ATCC 6633: biological properties. Arch Microbiol 153(3):276-281 (Pubitemid 20057961)
    • (1990) Archives of Microbiology , vol.153 , Issue.3 , pp. 276-281
    • Kugler, M.1    Loeffler, W.2    Rapp, C.3    Kern, A.4    Jung, G.5
  • 124
    • 0015496384 scopus 로고
    • Inhibition of bacterial DNA synthesis by edeine. Effect on Escherichia coli mutants lacking DNA polymerase I
    • Kuryło-Borowska Z, Szer W (1972) Inhibition of bacterial DNA synthesis by edeine. Effect on Escherichia coli mutants lacking DNA polymerase I. Biochim Biophys Acta 287:236-245
    • (1972) Biochim Biophys Acta , vol.287 , pp. 236-245
    • Kuryło-Borowska, Z.1    Szer, W.2
  • 125
    • 0013889674 scopus 로고
    • Inoculum-dependent division lag of Bacillus cultures and its relation to an endogenous factor(s) (Schizokinen)
    • Lankford CE, Walker JR, Reeves JB, Nabbut NH, Byers BR, Jones RJ (1966) Inoculum-dependent division lag of Bacillus cultures and its relation to an endogenous factor(s) (Schizokinen). J Bacteriol 91(3):1070-1079
    • (1966) J Bacteriol , vol.91 , Issue.3 , pp. 1070-1079
    • Lankford, C.E.1    Walker, J.R.2    Reeves, J.B.3    Nabbut, N.H.4    Byers, B.R.5    Jones, R.J.6
  • 128
    • 0020618817 scopus 로고
    • Natural ferric ionophores: Total synthesis of schizokinen, schizokinen A, and arthrobactin
    • Lee BH, Miller MJ (1983) Natural ferric ionophores: total synthesis of schizokinen, schizokinen A, and arthrobactin. J Org Chem 48:24-31
    • (1983) J Org Chem , vol.48 , pp. 24-31
    • Lee, B.H.1    Miller, M.J.2
  • 129
    • 34548667965 scopus 로고    scopus 로고
    • Isolation and structural analysis of bamylocin A, novel lipopeptide from Bacillus amyloliquefaciens LP03 having antagonistic and crude oil-emulsifying activity
    • DOI 10.1007/s00203-007-0250-9
    • Lee S-Ch, Kim S-H, Park I-H, Chung S-Y, Choi Y-L (2007) Isolation and structural analysis of bamylocin A, novel lipopeptide from Bacillusamyloliquefaciens LP03 having antagonistic and crude oil-emulsifying activity. Arch Microbiol 188(4):307-312 (Pubitemid 47415686)
    • (2007) Archives of Microbiology , vol.188 , Issue.4 , pp. 307-312
    • Lee, S.-C.1    Kim, S.-H.2    Park, I.-H.3    Chung, S.-Y.4    Choi, Y.-L.5
  • 130
    • 84954358295 scopus 로고    scopus 로고
    • Variants of lipopeptides produced by Bacillus licheniformis HSN221 in different medium components evaluated by a rapid method ESI-MS
    • Li Y-M, Haddad NIA, Yang S-Z, Mu B-Z (2008) Variants of lipopeptides produced by Bacillus licheniformis HSN221 in different medium components evaluated by a rapid method ESI-MS. Int J Pept Res Ther 14:229-235
    • (2008) Int J Pept Res Ther , vol.14 , pp. 229-235
    • Li, Y.-M.1    Haddad, N.I.A.2    Yang, S.-Z.3    Mu, B.-Z.4
  • 131
    • 0002854086 scopus 로고
    • Antifungal effects of bacilysin and fengymycin from Bacillus subtilis F-29-3 A comparison with activities of other Bacillus antibiotics
    • Loeffler W, Tschen JSM, Vanittanakom N, Kugler M, Knorpp E, Hsien T-F, Wu MS (1986) Antifungal effects of bacilysin and fengymycin from Bacillus subtilis F-29-3 A comparison with activities of other Bacillus antibiotics. J Phytopathol 115(3):204-213
    • (1986) J Phytopathol , vol.115 , Issue.3 , pp. 204-213
    • Loeffler, W.1    Tschen, J.S.M.2    Vanittanakom, N.3    Kugler, M.4    Knorpp, E.5    Hsien, T.-F.6    Wu, M.S.7
  • 132
    • 57349138602 scopus 로고    scopus 로고
    • Bacillus and other aerobic endospore-forming bacteria
    • Murray PR (ed) ASM Press, Washington, DC
    • Logan NA, Popovic T, Hoffmaster A (2007) Bacillus and other aerobic endospore-forming bacteria. In: Murray PR (ed) Manual of clinical microbiology, 9th edn. ASM Press, Washington, DC, pp 455-473
    • (2007) Manual of Clinical Microbiology, 9th Edn. , pp. 455-473
    • Logan, N.A.1    Popovic, T.2    Hoffmaster, A.3
  • 134
    • 0028258799 scopus 로고
    • Iturins, a special class of lipopeptides: Biological and properties pore-forming physicochemical
    • Maget-Dana R, Peypoux F (1994) Iturins, a special class of lipopeptides: biological and properties pore-forming physicochemical. Toxicology 87:151-174
    • (1994) Toxicology , vol.87 , pp. 151-174
    • Maget-Dana, R.1    Peypoux, F.2
  • 135
    • 0027104669 scopus 로고
    • Surfactin/iturin A interactions may explain the synergistic effect of surfactin on the biological properties of iturin A
    • Maget-Dana R, Thimon L, Peypoux F, Ptak M (1992) Surfactin/iturin A interactions may explain the synergistic effect of surfactin on the biological properties of iturin A. Biochimie 74:1047-1051
    • (1992) Biochimie , vol.74 , pp. 1047-1051
    • Maget-Dana, R.1    Thimon, L.2    Peypoux, F.3    Ptak, M.4
  • 136
    • 23744473698 scopus 로고
    • Amino acid sequence in mycobacillin
    • Majumdar SK, Bose SK (1960) Amino acid sequence in mycobacillin. Biochem J 74:596-599
    • (1960) Biochem J , vol.74 , pp. 596-599
    • Majumdar, S.K.1    Bose, S.K.2
  • 137
    • 67649112116 scopus 로고    scopus 로고
    • Higher structure of cereulide, an emetic toxin from Bacillus cereus, special comparison with valinomycin, an antibiotic from Streptomyces fulvissimus
    • Makarasen A, Yoza K, Isobe M (2009) Higher structure of cereulide, an emetic toxin from Bacillus cereus, special comparison with valinomycin, an antibiotic from Streptomyces fulvissimus. Chem Asian J 4:688-698
    • (2009) Chem Asian J , vol.4 , pp. 688-698
    • Makarasen, A.1    Yoza, K.2    Isobe, M.3
  • 138
    • 0035731314 scopus 로고    scopus 로고
    • Antibiotics produced by Bacillus bacteria
    • Mannanov RN, Sattarova RK (2001) Antibiotics produced by Bacillus bacteria. Chem Nat Compd 37(2):117-123
    • (2001) Chem Nat Compd , vol.37 , Issue.2 , pp. 117-123
    • Mannanov, R.N.1    Sattarova, R.K.2
  • 139
    • 0026696975 scopus 로고
    • Multidomain enzymes involved in peptide synthesis
    • Marahiel MA (1992) Multidomain enzymes involved in peptide synthesis. FEBS Lett 307:40-43
    • (1992) FEBS Lett , vol.307 , pp. 40-43
    • Marahiel, M.A.1
  • 140
    • 0027481468 scopus 로고
    • Regulation of peptide antibiotic production in Bacillus
    • Marahiel MA, Nakano MM, Zuber P (1993) Regulation of peptide antibiotic production in Bacillus. Mol Microbiol 7(5):631-636 (Pubitemid 23090345)
    • (1993) Molecular Microbiology , vol.7 , Issue.5 , pp. 631-636
    • Marahiel, M.A.1    Nakano, M.M.2    Zuber, P.3
  • 141
    • 9444278428 scopus 로고    scopus 로고
    • Modular peptide synthetases involved in nonribosomal peptide synthesis
    • Marahiel MA, Stachelhaus T, Mootz HD (1997) Modular peptide synthetases involved in nonribosomal peptide synthesis. Chem Rev 97:2651-2673 (Pubitemid 127667399)
    • (1997) Chemical Reviews , vol.97 , Issue.7 , pp. 2651-2673
    • Marahiel, M.A.1    Stachelhaus, T.2    Mootz, H.D.3
  • 142
    • 0037630382 scopus 로고    scopus 로고
    • Isolation, structural characterization, and properties of mattacin (polymyxin M), a cyclic peptide antibiotic produced by Paenibacillus kobensis M
