메뉴 건너뛰기




Volumn 78, Issue 5, 2010, Pages 1077-1087

The dawning of a 'Golden era' in lantibiotic bioengineering

Author keywords

[No Author keywords available]

Indexed keywords

ACTAGARDIN; CYSTEINE; DEXTRO ALANINE; DURAMYCIN; EPIDERMIN; GALLIDERMIN; HALODURACIN; HYDROXYBUTYRIC ACID; LACTICIN 3147; LACTICIN 481; LANTHIONINE; LANTIBIOTIC; LYSINOALANINE; MACEDOCIN; MECYSTEINE; MERSACIDIN; MICROBISPORICIN; MUTACIN B NY266; NISIN; NUKACIN ISK 1; PAENIBACILLIN; PLANOSPORICIN; PLANTARICIN C; SALIVARICIN B; TRYPTOPHAN; UNCLASSIFIED DRUG; VARIACIN; WARNERICIN RB4;

EID: 78649556678     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2010.07406.x     Document Type: Review
Times cited : (70)

References (103)
  • 1
    • 65749104456 scopus 로고    scopus 로고
    • Dissecting structural and functional diversity of the lantibiotic mersacidin
    • Appleyard, A.N., Choi, S., Read, D.M., Lightfoot, A., Boakes, S., Hoffmann, A., et al. (2009) Dissecting structural and functional diversity of the lantibiotic mersacidin. Chem Biol 16: 490-498.
    • (2009) Chem Biol , vol.16 , pp. 490-498
    • Appleyard, A.N.1    Choi, S.2    Read, D.M.3    Lightfoot, A.4    Boakes, S.5    Hoffmann, A.6
  • 2
    • 50949089673 scopus 로고    scopus 로고
    • Distinct contributions of the nisin biosynthesis enzymes NisB and NisC and transporter NisT to prenisin production by Lactococcus lactis
    • Van Den Berg van Saparoea, H.B., Bakkes, P.J., Moll, G.N., and Driessen, A.J. (2008) Distinct contributions of the nisin biosynthesis enzymes NisB and NisC and transporter NisT to prenisin production by Lactococcus lactis. Appl Environ Microbiol 74: 5541-5548.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 5541-5548
    • Van Den Berg van Saparoea, H.B.1    Bakkes, P.J.2    Moll, G.N.3    Driessen, A.J.4
  • 3
    • 65949089371 scopus 로고    scopus 로고
    • Lantibiotics: mode of action, biosynthesis and bioengineering
    • Bierbaum, G., and Sahl, H.G. (2009) Lantibiotics: mode of action, biosynthesis and bioengineering. Curr Pharm Biotechnol 10: 2-18.
    • (2009) Curr Pharm Biotechnol , vol.10 , pp. 2-18
    • Bierbaum, G.1    Sahl, H.G.2
  • 5
    • 65949124252 scopus 로고    scopus 로고
    • Organization of the genes encoding the biosynthesis of actagardine and engineering of a variant generation system
    • Boakes, S., Cortés, J., Appleyard, A.N., Rudd, B.A.M., and Dawson, M.J. (2009) Organization of the genes encoding the biosynthesis of actagardine and engineering of a variant generation system. Mol Microbiol 72: 1126-1136.
    • (2009) Mol Microbiol , vol.72 , pp. 1126-1136
    • Boakes, S.1    Cortés, J.2    Appleyard, A.N.3    Rudd, B.A.M.4    Dawson, M.J.5
  • 6
    • 33645779735 scopus 로고    scopus 로고
    • Insights into in vivo activities of lantibiotics from gallidermin and epidermin mode-of-action studies
    • Bonelli, R.R., Schneider, T., Sahl, H.G., and Wiedemann, I. (2006) Insights into in vivo activities of lantibiotics from gallidermin and epidermin mode-of-action studies. Antimicrob Agents Chemother 50: 1449-1457.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 1449-1457
    • Bonelli, R.R.1    Schneider, T.2    Sahl, H.G.3    Wiedemann, I.4
  • 7
    • 33645474378 scopus 로고    scopus 로고
    • Lipid II as a target for antibiotics
    • Breukink, E., and De Kruijff, B. (2006) Lipid II as a target for antibiotics. Nat Rev Drug Discov 5: 321-332.