    • DOI 10.1074/jbc.M212364200
    • Martin NI, Hu H, Moake MM, Churey JJ, Whittal R, Worobo RW, Vederas JC (2003) Isolation, structural characterization, and properties of mattacin (polymyxin M), a cyclic peptide antibiotic produced by Paenibacillus kobensis M. J Biol Chem 278(15):13124-13132 (Pubitemid 36800081)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.15 , pp. 13124-13132
    • Martin, N.I.1    Hu, H.2    Moake, M.M.3    Churey, J.J.4    Whittal, R.5    Worobo, R.W.6    Vederas, J.C.7
  • 143
    • 17844407663 scopus 로고    scopus 로고
    • Microbial genomics as a guide to drug discovery and structural elucidation: ECO-02301, a novel antifungal agent, as an example
    • DOI 10.1021/np0401664
    • McAlpine JB, Bachmann BO, Piraee M, Tremblay S, Alarco A-M, Zazopoulos E, Farnet CM (2005) Microbial genomics as a guide to drug discovery and structural elucidation: ECO-02301, a novel antifungal agent, as an example. J Nat Prod 68:493-496 (Pubitemid 40586306)
    • (2005) Journal of Natural Products , vol.68 , Issue.4 , pp. 493-496
    • McAlpine, J.B.1    Bachmann, B.O.2    Piraee, M.3    Tremblay, S.4    Alarco, A.-M.5    Zazopoulos, E.6    Farnet, C.M.7
  • 144
    • 67649604461 scopus 로고    scopus 로고
    • Ribosomal peptide natural products: Bridging the ribosomal and nonribosomal worlds
    • McIntosh JA, Donia MS, Schmidt EW (2009) Ribosomal peptide natural products: bridging the ribosomal and nonribosomal worlds. Nat Prod Rep 26:537-559
    • (2009) Nat Prod Rep , vol.26 , pp. 537-559
    • McIntosh, J.A.1    Donia, M.S.2    Schmidt, E.W.3
  • 145
    • 0017034072 scopus 로고
    • A nomenclature proposal for the octapeptin antibiotics
    • Meyers E, Parker WL, Brown WE, Shoji J, Wakisaka Y (1976) A nomenclature proposal for the octapeptin antibiotics. J Antibiot 29(11):1241-1242 (Pubitemid 8008513)
    • (1976) Journal of Antibiotics , vol.29 , Issue.11 , pp. 1241-1242
    • Meyers, E.1    Parker, W.L.2    Brown, W.E.3
  • 146
    • 0020326776 scopus 로고
    • Bacillomycin F, a new antibiotic of iturin group: Isolation and characterization
    • Mhammedi A, Peypoux F, Besson F, Michel G (1982) Bacillomycin F, a new antibiotic of iturin group: isolation and characterization. J Antibiot 35(3):306-311 (Pubitemid 12076469)
    • (1982) Journal of Antibiotics , vol.35 , Issue.3 , pp. 306-311
    • Mhammedi, A.1    Peypoux, F.2    Besson, F.3    Michel, G.4
  • 147
    • 15644375069 scopus 로고
    • Two antifungal substances from Bacillus subtilis cultures
    • Michener HD, Snell N (1949) Two antifungal substances from Bacillus subtilis cultures. Arch Biochem 22:208-214
    • (1949) Arch Biochem , vol.22 , pp. 208-214
    • Michener, H.D.1    Snell, N.2
  • 149
    • 0037173583 scopus 로고    scopus 로고
    • Metal binding and structure-activity relationship of the metalloantibiotic peptide bacitracin
    • DOI 10.1016/S0162-0134(02)00464-6, PII S0162013402004646
    • Ming L-J, Epperson JD (2002) Metal binding and structure-activity relationship of the metalloantibiotic peptide bacitracin. J Inorg Biochem 91:46-58 (Pubitemid 34727759)
    • (2002) Journal of Inorganic Biochemistry , vol.91 , Issue.1 , pp. 46-58
    • Ming, L.-J.1    Epperson, J.D.2
  • 150
    • 70849102756 scopus 로고    scopus 로고
    • Gramicidin S and polymyxins: The revival of cationic cyclic peptide antibiotics
    • Mogi T, Kita K (2009) Gramicidin S and polymyxins: the revival of cationic cyclic peptide antibiotics. Cell Mol Life Sci 66(23):3821-3826
    • (2009) Cell Mol Life Sci , vol.66 , Issue.23 , pp. 3821-3826
    • Mogi, T.1    Kita, K.2
  • 151
    • 0032560491 scopus 로고    scopus 로고
    • The complete genome of Bacillus subtilis: From sequence annotation to data management and analysis
    • Moszer I (1998) The complete genome of Bacillus subtilis: from sequence annotation to data management and analysis. FEBS Lett 430:28-36
    • (1998) FEBS Lett , vol.430 , pp. 28-36
    • Moszer, I.1
  • 152
    • 1942438128 scopus 로고    scopus 로고
    • Molecular characterization and analysis of the operon encoding the antifungal lipopeptide bacillomycin D
    • DOI 10.1016/j.femsle.2004.03.011, PII S0378109704001958
    • Moyne A-L, Cleveland TE, Tuzun S (2004) Molecular caracterization and analysis of the operon encoding the antifungal lipopeptide bacillomycin D. FEMS Microbiol Lett 234:43-49 (Pubitemid 38515749)
    • (2004) FEMS Microbiology Letters , vol.234 , Issue.1 , pp. 43-49
    • Moyne, A.-L.1    Cleveland, T.E.2    Tuzun, S.3
  • 153
    • 7044235235 scopus 로고    scopus 로고
    • Environmental applications for biosurfactants
    • Mulligan CN (2005) Environmental applications for biosurfactants. Environ Pollut 133:183-198
    • (2005) Environ Pollut , vol.133 , pp. 183-198
    • Mulligan, C.N.1
  • 154
    • 0015235664 scopus 로고
    • Structure of schizokinen, an iron-transport compound from Bacillus megaterium
    • Mullis KB, Pollack JR, Neilands JB (1971) Structure of schizokinen, an iron-transport compound from Bacillus megaterium. Biochemistry 10(26):4894-4898
    • (1971) Biochemistry , vol.10 , Issue.26 , pp. 4894-4898
    • Mullis, K.B.1    Pollack, J.R.2    Neilands, J.B.3
  • 155
    • 0022361622 scopus 로고
    • Absolute configuration of the beta-hydroxyl fatty acid constituent of permetin A
    • Murai A, Amino Y, Ando T (1985) Absolute configuration of the β-hydroxyl fatty acid constituent of permetin A. J Antibiot 38(11):1610-1613 (Pubitemid 16217852)
    • (1985) Journal of Antibiotics , vol.38 , Issue.11 , pp. 1610-1613
    • Murai, A.1    Amino, Y.2    Ando, T.3
  • 157
    • 0025264286 scopus 로고
    • Pumilacidin, a complex of new antiviral antibiotics. Production, isolation, chemical properties, structure and biological activity
    • Naruse N, Tenmyo O, Kobaru S, Kamei H, Miyaki T, Konishi M, Oki T (1990) Pumilacidin, a complex of new antiviral antibiotics: production, isolation, chemical properties, structure and biological activity. J Antibiot 43(3):267-280 (Pubitemid 20106390)
    • (1990) Journal of Antibiotics , vol.43 , Issue.3 , pp. 267-280
    • Naruse, N.1    Tenmyo, O.2    Kobaru, S.3    Kamei, H.4    Miyaki, T.5    Konishi, M.6    Oki, T.7
  • 158
    • 70350722394 scopus 로고    scopus 로고
    • Genomic basis for natural product biosynthetic diversity in the actinomycetes
    • Nett M, Ikeda H, Moore BS (2009) Genomic basis for natural product biosynthetic diversity in the actinomycetes. Nat Prod Rep 26:1362-1384
    • (2009) Nat Prod Rep , vol.26 , pp. 1362-1384
    • Nett, M.1    Ikeda, H.2    Moore, B.S.3
  • 159
    • 68949117184 scopus 로고
    • Antibiotics from a strain of Bacillus subtilis: Bacilipin A and B and bacilysin
    • Newton GGF (1949) Antibiotics from a strain of Bacillus subtilis: bacilipin A and B and bacilysin. J Exp Pathol 30:306-319
    • (1949) J Exp Pathol , vol.30 , pp. 306-319
    • Newton, G.G.F.1
  • 160
    • 0002088906 scopus 로고
    • The properties and mode of action of the polymyxins
    • Newton BA (1956) The properties and mode of action of the polymyxins. Bacteriol Rev 20:14-27