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 321-332
    • Breukink, E.1    De Kruijff, B.2
  • 9
    • 0036848132 scopus 로고    scopus 로고
    • Nisin, alone and combined with peptidoglycan-modulating antibiotics: activity against methicillin-resistant Staphylococcus aureus and vancomycin-resistant enterococci
    • Brumfitt, W., Salton, M.R., and Hamilton-Miller, J.M. (2002) Nisin, alone and combined with peptidoglycan-modulating antibiotics: activity against methicillin-resistant Staphylococcus aureus and vancomycin-resistant enterococci. J Antimicrob Chemother 50: 731-734.
    • (2002) J Antimicrob Chemother , vol.50 , pp. 731-734
    • Brumfitt, W.1    Salton, M.R.2    Hamilton-Miller, J.M.3
  • 10
    • 34249086855 scopus 로고    scopus 로고
    • A novel lantibiotic acting on bacterial cell wall synthesis produced by the uncommon actinomycete Planomonospora sp
    • Castiglione, F., Cavaletti, L., Losi, D., Lazzarini, A., Carrano, L., Feroggio, M., et al. (2007) A novel lantibiotic acting on bacterial cell wall synthesis produced by the uncommon actinomycete Planomonospora sp. Biochemistry 46: 5884-5895.
    • (2007) Biochemistry , vol.46 , pp. 5884-5895
    • Castiglione, F.1    Cavaletti, L.2    Losi, D.3    Lazzarini, A.4    Carrano, L.5    Feroggio, M.6
  • 11
    • 38349060901 scopus 로고    scopus 로고
    • Determining the structure and mode of action of microbisporicin, a potent lantibiotic active against multiresistant pathogens
    • Castiglione, F., Lazzarini, A., Carrano, L., Corti, E., Ciciliato, I., Gastaldo, L., et al. (2008) Determining the structure and mode of action of microbisporicin, a potent lantibiotic active against multiresistant pathogens. Chem Biol 15: 22-31.
    • (2008) Chem Biol , vol.15 , pp. 22-31
    • Castiglione, F.1    Lazzarini, A.2    Carrano, L.3    Corti, E.4    Ciciliato, I.5    Gastaldo, L.6
  • 12
    • 14844340728 scopus 로고    scopus 로고
    • Biosynthesis and mode of action of lantibiotics
    • Chatterjee, C., Paul, M., Xie, L., and Van Der Donk, W.A. (2005) Biosynthesis and mode of action of lantibiotics. Chem Rev 105: 633-684.
    • (2005) Chem Rev , vol.105 , pp. 633-684
    • Chatterjee, C.1    Paul, M.2    Xie, L.3    Van Der Donk, W.A.4
  • 13
    • 33749658643 scopus 로고    scopus 로고
    • Engineering dehydro amino acids and thioethers into peptides using lacticin 481 synthetase
    • Chatterjee, C., Patton, G.C., Cooper, L., Paul, M., and Van Der Donk, W.A. (2006) Engineering dehydro amino acids and thioethers into peptides using lacticin 481 synthetase. Chem Biol 13: 1109-1117.
    • (2006) Chem Biol , vol.13 , pp. 1109-1117
    • Chatterjee, C.1    Patton, G.C.2    Cooper, L.3    Paul, M.4    Van Der Donk, W.A.5
  • 14
    • 0031842742 scopus 로고    scopus 로고
    • Structure-activity study of the lantibiotic mutacin II from Streptococcus mutans T8 by a gene replacement strategy
    • Chen, P., Novak, J., Kirk, M., Barnes, S., Qi, F., and Caufield, P.W. (1998) Structure-activity study of the lantibiotic mutacin II from Streptococcus mutans T8 by a gene replacement strategy. Appl Environ Microbiol 64: 2335-2340.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2335-2340
    • Chen, P.1    Novak, J.2    Kirk, M.3    Barnes, S.4    Qi, F.5    Caufield, P.W.6
  • 15
    • 53649090841 scopus 로고    scopus 로고
    • Structure-activity relationship studies of the two-component lantibiotic haloduracin
    • Cooper, L.E., McClerren, A.L., Chary, A., and Van Der Donk, W.A. (2008) Structure-activity relationship studies of the two-component lantibiotic haloduracin. Chem Biol 15: 1035-1045.