    • (1956) Bacteriol Rev , vol.20 , pp. 14-27
    • Newton, B.A.1
  • 161
    • 0021069749 scopus 로고
    • Toxicity of cyclic peptide antibiotics to larvae of Aedes aegypti
    • Nickerson KW, Schnell DJ (1983) Toxicity of cyclic peptide antibiotics to larvae of Aedes aegypti. J Invertebr Pathol 42:407-409 (Pubitemid 14221780)
    • (1983) Journal of Invertebrate Pathology , vol.42 , Issue.3 , pp. 407-409
    • Nickerson, K.W.1    Schnell, D.J.2
  • 162
    • 0042322530 scopus 로고    scopus 로고
    • Molecular dynamics simulation of surfactin molecules at the water hexane interface
    • Nicolas JP (2003) Molecular dynamics simulation of surfactin molecules at the water hexane interface. Biophys J 85:1377-1391
    • (2003) Biophys J , vol.85 , pp. 1377-1391
    • Nicolas, J.P.1
  • 163
    • 0022447641 scopus 로고
    • 2, produced by Bacillus cereus BMG302-fF67 III. Structural elucidation of plipastatins
    • Nishikiori T, Naganawa H, Muraoka Y, Aoyagi T, Umezawa H (1986a) Plipastatins: new inhibitors of phospholipase A2, produced by Bacillus cereus BMG302-fF67. III. Structural elucidation of plipastatins. J Antibiot 39:755-761 (Pubitemid 16063646)
    • (1986) Journal of Antibiotics , vol.39 , Issue.6 , pp. 755-761
    • Nishikiori, T.1    Naganawa, H.2    Muraoka, Y.3
  • 164
  • 165
    • 0015226397 scopus 로고
    • Inhibition of peptide initiation on reticulocyte ribosomes by edeine
    • Obrig T, Irvin J, Culp W, Hardesty B (1971) Inhibition of peptide initiation on reticulocyte ribosomes by edeine. Eur J Biochem 21:31-41
    • (1971) Eur J Biochem , vol.21 , pp. 31-41
    • Obrig, T.1    Irvin, J.2    Culp, W.3    Hardesty, B.4
  • 166
    • 84902546010 scopus 로고
    • Esperin, a new antibiotic. I. Properties and constitution of esperin
    • Ogawa H, Ito T (1951) Esperin, a new antibiotic. I. Properties and constitution of esperin. Nippon Nogei Kagaku Kaishi 24:191-196
    • (1951) Nippon Nogei Kagaku Kaishi , vol.24 , pp. 191-196
    • Ogawa, H.1    Ito, T.2
  • 167
    • 33646592214 scopus 로고    scopus 로고
    • Role of the Fur regulon in iron transport in Bacillus subtilis
    • DOI 10.1128/JB.188.10.3664-3673.2006
    • Ollinger J, Song K-B, Antelmann H, Hecker M, Helmann JD (2006) Role of the fur regulon in iron transport in Bacillus subtilis. J Bacteriol 88(10):3664-3673 (Pubitemid 43726229)
    • (2006) Journal of Bacteriology , vol.188 , Issue.10 , pp. 3664-3673
    • Ollinger, J.1    Song, K.-B.2    Antelmann, H.3    Hecker, M.4    Helmann, J.D.5
  • 168
    • 74049115080 scopus 로고    scopus 로고
    • Follow the leader: The use of leader peptides to guide natural product biosynthesis
    • Oman TJ, van der Donk WA (2010) Follow the leader: the use of leader peptides to guide natural product biosynthesis. Nat Chem Biol 6:9-18
    • (2010) Nat Chem Biol , vol.6 , pp. 9-18
    • Oman, T.J.1    Van Der Donk, W.A.2
  • 169
    • 40049086245 scopus 로고    scopus 로고
    • Bacillus lipopeptides: Versatile weapons for plant disease biocontrol
    • Ongena M, Jacques P (2008) Bacillus lipopeptides: versatile weapons for plant disease biocontrol. Trends Microbiol 16:115-125
    • (2008) Trends Microbiol , vol.16 , pp. 115-125
    • Ongena, M.1    Jacques, P.2
  • 170
    • 0023902558 scopus 로고
    • Screening for new nematocidal substances of microbial origin by a new method using the pine wood nematode
    • Otoguro K, Liu ZX, Fukuda K, Li Y, Iwai Y, Tanaka H, Omura S (1988) Screening for new nematocidal substances of microbial origin by a new method using the pine wood nematode. J Antibiot 41:573-575
    • (1988) J Antibiot , vol.41 , pp. 573-575
    • Otoguro, K.1    Liu, Z.X.2    Fukuda, K.3    Li, Y.4    Iwai, Y.5    Tanaka, H.6    Omura, S.7
  • 171
    • 0028939988 scopus 로고
    • Inhibition of the binding of oxidized low density lipoprotein to the macrophages by iturin C-related compounds
    • Park JK, Hasumi K, Endo A (1995) Inhibition of the binding of oxidized low density lipoprotein to the macrophages by iturin C-related compounds. J Antibiot 48(3):226-232
    • (1995) J Antibiot , vol.48 , Issue.3 , pp. 226-232
    • Park, J.K.1    Hasumi, K.2    Endo, A.3
  • 172
    • 0016750865 scopus 로고
    • EM49, a new peptide antibiotic. IV. Structure of EM49
    • Parker WL, Rathnum ML (1975) EM49, a new peptide antibiotic. IV. Structure of EM49. J Antibiot 28(5):379-389
    • (1975) J Antibiot , vol.28 , Issue.5 , pp. 379-389
    • Parker, W.L.1    Rathnum, M.L.2
  • 173
    • 0017624701 scopus 로고
    • Polymyxin F, a new peptide antibiotic
    • Parker WL, Rathnum ML, Dean LD, Nimeck MW, Brown WE, Meyers E (1977) Polymyxin F, a new peptide antibiotic. J Antibiot 30:767-769 (Pubitemid 8199661)
    • (1977) Journal of Antibiotics , vol.30 , Issue.9 , pp. 767-769
    • Parker, W.L.1    Rathnum, M.L.2    Dean, L.D.3
  • 174
    • 33750612344 scopus 로고    scopus 로고
    • Pathways of chemical degradation of polypeptide antibiotic bacitracin
    • DOI 10.1248/bpb.29.2160
    • Pavli V, Kmetec V (2006) Pathways of chemical degradation of polypeptide antibiotic bacitracin. Biol Pharm Bull 29(11):2160-2167 (Pubitemid 44690936)
    • (2006) Biological and Pharmaceutical Bulletin , vol.29 , Issue.11 , pp. 2160-2167
    • Pavli, V.1    Kmetec, V.2
  • 176
    • 0018092840 scopus 로고
    • Structure of iturine A, a peptidolipid antibiotic from Bacillus subtilis
    • Peypoux F, Guinand M, Michel G, Delcambe L, Das BC, Lederer E (1978a) Structure of iturin A, a peptidolipid antibiotic from Bacillus subtilis. Biochemistry 17:3992-3996 (Pubitemid 9036514)
    • (1978) Biochemistry , vol.17 , Issue.19 , pp. 3992-3996
    • Peypoux, F.1    Guinand, M.2    Michel, G.3
  • 179
    • 0022373070 scopus 로고
    • Structure of bacillomycin F, a new peptidolipid antibiotic of the iturin group
    • DOI 10.1111/j.1432-1033.1985.tb09307.x
    • Peypoux F, Marion D, Maget-Dana R, Ptak M, Das BC, Michel G (1985) Structure of bacillomycin F, a new peptidolipid antibiotic of the iturin group. Eur J Biochem 153:335-340 (Pubitemid 16209834)
    • (1985) European Journal of Biochemistry , vol.153 , Issue.2 , pp. 335-340
    • Peypoux, F.1    Marion, D.2    Maget-Dana, R.3
  • 180
    • 0022644643 scopus 로고
    • Revised structure of mycosubtilin, a peptidolipid antibiotic from Bacillus subtilis
    • Peypoux F, Pommier MT, Marion D, Ptak M, Das BC, Michel G (1986) Revised structure of mycosubtilin, a peptidolipid antibiotic from Bacillus subtilis. J Antibiot 39(5):636-641 (Pubitemid 16118063)
    • (1986) Journal of Antibiotics , vol.39 , Issue.5 , pp. 636-641
    • Peypoux, F.1    Pommier, M.T.2    Marion, D.3
  • 183
    • 0028819970 scopus 로고
    • Gavaserin and saltavalin, new peptide antibiotics produced by Bacillus polymyxa
    • Pichard B, Larue J-P, Thouvenot D (1995) Gavaserin and saltavalin, new peptide antibiotics produced by Bacillus polymyxa. FEMS Microbiol Lett 133(3):215-218
    • (1995) FEMS Microbiol Lett , vol.133 , Issue.3 , pp. 215-218
    • Pichard, B.1    Larue, J.-P.2    Thouvenot, D.3