    • (2008) Chem Biol , vol.15 , pp. 1035-1045
    • Cooper, L.E.1    McClerren, A.L.2    Chary, A.3    Van Der Donk, W.A.4
  • 17
    • 13844314218 scopus 로고    scopus 로고
    • Bacterial lantibiotics: strategies to improve therapeutic potential
    • Cotter, P.D., Hill, C., and Ross, R.P. (2005a) Bacterial lantibiotics: strategies to improve therapeutic potential. Curr Protein Pept Sci 6: 61-75.
    • (2005) Curr Protein Pept Sci , vol.6 , pp. 61-75
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 18
    • 29444457743 scopus 로고    scopus 로고
    • Posttranslational conversion of l-serines to d-alanines is vital for optimal production and activity of the lantibiotic lacticin 3147
    • Cotter, P.D., O'Connor, P.M., Draper L.A., Lawton, E.M., Deegan, L.H., Hill, C., and Ross, R.P. (2005b) Posttranslational conversion of l-serines to d-alanines is vital for optimal production and activity of the lantibiotic lacticin 3147. Proc Natl Acad Sci USA 102: 18584-18589.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 18584-18589
    • Cotter, P.D.1    O'Connor, P.M.2    Draper, L.A.3    Lawton, E.M.4    Deegan, L.H.5    Hill, C.6    Ross, R.P.7
  • 19
    • 33749999203 scopus 로고    scopus 로고
    • Complete alanine scanning of the two-component lantibiotic lacticin 3147: generating a blueprint for rational drug design
    • Cotter, P.D., Deegan, L.H., Lawton, E.M., Draper, L.A., O'Connor, P.M., Hill C., and Ross, R.P. (2006) Complete alanine scanning of the two-component lantibiotic lacticin 3147: generating a blueprint for rational drug design. Mol Microbiol 62: 735-747.
    • (2006) Mol Microbiol , vol.62 , pp. 735-747
    • Cotter, P.D.1    Deegan, L.H.2    Lawton, E.M.3    Draper, L.A.4    O'Connor, P.M.5    Hill, C.6    Ross, R.P.7
  • 20
  • 21
    • 0030047564 scopus 로고    scopus 로고
    • Nisin Z, mutant nisin Z and lacticin 481 interactions with anionic lipids correlate with antimicrobial activity. A monolayer study
    • Demel, R.A., Peelen, T., Siezen, R.J., De, B., and Kuipers, O.P. (1996) Nisin Z, mutant nisin Z and lacticin 481 interactions with anionic lipids correlate with antimicrobial activity. A monolayer study. Eur J Biochem 235: 267-274.
    • (1996) Eur J Biochem , vol.235 , pp. 267-274
    • Demel, R.A.1    Peelen, T.2    Siezen, R.J.3    De, B.4    Kuipers, O.P.5
  • 22
    • 0026473125 scopus 로고
    • A lactococcal expression system for engineered nisins
    • Dodd, H.M., Horn, N., Hao, Z., and Gasson, M.J. (1992) A lactococcal expression system for engineered nisins. Appl Environ Microbiol 58: 3683-3693.
    • (1992) Appl Environ Microbiol , vol.58 , pp. 3683-3693
    • Dodd, H.M.1    Horn, N.2    Hao, Z.3    Gasson, M.J.4
  • 23
    • 0029146104 scopus 로고
    • A cassette vector for protein engineering the lantibiotic nisin
    • Dodd, H.M., Horn, N., and Gasson, M.J. (1995) A cassette vector for protein engineering the lantibiotic nisin. Gene 162: 163-164.
    • (1995) Gene , vol.162 , pp. 163-164
    • Dodd, H.M.1    Horn, N.2    Gasson, M.J.3
  • 24
    • 0030071838 scopus 로고    scopus 로고
    • A gene replacement strategy for engineering nisin
    • Dodd, H.M., Horn, N., Giffard, C.J., and Gasson, M.J. (1996) A gene replacement strategy for engineering nisin. Microbiology 142 (Part 1): 47-55.
    • (1996) Microbiology , vol.142 , Issue.PART 1 , pp. 47-55
    • Dodd, H.M.1    Horn, N.2    Giffard, C.J.3    Gasson, M.J.4
  • 25
    • 0037053393 scopus 로고    scopus 로고
    • Thiol-disulfide oxidoreductases are essential for the production of the lantibiotic sublancin 168
    • Dorenbos, R., Stein, T., Kabel, J., Bruand, C., Bolhuis, A., Bron, S., et al. (2002) Thiol-disulfide oxidoreductases are essential for the production of the lantibiotic sublancin 168. J Biol Chem 277: 16682-16688.
    • (2002) J Biol Chem , vol.277 , pp. 16682-16688
    • Dorenbos, R.1    Stein, T.2    Kabel, J.3    Bruand, C.4    Bolhuis, A.5    Bron, S.6
  • 26
    • 34548498172 scopus 로고    scopus 로고
    • A system for the random mutagenesis of the two-peptide lantibiotic lacticin 3147: analysis of mutants producing reduced antibacterial activities
    • Field, D., Collins, B., Cotter, P.D., Hill, C., and Ross, R.P. (2007) A system for the random mutagenesis of the two-peptide lantibiotic lacticin 3147: analysis of mutants producing reduced antibacterial activities. J Mol Microbiol Biotechnol 13: 226-234.
    • (2007) J Mol Microbiol Biotechnol , vol.13 , pp. 226-234
    • Field, D.1    Collins, B.2    Cotter, P.D.3    Hill, C.4    Ross, R.P.5
  • 27
    • 45149121558 scopus 로고    scopus 로고
    • The generation of nisin variants with enhanced activity against specific gram-positive pathogens
    • Field, D., Connor, P.M., Cotter, P.D., Hill, C., and Ross, R.P. (2008) The generation of nisin variants with enhanced activity against specific gram-positive pathogens. Mol Microbiol 69: 218-230.
    • (2008) Mol Microbiol , vol.69 , pp. 218-230
    • Field, D.1    Connor, P.M.2    Cotter, P.D.3    Hill, C.4    Ross, R.P.5
  • 28
    • 77954168712 scopus 로고    scopus 로고
    • Studies with bioengineered Nisin peptides highlight the broad-spectrum potency of Nisin V
    • Field, D., Quigley, L., O'Connor, P.M., Rea M.C., Daly, K., Cotter, P.D., et al. (2010) Studies with bioengineered Nisin peptides highlight the broad-spectrum potency of Nisin V. Microb Biotechnol 3: 473-486.
    • (2010) Microb Biotechnol , vol.3 , pp. 473-486
    • Field, D.1    Quigley, L.2    O'Connor, P.M.3    Rea, M.C.4    Daly, K.5    Cotter, P.D.6
  • 29
    • 77955814236 scopus 로고    scopus 로고
    • Microbisporicin gene cluster reveals unusual features of lantibiotic biosynthesis in actinomycetes
    • Foulston, L.C., and Bibb, M.J. (2010) Microbisporicin gene cluster reveals unusual features of lantibiotic biosynthesis in actinomycetes. Proc Natl Acad Sci USA 107: 13461-13466.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 13461-13466
    • Foulston, L.C.1    Bibb, M.J.2
  • 30
    • 47249093322 scopus 로고    scopus 로고
    • In vitro reconstitution and substrate specificity of a lantibiotic protease
    • Furgerson Ihnken, L.A., Chatterjee, C., and Van Der Donk, W.A. (2008) In vitro reconstitution and substrate specificity of a lantibiotic protease. Biochemistry 47: 7352-7363.
    • (2008) Biochemistry , vol.47 , pp. 7352-7363
    • Furgerson Ihnken, L.A.1    Chatterjee, C.2    Van Der Donk, W.A.3
  • 32
    • 77952668657 scopus 로고    scopus 로고
    • Microbial antagonists to food-borne pathogens and biocontrol
    • Gálvez, A., Abriouel, H., Benomar, N., and Lucas, R. (2010) Microbial antagonists to food-borne pathogens and biocontrol. Curr Opin Biotechnol 21: 142-148.