  • 186
    • 0001768844 scopus 로고
    • Systematics and ecology of Bacillus
    • Sonenshein AL, Hoch JA, Losick R (eds) ASM Press, Washington, DC
    • Priest F (1993) Systematics and ecology of Bacillus. In: Sonenshein AL, Hoch JA, Losick R (eds) Bacillus subtilis and other Gram-positive bacteria. ASM Press, Washington, DC, pp 3-16
    • (1993) Bacillus Subtilis and Other Gram-positive Bacteria , pp. 3-16
    • Priest, F.1
  • 188
    • 78649388416 scopus 로고    scopus 로고
    • Natural functions of lipopeptides from Bacillus and Pseudomonas: More than surfactants and antibiotics
    • Raaijmakers JM, De Bruijn I, Nybroe O, Ongena M (2010) Natural functions of lipopeptides from Bacillus and Pseudomonas: more than surfactants and antibiotics. FEMS Microbiol Rev 34:1037-1062
    • (2010) FEMS Microbiol Rev , vol.34 , pp. 1037-1062
    • Raaijmakers, J.M.1    De Bruijn, I.2    Nybroe, O.3    Ongena, M.4
  • 190
    • 84902537560 scopus 로고
    • Amino acid composition and physical-chemical properties of esein and bresein, new antibiotics from Bacillus brevis
    • Radzhapov RA, Zharikova GG, Silaev AB, Katrukha GS (1968) Amino acid composition and physical-chemical properties of esein and bresein, new antibiotics from Bacillus brevis. Nauchnye Doki Vyss Shkoly Biol Nauki 3:99-102
    • (1968) Nauchnye Doki Vyss Shkoly Biol Nauki , vol.3 , pp. 99-102
    • Radzhapov, R.A.1    Zharikova, G.G.2    Silaev, A.B.3    Katrukha, G.S.4
  • 191
    • 33748324608 scopus 로고    scopus 로고
    • Second stage production of iturin A by induced germination of Bacillus subtilis RB14
    • DOI 10.1016/j.jbiotec.2006.03.016, PII S016816560600215X
    • Rahman MS, Ano T, Shoda M (2006) Second stage production of iturin A by induced germination of Bacillus subtilis RB14. J Biotechnol 125:513-515 (Pubitemid 44333119)
    • (2006) Journal of Biotechnology , vol.125 , Issue.4 , pp. 513-515
    • Rahman, M.S.1    Ano, T.2    Shoda, M.3
  • 192
    • 0009496155 scopus 로고
    • Chlorotetaine from Bacillus subtilis, an antifungal dipeptide with an unusual chloro containing amino acid
    • Rapp C, Jung G, Katzer W, Loeffler W (1988a) Chlorotetaine from Bacillus subtilis, an antifungal dipeptide with an unusual chloro containing amino acid. Angew Chem 100(12):1801-1802
    • (1988) Angew Chem , vol.100 , Issue.12 , pp. 1801-1802
    • Rapp, C.1    Jung, G.2    Katzer, W.3    Loeffler, W.4
  • 193
    • 84985200090 scopus 로고
    • Rhizocticins-new phosphono-oligopeptides with antifungal activity
    • Rapp C, Jung G, Kugler M, Loeffler W (1988b) Rhizocticins-new phosphono-oligopeptides with antifungal activity. Liebigs Ann Chem 7:655-661
    • (1988) Liebigs Ann Chem , vol.7 , pp. 655-661
    • Rapp, C.1    Jung, G.2    Kugler, M.3    Loeffler, W.4
  • 194
    • 15944417910 scopus 로고    scopus 로고
    • Genomics of the Bacillus cereus group of organisms
    • DOI 10.1016/j.femsre.2004.12.005, Bacterial Genomics
    • Rasko DA, Altherr MR, Han CS, Ravel J (2005) Genomics of the Bacillus cereus group of organisms. FEMS Microbiol Rev 29:303-329 (Pubitemid 40432471)
    • (2005) FEMS Microbiology Reviews , vol.29 , Issue.2 , pp. 303-329
    • Rasko, D.A.1    Altherr, M.R.2    Han, C.S.3    Ravel, J.4
  • 195
    • 84866627583 scopus 로고
    • An antibiotic active against dermatophytes, derived from Bacillus subtilis
    • Raubitschek F, Dostrovsky A (1950) An antibiotic active against dermatophytes, derived from Bacillus subtilis. Dermatologica 100:45-49
    • (1950) Dermatologica , vol.100 , pp. 45-49
    • Raubitschek, F.1    Dostrovsky, A.2
  • 196
    • 14644427801 scopus 로고    scopus 로고
    • Genomics at the genus scale
    • DOI 10.1016/j.tim.2005.01.004
    • Ravel J, Fraser CM (2005) Genomics at the genus scale. Trends Microbiol 13:95-97 (Pubitemid 40311890)
    • (2005) Trends in Microbiology , vol.13 , Issue.3 , pp. 95-97
    • Ravel, J.1    Fraser, C.M.2
  • 197
    • 84902537103 scopus 로고    scopus 로고
    • A catechol type siderophore, bacillibactin: Biosynthesis, regulation and transport in Bacillus subtilis
    • Raza W, Wu H, Shah MAA, Shen Q (2008) A catechol type siderophore, bacillibactin: biosynthesis, regulation and transport in Bacillus subtilis. J Basic Microbiol 48:1-12
    • (2008) J Basic Microbiol , vol.48 , pp. 1-12
    • Raza, W.1    Wu, H.2    Shah, M.A.A.3    Shen, Q.4
  • 203
    • 79952299225 scopus 로고    scopus 로고
    • Antifungal lipopeptides from Bacillus amyloliquefaciens strain BO7
    • Romano A, Vitullo D, Di Pietro A, Lima G, Lanzotti V (2011) Antifungal lipopeptides from Bacillus amyloliquefaciens strain BO7. J Nat Prod 74:145-151
    • (2011) J Nat Prod , vol.74 , pp. 145-151
    • Romano, A.1    Vitullo, D.2    Di Pietro, A.3    Lima, G.4    Lanzotti, V.5
  • 204
    • 0032831422 scopus 로고    scopus 로고
    • High- and low-molecular-mass microbial surfactants
    • DOI 10.1007/s002530051502
    • Rosenberg E, Ron EZ (1999) High- and low-molecular-mass microbial surfactants. Appl Microbiol Biotechnol 52:154-162 (Pubitemid 29424508)
    • (1999) Applied Microbiology and Biotechnology , vol.52 , Issue.2 , pp. 154-162
    • Rosenberg, E.1    Ron, E.Z.2
  • 205
    • 34447280364 scopus 로고    scopus 로고
    • Detergent alkaline proteases: enzymatic properties, genes, and crystal structures
    • DOI 10.1263/jbb.103.501, PII S1389172307700968
    • Saeki K, Ozaki K, Kobayashi T, Ito S (2007) Detergent alkaline proteases: enzymatic properties, genes, and crystal structures. J Biosci Bioeng 103:501-508 (Pubitemid 47043544)
    • (2007) Journal of Bioscience and Bioengineering , vol.103 , Issue.6 , pp. 501-508
    • Saeki, K.1    Ozaki, K.2    Kobayashi, T.3    Ito, S.4
  • 206
    • 0027468111 scopus 로고
    • Iron-hydroxamate uptake systems in Bacillus subtilis: Identification of a lipoprotein as part of a binding protein-dependent transport system
    • Schneider R, Hantke K (1993) Iron-hydroxamate uptake systems in Bacillus subtilis: identification of a lipoprotein as part of a binding protein-dependent transport system. Mol Microbiol 8(1):111-121 (Pubitemid 23114827)
    • (1993) Molecular Microbiology , vol.8 , Issue.1 , pp. 111-121
    • Schneider, R.1    Hantke, K.2
  • 209
    • 84975496934 scopus 로고    scopus 로고
    • A mutant of Bacillus subtilis strain LB5 with enhanced antifungal activities against Colletotrichum gloeosporioides
    • Senghor A, Liang WL, Ho W (2007) A mutant of Bacillus subtilis strain LB5 with enhanced antifungal activities against Colletotrichum gloeosporioides. Biocontrol Sci Technol 9:575-580
    • (2007) Biocontrol Sci Technol , vol.9 , pp. 575-580
    • Senghor, A.1    Liang, W.L.2    Ho, W.3
  • 210
    • 41949088228 scopus 로고    scopus 로고
    • Review of surfactin chemical properties and the potential biomedical applications
    • Seydlova G, Svobodova J (2008) Review of surfactin chemical properties and the potential biomedical applications. Cent Eur J Med 3:123-133
    • (2008) Cent Eur J Med , vol.3 , pp. 123-133
    • Seydlova, G.1    Svobodova, J.2
  • 211