    • (2010) Curr Opin Biotechnol , vol.21 , pp. 142-148
    • Gálvez, A.1    Abriouel, H.2    Benomar, N.3    Lucas, R.4
  • 33
    • 0032917363 scopus 로고    scopus 로고
    • Lacticin 3147 displays activity in buffer against gram-positive bacterial pathogens which appear insensitive in standard plate assays
    • Galvin, M., Hill, C., and Ross, R.P. (1999) Lacticin 3147 displays activity in buffer against gram-positive bacterial pathogens which appear insensitive in standard plate assays. Lett Appl Microbiol 28: 355-358.
    • (1999) Lett Appl Microbiol , vol.28 , pp. 355-358
    • Galvin, M.1    Hill, C.2    Ross, R.P.3
  • 35
    • 0028238737 scopus 로고
    • Detection, purification, and partial characterization of plantaricin C, a bacteriocin produced by a Lactobacillus plantarum strain of dairy origin
    • González, B., Arca, P., Mayo, B., and Suárez, J.E. (1994) Detection, purification, and partial characterization of plantaricin C, a bacteriocin produced by a Lactobacillus plantarum strain of dairy origin. Appl Environ Microbiol 60: 2158-2163.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 2158-2163
    • González, B.1    Arca, P.2    Mayo, B.3    Suárez, J.E.4
  • 36
    • 77950563372 scopus 로고    scopus 로고
    • Discovery of unique lanthionine synthetases reveals new mechanistic and evolutionary insights
    • doi:1000310.1001371/journal.pbio.1000339
    • Goto, Y., Li, B., Claesen, J., Shi, Y., Bibb, M.J., and Van Der Donk, W.A. (2010) Discovery of unique lanthionine synthetases reveals new mechanistic and evolutionary insights. PLoS Biol 8: e1000339. doi:1000310.1001371/journal.pbio.1000339
    • (2010) PLoS Biol , vol.8
    • Goto, Y.1    Li, B.2    Claesen, J.3    Shi, Y.4    Bibb, M.J.5    Van Der Donk, W.A.6
  • 39
    • 33846145110 scopus 로고    scopus 로고
    • Isolation and identification of a Paenibacillus polymyxa strain that coproduces a novel lantibiotic and polymyxin
    • He, Z., Kisla, D., Zhang, L., Yuan, C., Green-Church, K.B., and Yousef, A.E. (2007) Isolation and identification of a Paenibacillus polymyxa strain that coproduces a novel lantibiotic and polymyxin. Appl Environ Microbiol 73: 168-178.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 168-178
    • He, Z.1    Kisla, D.2    Zhang, L.3    Yuan, C.4    Green-Church, K.B.5    Yousef, A.E.6
  • 40
    • 0037205949 scopus 로고    scopus 로고
    • Combination of antibiotic mechanisms in lantibiotics
    • Hoffmann, A., Pag, U., Wiedemann, I., and Sahl, H.G. (2002) Combination of antibiotic mechanisms in lantibiotics. Farmaco 57: 685-691.
    • (2002) Farmaco , vol.57 , pp. 685-691
    • Hoffmann, A.1    Pag, U.2    Wiedemann, I.3    Sahl, H.G.4
  • 41
    • 66949175869 scopus 로고    scopus 로고
    • Evaluation of essential and variable residues of nukacin ISK-1 by NNK scanning
    • Islam, M.R., Shioya, K., Nagao, J., Nishie, M., Jikuya, H., Zendo, T., et al. (2009) Evaluation of essential and variable residues of nukacin ISK-1 by NNK scanning. Mol Microbiol 72: 1438-1447.
    • (2009) Mol Microbiol , vol.72 , pp. 1438-1447
    • Islam, M.R.1    Shioya, K.2    Nagao, J.3    Nishie, M.4    Jikuya, H.5    Zendo, T.6
  • 42
    • 0033560968 scopus 로고    scopus 로고
    • Post-translational modification of nisin. The involvement of NisB in the dehydration process
    • Karakas Sen, A., Narbad, A., Horn, N., Dodd, H.M., Parr, A.J., Colquhoun, I., and Gasson, M.J. (1999) Post-translational modification of nisin. The involvement of NisB in the dehydration process. Eur J Biochem 261: 524-532.