    • 0008826581 scopus 로고
    • Homocereulide, an extremely potent cytotoxic depsipeptide from the marine bacterium Bacillus cereus
    • Sheng G-Y-W, Makoto K, Kaoru Y, Kazunaga Y, Daisuke U (1995) Homocereulide, an extremely potent cytotoxic depsipeptide from the marine bacterium Bacillus cereus. Chem Lett 9:791-792
    • (1995) Chem Lett , vol.9 , pp. 791-792
    • Sheng, G.-Y.-W.1    Makoto, K.2    Kaoru, Y.3    Kazunaga, Y.4    Daisuke, U.5
  • 212
    • 0034210205 scopus 로고    scopus 로고
    • Bacterial control of plant diseases
    • Shoda M (2000) Bacterial control of plant diseases. J Biosci Bioeng 89(6):515-521
    • (2000) J Biosci Bioeng , vol.89 , Issue.6 , pp. 515-521
    • Shoda, M.1
  • 213
    • 0018067460 scopus 로고
    • Recent chemical studies on peptide antibiotics from the genus Bacillus
    • Shoji J (1978) Recent chemical studies on peptide antibiotics from the genus Bacillus. Adv Appl Microbiol 18:187-214
    • (1978) Adv Appl Microbiol , vol.18 , pp. 187-214
    • Shoji, J.1
  • 214
    • 0016663722 scopus 로고
    • Antibiotics from the genus Bacillus. II. Chemical characterization of new antibiotics, cerexins A and B
    • Shoji J, Hinoo H (1975) Antibiotics from the genus Bacillus. II. Chemical characterization of new antibiotics, cerexins A and B. J Antibiot 28:60-63
    • (1975) J Antibiot , vol.28 , pp. 60-63
    • Shoji, J.1    Hinoo, H.2
  • 215
    • 0017077736 scopus 로고
    • Studies on antibiotics from the genus Bacillus. X. The structure of brevistin
    • Shoji J, Kato T (1976a) Studies on antibiotics from the genus Bacillus. X. The structure of brevistin. J Antibiot 29(4):380-389
    • (1976) J Antibiot , vol.29 , Issue.4 , pp. 380-389
    • Shoji, J.1    Kato, T.2
  • 216
    • 0017049387 scopus 로고
    • The structure of cerexin B (studies on antibiotics from the genus Bacillus. XVII)
    • Shoji J, Kato T (1976b) Studies on antibiotics from the genus Bacillus. XVII. The structure of cerexin B. J Antibiot 29:1275-1280 (Pubitemid 8018010)
    • (1976) Journal of Antibiotics , vol.29 , Issue.12 , pp. 1275-1280
    • Shoji, J.1    Kato, T.2
  • 217
    • 0017118655 scopus 로고
    • Studies on antibiotics from the genus Bacillus. IX. Isolation of brevistin, a new peptide antibiotic
    • Shoji J, Sakazaki R, Wakisaka Y, Koizumi K, Mayama M, Matsuura S, Matsumoto K (1976a) Studies on antibiotics from the genus Bacillus. IX. Isolation of brevistin, a new peptide antibiotic. J Antibiot 29:375-379
    • (1976) J Antibiot , vol.29 , pp. 375-379
    • Shoji, J.1    Sakazaki, R.2    Wakisaka, Y.3    Koizumi, K.4    Mayama, M.5    Matsuura, S.6    Matsumoto, K.7
  • 218
    • 0017136162 scopus 로고
    • Isolation of a new antibiotic 333-25, related to antibiotic EM49 (Studies on antibiotics from the genus Bacillus. XI)
    • Shoji J, Hwoo H, Wakisaka Y, Koizumi K, Mayama M, Matsuura S, Matsumoto K (1976b) Isolation of a new antibiotic 333-25, related to antibiotic EM49 (Studies on antibiotics from the genus Bacillus. XI). J Antibiot 29:516-520
    • (1976) J Antibiot , vol.29 , pp. 516-520
    • Shoji, J.1    Hwoo, H.2    Wakisaka, Y.3    Koizumi, K.4    Mayama, M.5    Matsuura, S.6    Matsumoto, K.7
  • 219
    • 0017078825 scopus 로고
    • Studies on antibiotics from the genus Bacillus. VIII. Isolation of three new antibiotics, thiocillins I, II and III, related to micrococcin P
    • Shoji J, Hinoo H, Wakisaka Y, Koizumi K, Mayama M, Matsuura S, Matsumoto K (1976c) Studies on antibiotics from the genus Bacillus. VIII. Isolation of three new antibiotics, thiocillins I, II and III, related to micrococcin P. J Antibiot 29(4):366-374
    • (1976) J Antibiot , vol.29 , Issue.4 , pp. 366-374
    • Shoji, J.1    Hinoo, H.2    Wakisaka, Y.3    Koizumi, K.4    Mayama, M.5    Matsuura, S.6    Matsumoto, K.7
  • 220
    • 0017042752 scopus 로고
    • The total structure of cerexin A (studies on antibiotics from the genus bacillus. XVI)
    • Shoji J, Kato T, Sakazaki R (1976d) Studies on antibiotics from the genus Bacillus. XVI. The total structure of cerexin A. J Antibiot 29(12):1268-1274 (Pubitemid 8018009)
    • (1976) Journal of Antibiotics , vol.29 , Issue.12 , pp. 1268-1274
    • Shoji, J.1    Kato, T.2    Sakazaki, R.3
  • 221
    • 0017046298 scopus 로고
    • Production and isolation of cerexins C and D: studies on antibiotics from the genus Bacillus. XVIII
    • Shoji J, Kato T, Matsumoto K, Takahashi Y, Mayama M (1976e) Studies on antibiotics from the genus Bacillus. XVIII. Production and isolation of cerexins C and D. J Antibiot 29(12):1281-1285 (Pubitemid 8018011)
    • (1976) Journal of Antibiotics , vol.29 , Issue.12 , pp. 1281-1285
    • Shoji, J.1    Kato, T.2    Matsumoto, K.3
  • 222
    • 0017397986 scopus 로고
    • The structures of two new polymyxin group antibiotics
    • Shoji J, Kato T, Hinoo H (1977a) The structures of two new polymyxin group antibiotics. J Antibiot 30(5):427-429 (Pubitemid 8113118)
    • (1977) Journal of Antibiotics , vol.30 , Issue.5 , pp. 427-429
    • Shoji, J.1    Kato, T.2    Hinoo, H.3
  • 223
    • 0017571786 scopus 로고
    • 1. (Studies on antibiotics from the genus Bacillus. XXI)
    • Shoji J, Kato T, Hinoo H (1977b) The structure of polymyxin S. (Studies on antibiotics from the genus Bacillus. XXI). J Antibiot 30(12):1035-1041 (Pubitemid 8268351)
    • (1977) Journal of Antibiotics , vol.30 , Issue.12 , pp. 1035-1041
    • Shoji, J.1    Kato, T.2    Hinoo, H.3
  • 224
    • 0018362575 scopus 로고
    • Resolution of peptide antibiotics, cerexins and tridecaptins, by high performance liquid chromatography. (Studies on antibiotics from the genus Bacillus. XXVI)
    • Shoji J, Kato T, Terabe S, Konaka R (1979) Studies on antibiotics from the genus Bacillus. XXVI. Resolution of peptide antibiotics, cerexins and tridecaptins, by high performance liquid chromatography. J Antibiot 32(4):313-319 (Pubitemid 9189892)
    • (1979) Journal of Antibiotics , vol.32 , Issue.4 , pp. 313-319
    • Shoji, J.1    Kato, T.2    Terabe, S.3    Konaka, R.4
  • 225
    • 0019806682 scopus 로고
    • Structural studies on thiocillins I, II and III. (Studies on antibiotics from the Genus bacillus. XXIX)
    • Shoji J, Kato T, Yoshimura Y, Tori K (1981) Structural studies on thiocillins I, II and III (Studies on antibiotics from the genus Bacillus. XXIX). J Antibiot 34(9):1126-1136 (Pubitemid 12174608)
    • (1981) Journal of Antibiotics , vol.34 , Issue.9 , pp. 1126-1136
    • Shoji, J.1    Kato, T.2    Yoshimura, Y.3    Tori, K.4
  • 227
    • 70349704494 scopus 로고    scopus 로고
    • The genus Bacillus. Nonmedical
    • Dworkin M, Falkow S, Rosenberg E, Schleifer K-H, Stackebrandt E (eds) Springer, New York
    • Slepecky R, Hemphill E (2006) The genus Bacillus. Nonmedical. In: Dworkin M, Falkow S, Rosenberg E, Schleifer K-H, Stackebrandt E (eds) The prokaryotes, vol 4. Springer, New York, pp 530-562
    • (2006) The Prokaryotes , vol.4 , pp. 530-562
    • Slepecky, R.1    Hemphill, E.2
  • 228
    • 0017088449 scopus 로고
    • Structure of the peptide antibiotic polypeptin
    • Sogn JA (1976) Structure of the peptide antibiotic polypeptin. J Med Chem 19(10):1228-1231
    • (1976) J Med Chem , vol.19 , Issue.10 , pp. 1228-1231
    • Sogn, J.A.1
  • 229
    • 33749424162 scopus 로고    scopus 로고
    • Applications of microbial biosurfactants
    • Solaiman D (2005) Applications of microbial biosurfactants. Inform 16:408-410
    • (2005) Inform , vol.16 , pp. 408-410
    • Solaiman, D.1
  • 230
    • 9344239899 scopus 로고    scopus 로고
    • Rhizosphere bacterial signalling: A love parade beneath our feet
    • DOI 10.1080/10408410490468786
    • Somers E, Vanderleyden J, Srinivasan M (2004) Rhizosphere bacterial signalling: a love parade beneath our feet. Crit Rev Microbiol 30:205-240 (Pubitemid 39557581)
    • (2004) Critical Reviews in Microbiology , vol.30 , Issue.4 , pp. 205-240
    • Somers, E.1    Vanderleyden, J.2    Srinivasan, M.3
  • 231
    • 18444415756 scopus 로고    scopus 로고
    • Bacillus subtilis antibiotics: Structures, syntheses and specific functions
    • Stein T (2005) Bacillus subtilis antibiotics: structures, syntheses and specific functions. Mol Microbiol 56(4):845-857
    • (2005) Mol Microbiol , vol.56 , Issue.4 , pp. 845-857
    • Stein, T.1
  • 232
    • 13844252038 scopus 로고    scopus 로고
    • bac genes for recombinant bacilysin and anticapsin production in Bacillus host strains
    • DOI 10.1007/s00203-004-0743-8
    • Steinborn G, Hajirezaei M-R, Hofemeister J (2005) BAC genes for recombinant bacilysin and anticapsin production in Bacillus host strains. Arch Microbiol 183(2):71-79 (Pubitemid 40248271)
    • (2005) Archives of Microbiology , vol.183 , Issue.2 , pp. 71-79
    • Steinborn, G.1    Hajirezaei, M.-R.2    Hofemeister, J.3
  • 236
    • 33751514303 scopus 로고    scopus 로고
    • Isolation and characterization of a co-producer of fengycins and surfactins, endophytic Bacillus amyloliquefaciens ES-2, from Scutellaria baicalensis Georgi
    • DOI 10.1007/s11274-006-9170-0
    • Sun L, Lu Z, Bie X, Lu F, Yang S (2006) Isolation and characterization of a co-producer of fengycins and surfactins, endophytic Bacillus amyloliquefaciens ES-2, from Scutellaria baicalensis Georgi. World J Microbiol Biotechnol 22(12):1259-1266 (Pubitemid 44832659)
    • (2006) World Journal of Microbiology and Biotechnology , vol.22 , Issue.12 , pp. 1259-1266
    • Sun, L.1    Lu, Z.2    Bie, X.3    Lu, F.4    Yang, S.5
  • 239
    • 84902537561 scopus 로고    scopus 로고
    • Preparation of Bacillus alkali proteasa and use of the enzyme for production of ferrichrome
    • Takimura Y, Saeki K, Kobayashi T (2004) Preparation of Bacillus alkali proteasa and use of the enzyme for production of ferrichrome. Jpn. Kokai Tokkyo Koho JP 2004065171
    • (2004) Jpn. Kokai Tokkyo Koho JP 2004065171
    • Takimura, Y.1    Saeki, K.2    Kobayashi, T.3
  • 242
    • 36549061071 scopus 로고    scopus 로고
    • Isolation, purification and characterization of an antifungal molecule produced by Bacillus licheniformis BC98, and its effect on phytopathogen Magnaporthe grisea
    • DOI 10.1111/j.1365-2672.2007.03501.x
    • Tendulkar SR, Saikumari YK, Patel V, Raghotama S, Munshi TK, Balaram P, Chattoo BB (2007) Isolation, purification and characterization of an antifungal molecule produced by Bacillus licheniformis BC98, and its effect on phytopathogen Magnaporthe grisea. J Appl Microbiol 103(6):2331-2339 (Pubitemid 350191194)
    • (2007) Journal of Applied Microbiology , vol.103 , Issue.6 , pp. 2331-2339
    • Tendulkar, S.R.1    Saikumari, Y.K.2    Patel, V.3    Raghotama, S.4    Munshi, T.K.5    Balaram, P.6    Chattoo, B.B.7
  • 243
    • 0029023319 scopus 로고
    • Effect of the lipopeptide antibiotic, iturin A, on morphology and membrane ultrastructure of yeast cells
    • Thimon L, Peypoux F, Wallach J, Michel G (1995) Effect of the lipopeptide antibiotic, iturin A, on morphology and membrane ultrastructure of yeast cells. FEMS Microbiol Lett 128(2):101-106
    • (1995) FEMS Microbiol Lett , vol.128 , Issue.2 , pp. 101-106
    • Thimon, L.1    Peypoux, F.2    Wallach, J.3    Michel, G.4
  • 244
    • 0014512176 scopus 로고
    • Determination of amino acid sequences in oligopeptides by mass spectrometry. XVI. Revised structure of the peptide antibiotic esperin, established by mass spectrometry
    • Thomas DW, Ito T (1969) Determination of amino acid sequences in oligopeptides by mass spectrometry. XVI. Revised structure of the peptide antibiotic esperin, established by mass spectrometry. Tetrahedron 25(9):1985-1990
    • (1969) Tetrahedron , vol.25 , Issue.9 , pp. 1985-1990
    • Thomas, D.W.1    Ito, T.2
  • 245
    • 0030868265 scopus 로고    scopus 로고
    • Bacillus subtilis contains four closely related type I signal peptidases with overlapping substrate specificities. Constitutive and temporally controlled expression of different sip genes
    • DOI 10.1074/jbc.272.41.25983
    • Tjalsma H, Noback MA, Bron S, Venema G, Yamane K, van Dijl JM (1997) Bacillus subtilis contains four closely related type I signal peptidases with overlapping substrate specificities: constitutive and temporally controlled expression of different sip genes. J Biol Chem 272:25983-25992 (Pubitemid 27438926)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.41 , pp. 25983-25992
    • Tjalsma, H.1    Noback, M.A.2    Bron, S.3    Venema, G.4    Yamane, K.5    Van Dijl, J.M.6
  • 246
    • 0029013860 scopus 로고
    • Purification and structural determination of an inhibitor of starfish oocyte maturation from a Bacillus sp
    • Toraya T, Maoka T, Tsuji H, Kobayashi M (1995) Purification and structural determination of an inhibitor of starfish oocyte maturation from a Bacillus sp. Appl Environ Microbiol 61:1799-1804
    • (1995) Appl Environ Microbiol , vol.61 , pp. 1799-1804
    • Toraya, T.1    Maoka, T.2    Tsuji, H.3    Kobayashi, M.4
  • 247
    • 2342450559 scopus 로고    scopus 로고
    • Role of lipopeptides produced by Bacillus subtilis GA1 in the reduction of grey mould disease caused by Botrytis cinerea on apple
    • DOI 10.1111/j.1365-2672.2004.02252.x
    • Touré Y, Ongena M, Jacques P, Guiro A, Thonart P (2004) Role of lipopeptides produced by Bacillus subtilis GA1 in the reduction of grey mould disease caused by Botrytis cinerea on apple. J Appl Microbiol 96:1151-1160 (Pubitemid 38582163)
    • (2004) Journal of Applied Microbiology , vol.96 , Issue.5 , pp. 1151-1160
    • Toure, Y.1    Ongena, M.2    Jacques, P.3    Guiro, A.4    Thonart, P.5
  • 248
    • 0028102138 scopus 로고
    • Halobacillin: A cytotoxic cyclic acylpeptide of the iturin class produced by a marine Bacillus
    • DOI 10.1016/S0040-4039(00)77249-2
    • Trischman JA, Jensen PR, Fenical W (1994) Halobacillin: a cytotoxic cyclic acylpeptide of the iturin class produced by a marine Bacillus. Tetrahedron Lett 35(31):5571-5574 (Pubitemid 24248508)
    • (1994) Tetrahedron Letters , vol.35 , Issue.31 , pp. 5571-5574
    • Trischman, J.A.1    Jensen, P.R.2    Fenical, W.3
  • 249
    • 0029886333 scopus 로고    scopus 로고