    • (1999) Eur J Biochem , vol.261 , pp. 524-532
    • Karakas Sen, A.1    Narbad, A.2    Horn, N.3    Dodd, H.M.4    Parr, A.J.5    Colquhoun, I.6    Gasson, M.J.7
  • 43
    • 25444499680 scopus 로고    scopus 로고
    • Post-translational modification of therapeutic peptides by NisB, the dehydratase of the lantibiotic nisin
    • Kluskens, L.D., Kuipers, A., Rink, R., De Boef, E., Fekken, S., Driessen, A.J., et al. (2005) Post-translational modification of therapeutic peptides by NisB, the dehydratase of the lantibiotic nisin. Biochemistry 44: 12827-12834.
    • (2005) Biochemistry , vol.44 , pp. 12827-12834
    • Kluskens, L.D.1    Kuipers, A.2    Rink, R.3    De Boef, E.4    Fekken, S.5    Driessen, A.J.6
  • 44
    • 62449281004 scopus 로고    scopus 로고
    • Angiotensin-(1-7) with thioether bridge: an angiotensin-converting enzyme-resistant, potent angiotensin-(1-7) analog
    • Kluskens, L.D., Nelemans, S.A., Rink, R., De Vries, L., Meter-Arkema, A., Wang, Y., et al. (2009) Angiotensin-(1-7) with thioether bridge: an angiotensin-converting enzyme-resistant, potent angiotensin-(1-7) analog. J Pharmacol Exp Ther 328: 849-854.
    • (2009) J Pharmacol Exp Ther , vol.328 , pp. 849-854
    • Kluskens, L.D.1    Nelemans, S.A.2    Rink, R.3    De Vries, L.4    Meter-Arkema, A.5    Wang, Y.6
  • 45
    • 3843091511 scopus 로고    scopus 로고
    • The SapB morphogen is a lantibiotic-like peptide derived from the product of the developmental gene ramS in Streptomyces coelicolor
    • Kodani, S., Hudson, M.E., Durrant, M.C., Buttner, M.J., Nodwell, J.R., and Willey, J.M. (2004) The SapB morphogen is a lantibiotic-like peptide derived from the product of the developmental gene ramS in Streptomyces coelicolor. Proc Natl Acad Sci USA 101: 11448-11453.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 11448-11453
    • Kodani, S.1    Hudson, M.E.2    Durrant, M.C.3    Buttner, M.J.4    Nodwell, J.R.5    Willey, J.M.6
  • 46
    • 28244437191 scopus 로고    scopus 로고
    • SapT, a lanthionine-containing peptide involved in aerial hyphae formation in the streptomycetes
    • Kodani, S., Lodato, M.A., Durrant, M.C., Picart, F., and Willey, J.M. (2005) SapT, a lanthionine-containing peptide involved in aerial hyphae formation in the streptomycetes. Mol Microbiol 58: 1368-1380.
    • (2005) Mol Microbiol , vol.58 , pp. 1368-1380
    • Kodani, S.1    Lodato, M.A.2    Durrant, M.C.3    Picart, F.4    Willey, J.M.5
  • 49
    • 2542432896 scopus 로고    scopus 로고
    • NisT, the transporter of the lantibiotic nisin, can transport fully modified, dehydrated, and unmodified prenisin and fusions of the leader peptide with non-lantibiotic peptides
    • Kuipers, A., De Boef, E., Rink, R., Fekken, S., Kluskens, L.D., Driessen, A.J., et al. (2004) NisT, the transporter of the lantibiotic nisin, can transport fully modified, dehydrated, and unmodified prenisin and fusions of the leader peptide with non-lantibiotic peptides. J Biol Chem 279: 22176-22182.