    • Isolation of a gene essential for biosynthesis of the lipopeptide antibiotics plipastatin B1 and surfactin in Bacillus subtilis YB8
    • DOI 10.1007/s002030050322
    • Tsuge K, Ano T, Shoda M (1996) Isolation of a gene essential for biosynthesis of the lipopeptide antibiotics plipastatin B1 and surfactin in Bacillus subtilis YB8. Arch Microbiol 165:243-251 (Pubitemid 26155053)
    • (1996) Archives of Microbiology , vol.165 , Issue.4 , pp. 243-251
    • Tsuge, K.1    Ano, T.2    Shoda, M.3
  • 250
    • 0032874789 scopus 로고    scopus 로고
    • The genes degQ, pps, and lpa-8 (sfp) are responsible for conversion of Bacillus subtilis 168 to plipastatin production
    • Tsuge K, Ano T, Hirai M, Nakamura Y, Shoda M (1999) The genes degQ, pps, and lpa-8 (sfp) are responsible for conversion of Bacillus subtilis 168 to plipastatin production. Antimicrob Agents Chemother 43:2183-2192 (Pubitemid 29421198)
    • (1999) Antimicrobial Agents and Chemotherapy , vol.43 , Issue.9 , pp. 2183-2192
    • Tsuge, K.1    Ano, T.2    Hirai, M.3    Nakamura, Y.4    Shoda, M.5
  • 253
    • 0022469743 scopus 로고
    • 2, produced by Bacillus cereus BMG302-fF67 I. Taxonomy, production, isolation and preliminary characterization
    • Umezawa H, Aoyagi T, Nishikiori T, Okuyama A, Yamagishi Y, Hamada M, Takeuchi T (1986) Plipastatins: new inhibitors of phospholipase A2, produced by Bacillus cereus BMG302-fF67. I. Taxonomy, production, isolation and preliminary characterization. J Antibiot 39:737-744 (Pubitemid 16063644)
    • (1986) Journal of Antibiotics , vol.39 , Issue.6 , pp. 737-744
    • Umezawa, H.1    Aoyagi, T.2    Nishikiori, T.3
  • 254
    • 84902543474 scopus 로고    scopus 로고
    • Polymyxin derivatives and uses thereof, including for the treatment of Gram-negative bacterial infections
    • US Patent US 2009215677
    • Vaara MS, Vaara TI (2009) Polymyxin derivatives and uses thereof, including for the treatment of Gram-negative bacterial infections. US Patent US 2009215677
    • (2009)
    • Vaara, M.S.1    Vaara, T.I.2
  • 255
    • 0022457256 scopus 로고
    • Fengycin - A novel antifungal lipopeptide antibiotic produced by Bacillus subtilis F-29-3
    • Vanittanakom N, Loeffler W, Koch U, Jung G (1986) Fengycin a novel antifungal lipopeptide antibiotic produced by Bacillus subtilis F-29-3. J Antibiot 39(7):888-901 (Pubitemid 16038806)
    • (1986) Journal of Antibiotics , vol.39 , Issue.7 , pp. 888-901
    • Vanittanakom, N.1    Loeffler, W.2    Koch, U.3    Jung, G.4
  • 256
    • 0002908214 scopus 로고
    • Lipopeptides, an attractive class of microbial surfactants
    • Vater J (1986) Lipopeptides, an attractive class of microbial surfactants. Prog Colloid Polym Sci 72:12-18
    • (1986) Prog Colloid Polym Sci , vol.72 , pp. 12-18
    • Vater, J.1
  • 257
    • 0036952601 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption ionization-time of flight mass spectrometry of lipopeptide biosurfactants in whole cells and culture filtrates of Bacillus subtilis C-1 isolated from petroleum sludge
    • DOI 10.1128/AEM.68.12.6210-6219.2002
    • Vater J, Kablitz B, Wilde C, Franke P, Mehta N, Cameotra SS (2002) Matrix-assisted laser desorption ionization-time of flight mass spectrometry of lipopeptide biosurfactants in whole cells and culture filtrates of Bacillus subtilis C-1 isolated from petroleum sludge. Appl Environ Microbiol 68(12):6210-6219 (Pubitemid 36342458)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.12 , pp. 6210-6219
    • Vater, J.1    Kablitz, B.2    Wilde, C.3    Franke, P.4    Mehta, N.5    Cameotra, S.S.6
  • 259
    • 79851508812 scopus 로고    scopus 로고
    • Genome mining for ribosomally synthesized natural products
    • Velasquez JE, van der Donk WA (2011) Genome mining for ribosomally synthesized natural products. Curr Opin Chem Biol 15:11-21
    • (2011) Curr Opin Chem Biol , vol.15 , pp. 11-21
    • Velasquez, J.E.1    Van Der Donk, W.A.2
  • 260
    • 0014016796 scopus 로고
    • The chemistry of the polymyxin antibiotics
    • Vogler K, Studer RO (1966) The chemistry of the polymyxin antibiotics. Experientia 22:345-416
    • (1966) Experientia , vol.22 , pp. 345-416
    • Vogler, K.1    Studer, R.O.2
  • 261
    • 0038703416 scopus 로고    scopus 로고
    • Biosynthesis of isotopically labeled gramicidins and tyrocidins by Bacillus brevis
    • DOI 10.1023/A:1023074911861
    • Vogt TCB, Schinzel S, Bechinger B (2003) Biosynthesis of isotopically labeled gramicidins and tyrocidins by Bacillus brevis. J Biomol NMR 26(1):1-11 (Pubitemid 36553448)
    • (2003) Journal of Biomolecular NMR , vol.26 , Issue.1 , pp. 1-11
    • Vogt, T.C.B.1    Schinzel, S.2    Bechinger, B.3
  • 263
    • 0031015251 scopus 로고    scopus 로고
    • Antimycoplasma properties and application in cell culture of surfactin, a lipopeptide antibiotic from Bacillus subtilis
    • Vollenbroich D, Pauli G, Ozel M, Vater J (1997a) Antimycoplasma properties and applications in cell culture of surfactin, a lipopeptide antibiotic from Bacillus subtilis. Appl Environ Microbiol 63:44-49 (Pubitemid 27020367)
    • (1997) Applied and Environmental Microbiology , vol.63 , Issue.1 , pp. 44-49
    • Vollenbroich, D.1    Pauli, G.2    Ozel, M.3    Vater, J.4
  • 264
    • 0031234420 scopus 로고    scopus 로고
    • Mechanism of inactivation of enveloped viruses by the biosurfactant surfactin from Bacillus subtilis
    • DOI 10.1006/biol.1997.0099
    • Vollenbroich D, Ozel M, Vater J, Kamp RM, Pauli G (1997b) Mechanism of inactivation of enveloped viruses by the biosurfactant surfactin from Bacillus subtilis. Biologicals 25:289-297 (Pubitemid 27453251)
    • (1997) Biologicals , vol.25 , Issue.3 , pp. 289-297
    • Vollenbroich, D.1    Ozel, M.2    Vater, J.3    Kamp, R.M.4    Pauli, G.5
  • 265
    • 0033567189 scopus 로고    scopus 로고
    • NMR structure of active and inactive forms of the sterol-dependent antifungal antibiotic bacillomycin L
    • DOI 10.1046/j.1432-1327.1999.00605.x
    • Volpon L, Besson F, Lancelin J-M (1999) NMR structure of active and inactive forms of the sterol-dependent antifungal antibiotic bacillomycin L. Eur J Biochem 264:200-210 (Pubitemid 29385883)
    • (1999) European Journal of Biochemistry , vol.264 , Issue.1 , pp. 200-210
    • Volpon, L.1    Besson, F.2    Lancelin, J.-M.3
  • 266
    • 0034680763 scopus 로고    scopus 로고
    • NMR structure of antibiotics plipastatins A and B from Bacillus subtilis inhibitors of phospholipase A2
    • Volpon L, Besson F, Lancelin J-M (2000) NMR structure of antibiotics plipastatins A and B from Bacillus subtilis inhibitors of phospholipase A2. FEBS Lett 485:76-80
    • (2000) FEBS Lett , vol.485 , pp. 76-80
    • Volpon, L.1    Besson, F.2    Lancelin, J.-M.3
  • 267
    • 0022640540 scopus 로고
    • Structure of gramicidin A
    • Wallace BA (1986) Structure of gramicidin A. Biophys J 49:295-306
    • (1986) Biophys J , vol.49 , pp. 295-306
    • Wallace, B.A.1
  • 268
    • 0031830332 scopus 로고    scopus 로고
    • Recent advances in the high resolution structures of bacterial channels: Gramicidin A