    • (2004) J Biol Chem , vol.279 , pp. 22176-22182
    • Kuipers, A.1    De Boef, E.2    Rink, R.3    Fekken, S.4    Kluskens, L.D.5    Driessen, A.J.6
  • 51
    • 55049131364 scopus 로고    scopus 로고
    • Mechanistic dissection of the enzyme complexes involved in biosynthesis of lacticin 3147 and nisin
    • Kuipers, A., Meijer-Wierenga, J., Rink, R., Kluskens, L.D., and Moll, G.N. (2008) Mechanistic dissection of the enzyme complexes involved in biosynthesis of lacticin 3147 and nisin. Appl Environ Microbiol 74: 6591-6597.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 6591-6597
    • Kuipers, A.1    Meijer-Wierenga, J.2    Rink, R.3    Kluskens, L.D.4    Moll, G.N.5
  • 52
    • 66249125663 scopus 로고    scopus 로고
    • Translocation of a thioether-bridged azurin peptide fragment via the sec pathway in Lactococcus lactis
    • Kuipers, A., Rink, R., and Moll, G.N. (2009) Translocation of a thioether-bridged azurin peptide fragment via the sec pathway in Lactococcus lactis. Appl Environ Microbiol 75: 3800-3802.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 3800-3802
    • Kuipers, A.1    Rink, R.2    Moll, G.N.3
  • 53
    • 0026496892 scopus 로고
    • Engineering dehydrated amino acid residues in the antimicrobial peptide nisin
    • Kuipers, O.P., Rollema, H.S., Yap, W.M., Boot, H.J., Siezen, R.J., and De Vos, W.M. (1992) Engineering dehydrated amino acid residues in the antimicrobial peptide nisin. J Biol Chem 267: 24340-24346.
    • (1992) J Biol Chem , vol.267 , pp. 24340-24346
    • Kuipers, O.P.1    Rollema, H.S.2    Yap, W.M.3    Boot, H.J.4    Siezen, R.J.5    De Vos, W.M.6
  • 54
    • 0028142446 scopus 로고
    • Mass spectroscopic analysis of a novel enzymatic reaction. Oxidative decarboxylation of the lantibiotic precursor peptide EpiA catalyzed by the flavoprotein EpiD
    • Kupke, T., Kempter, C., Gnau, V., Jung, G., and Gotz, F. (1994) Mass spectroscopic analysis of a novel enzymatic reaction. Oxidative decarboxylation of the lantibiotic precursor peptide EpiA catalyzed by the flavoprotein EpiD. J Biol Chem 269: 5653-5659.
    • (1994) J Biol Chem , vol.269 , pp. 5653-5659
    • Kupke, T.1    Kempter, C.2    Gnau, V.3    Jung, G.4    Gotz, F.5
  • 55
  • 56
    • 43549100204 scopus 로고    scopus 로고
    • Use of lantibiotic synthetases for the preparation of bioactive constrained peptides
    • Levengood, M.R., and Van Der Donk, W.A. (2008) Use of lantibiotic synthetases for the preparation of bioactive constrained peptides. Bioorg Med Chem Lett 18: 3025-3028.
    • (2008) Bioorg Med Chem Lett , vol.18 , pp. 3025-3028
    • Levengood, M.R.1    Van Der Donk, W.A.2
  • 57
    • 69349083675 scopus 로고    scopus 로고
    • In vitro mutasynthesis of lantibiotic analogues containing nonproteinogenic amino acids
    • Levengood, M.R., Knerr, P.J., Oman, T.J., and Van Der Donk, W.A. (2009a) In vitro mutasynthesis of lantibiotic analogues containing nonproteinogenic amino acids. J Am Chem Soc 131: 12024-12025.
    • (2009) J Am Chem Soc , vol.131 , pp. 12024-12025
    • Levengood, M.R.1    Knerr, P.J.2    Oman, T.J.3    Van Der Donk, W.A.4
  • 58
    • 65549105876 scopus 로고    scopus 로고
    • Investigation of the substrate specificity of lacticin 481 synthetase by using nonproteinogenic amino acids
    • Levengood, M.R., Kerwood, C.C., Chatterjee, C., and Van Der Donk, W.A. (2009b) Investigation of the substrate specificity of lacticin 481 synthetase by using nonproteinogenic amino acids. Chembiochem 10: 911-919.