    • Wallace BA (1998) Recent advances in the high resolution structures of bacterial channels: gramicidin A. J Struct Biol 121:123-141
    • (1998) J Struct Biol , vol.121 , pp. 123-141
    • Wallace, B.A.1
  • 269
    • 38949083855 scopus 로고    scopus 로고
    • The chemical versatility of natural-product assembly lines
    • Walsh CT (2008) The chemical versatility of natural-product assembly lines. Acc Chem Res 41:4-10
    • (2008) Acc Chem Res , vol.41 , pp. 4-10
    • Walsh, C.T.1
  • 270
    • 54249158674 scopus 로고    scopus 로고
    • Crystal structure of a molecular assembly line
    • Weissman KJ, Mueller R (2008) Crystal structure of a molecular assembly line. Angew Chem Int Edit 47:8344-8346
    • (2008) Angew Chem Int Edit , vol.47 , pp. 8344-8346
    • Weissman, K.J.1    Mueller, R.2
  • 271
    • 36949043952 scopus 로고
    • Structures of the polymixins A and the question of identity with the polymixin M
    • Wilkinson S, Lowe LA (1966) Structures of the polymixins A and the question of identity with the polymixin M. Nature 212(5059):311
    • (1966) Nature , vol.212 , Issue.5059 , pp. 311
    • Wilkinson, S.1    Lowe, L.A.2
  • 274
    • 0032919153 scopus 로고    scopus 로고
    • The Bacillus subtilis genome sequence: The molecular blueprint of a soil bacterium
    • DOI 10.1016/S0168-6496(98)00080-4, PII S0168649698000804
    • Wipat A, Harwood CR (1999) The Bacillus subtilis genome sequence: the molecular blueprint of a soil bacterium. FEMS Microbiol Ecol 28(1):1-9 (Pubitemid 29062908)
    • (1999) FEMS Microbiology Ecology , vol.28 , Issue.1 , pp. 1-9
    • Wipat, A.1    Harwood, C.R.2
  • 275
    • 0021081756 scopus 로고
    • The antibiotic edeine. XII. Isolation and structure of edeine F
    • Wojciechowska H, Zgoda W, Borowski E, Dziegielewski K, Ulikowski S (1983) The antibiotic edeine. XII. Isolation and structure of edeine F. J Antibiot 36(7):793-798 (Pubitemid 14231971)
    • (1983) Journal of Antibiotics , vol.36 , Issue.7 , pp. 793-798
    • Wojciechowska, H.1    Zgoda, W.2    Borowski, E.3
  • 276
    • 34547428004 scopus 로고    scopus 로고
    • Purification and characterization of the siderophore from Bacillus licheniformis K11, a multi-functional plant growth promoting rhizobacterium
    • Woo S-M, Woo JU, Kim S-D (2007) Purification and characterization of the siderophore from Bacillus licheniformis K11, a multifunctional plant growth-promoting rhizobacterium. Han'guk Misaengmul-Saengmyongkong Hakhoechi 35(2):128-134 (Pubitemid 47167791)
    • (2007) Korean Journal of Microbiology and Biotechnology , vol.35 , Issue.2 , pp. 128-134
    • Woo, S.-M.1    Jae, U.W.2    Kim, S.-D.3
  • 277
    • 4444366501 scopus 로고
    • Differential mechanism of action of the antibiotic edeine on prokaryotic and eukaryotic organism points to new basis for selective toxicity
    • Woynarowska B, Chmara H, Borowski E (1979) Differential mechanism of action of the antibiotic edeine on prokaryotic and eukaryotic organism points to new basis for selective toxicity. Drugs Exp Clin Res 5:181-186
    • (1979) Drugs Exp Clin Res , vol.5 , pp. 181-186
    • Woynarowska, B.1    Chmara, H.2    Borowski, E.3
  • 278
    • 0029206658 scopus 로고
    • A variable target intensity restrained global optimization (VARTIGO) procedure for determining three-dimensional structures of polypeptides from NOESY data: Application to gramicidin-S
    • Xu Y, Sugar IP, Krishna NR (1995) A variable target intensity restrained global optimization (VARTIGO) procedure for determining three-dimensional structures of polypeptides from NOESY data: application to gramicidin-S. J Biomol NMR 5:37-48
    • (1995) J Biomol NMR , vol.5 , pp. 37-48
    • Xu, Y.1    Sugar, I.P.2    Krishna, N.R.3
  • 279
    • 0029016528 scopus 로고
    • Characterization of a new lipopeptide surfactant produced by thermotolerant and halotolerant subsurface Bacillus licheniformis BAS50
    • Yakimov MM, Timmis KN, Wray V, Fredrickson HL (1995) Characterization of a new lipopeptide surfactant produced by thermotolerant and halotolerant subsurface Bacillus licheniformis BAS50. Appl Environ Microbiol 61:1706-1713
    • (1995) Appl Environ Microbiol , vol.61 , pp. 1706-1713
    • Yakimov, M.M.1    Timmis, K.N.2    Wray, V.3    Fredrickson, H.L.4
  • 282
    • 33745003659 scopus 로고    scopus 로고
    • Determination of the amino acid sequence in a cyclic lipopeptide using MS with DHT mechanism
    • DOI 10.1016/j.jbbm.2006.03.008, PII S0165022X06000674
    • Yang S, Wei D, Mu B (2006) Determination of the amino acid sequence in a cyclic lipopeptide using MS with DHT mechanism. J Biochem Biophys Methods 68:69-74 (Pubitemid 43866228)
    • (2006) Journal of Biochemical and Biophysical Methods , vol.68 , Issue.1 , pp. 69-74
    • Yang, S.-Z.1    Wei, D.-Z.2    Mu, B.-Z.3
  • 283
    • 71549158601 scopus 로고    scopus 로고
    • Study on the control of peach postharvest diseases using Bacillus subtilis
    • Yang Z, Guo H, Zhang X (2008) Study on the control of peach postharvest diseases using Bacillus subtilis. China Fruits 23:35-38
    • (2008) China Fruits , vol.23 , pp. 35-38
    • Yang, Z.1    Guo, H.2    Zhang, X.3
  • 284
    • 0018344296 scopus 로고
    • The structure of permetin A, a new polypeptin type antibiotic produced by Bacillus circulans
    • Yoko T, Asao M, Yoshiyuki T, Masatsune K (1979) The structure of permetin A, a new polypeptin type antibiotic produced by Bacillus circulans. J Antibiot 32(2):121-129
    • (1979) J Antibiot , vol.32 , Issue.2 , pp. 121-129
    • Yoko, T.1    Asao, M.2    Yoshiyuki, T.3    Masatsune, K.4
  • 286
    • 85153636936 scopus 로고    scopus 로고
    • The genus Bacillus
    • Goldman E, Green LH (eds) The Ohio State University, Columbus, OH
    • Zeigler DR, Perkins JB (2009) The genus Bacillus. In: Goldman E, Green LH (eds) Practical handbook of microbiology, 2nd edn. The Ohio State University, Columbus, OH, pp 309-337
    • (2009) Practical Handbook of Microbiology, 2nd Edn. , pp. 309-337
    • Zeigler, D.R.1    Perkins, J.B.2
  • 288
    • 70249115065 scopus 로고    scopus 로고
    • Study of the antifungal activity of Bacillus vallismortis ZZ185 in vitro and identification of its antifungal components
    • Zhenzhen Z, Qiushuo W, Kaimei W, Kemp B, Changhong L, Yucheng G (2010) Study of the antifungal activity of Bacillus vallismortis ZZ185 in vitro and identification of its antifungal components. Bioresour Technol 101:292-297
    • (2010) Bioresour Technol , vol.101 , pp. 292-297
    • Zhenzhen, Z.1    Qiushuo, W.2    Kaimei, W.3    Kemp, B.4    Changhong, L.5    Yucheng, G.6
  • 289
    • 50849130222 scopus 로고    scopus 로고
    • Novel roles of Bacillus thuringiensis to control plant diseases
    • Zhou Y, Choi YL, Sun M, Yu ZN (2008) Novel roles of Bacillus thuringiensis to control plant diseases. Appl Microbiol Biotechnol 80:563-572
    • (2008) Appl Microbiol Biotechnol , vol.80 , pp. 563-572
    • Zhou, Y.1    Choi, Y.L.2    Sun, M.3    Yu, Z.N.4


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