    • (2009) Chembiochem , vol.10 , pp. 911-919
    • Levengood, M.R.1    Kerwood, C.C.2    Chatterjee, C.3    Van Der Donk, W.A.4
  • 59
    • 34547137156 scopus 로고    scopus 로고
    • Identification of essential catalytic residues of the cyclase NisC involved in the biosynthesis of nisin
    • Li, B., and Van Der Donk, W.A. (2007) Identification of essential catalytic residues of the cyclase NisC involved in the biosynthesis of nisin. J Biol Chem 282: 21169-21175.
    • (2007) J Biol Chem , vol.282 , pp. 21169-21175
    • Li, B.1    Van Der Donk, W.A.2
  • 60
    • 33644854595 scopus 로고    scopus 로고
    • Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis
    • Li, B., Yu, J.P., Brunzelle, J.S., Moll, G.N., Van Der Donk, W.A., and Nair, S.K. (2006) Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis. Science 311: 1464-1467.
    • (2006) Science , vol.311 , pp. 1464-1467
    • Li, B.1    Yu, J.P.2    Brunzelle, J.S.3    Moll, G.N.4    Van Der Donk, W.A.5    Nair, S.K.6
  • 61
    • 49449112664 scopus 로고    scopus 로고
    • Influence of shifting positions of Ser, Thr, and Cys residues in prenisin on the efficiency of modification reactions and on the antimicrobial activities of the modified prepeptides
    • Lubelski, J., Overkamp, W., Kluskens, L.D., Moll, G.N., and Kuipers, O.P. (2008a) Influence of shifting positions of Ser, Thr, and Cys residues in prenisin on the efficiency of modification reactions and on the antimicrobial activities of the modified prepeptides. Appl Environ Microbiol 74: 4680-4685.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 4680-4685
    • Lubelski, J.1    Overkamp, W.2    Kluskens, L.D.3    Moll, G.N.4    Kuipers, O.P.5
  • 62
    • 38949166717 scopus 로고    scopus 로고
    • Biosynthesis, immunity, regulation, mode of action and engineering of the model lantibiotic nisin
    • Lubelski, J., Rink, R., Khusainov, R., Moll, G.N., and Kuipers, O.P. (2008b) Biosynthesis, immunity, regulation, mode of action and engineering of the model lantibiotic nisin. Cell Mol Life Sci 65: 455-476.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 455-476
    • Lubelski, J.1    Rink, R.2    Khusainov, R.3    Moll, G.N.4    Kuipers, O.P.5
  • 64
    • 77950113113 scopus 로고    scopus 로고
    • Production of a class II two-component lantibiotic of Streptococcus pneumoniae using the class I nisin synthetic machinery and leader sequence
    • Majchrzykiewicz, J.A., Lubelski, J., Moll, G.N., Kuipers, A., Bijlsma, J.J.E., Kuipers, O.P., and Rink, R. (2010) Production of a class II two-component lantibiotic of Streptococcus pneumoniae using the class I nisin synthetic machinery and leader sequence. Antimicrob Agents Chemother 54: 1498-1505.
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 1498-1505
    • Majchrzykiewicz, J.A.1    Lubelski, J.2    Moll, G.N.3    Kuipers, A.4    Bijlsma, J.J.E.5    Kuipers, O.P.6    Rink, R.7
  • 65
    • 0036178887 scopus 로고    scopus 로고
    • The flavoprotein MrsD catalyzes the oxidative decarboxylation reaction involved in formation of the peptidoglycan biosynthesis inhibitor mersacidin
    • Majer, F., Schmid, D.G., Altena, K., Bierbaum, G., and Kupke, T. (2002) The flavoprotein MrsD catalyzes the oxidative decarboxylation reaction involved in formation of the peptidoglycan biosynthesis inhibitor mersacidin. J Bacteriol 184: 1234-1243.
    • (2002) J Bacteriol , vol.184 , pp. 1234-1243
    • Majer, F.1    Schmid, D.G.2    Altena, K.3    Bierbaum, G.4    Kupke, T.5
  • 67
    • 0029115380 scopus 로고
    • Nucleotide sequence of the lantibiotic Pep5 biosynthetic gene cluster and functional analysis of PepP and PepC. Evidence for a role of PepC in thioether formation
    • Meyer, C., Bierbaum, G., Heidrich, C., Reis, M., Suling, J., Iglesias-Wind, M.I., et al. (1995) Nucleotide sequence of the lantibiotic Pep5 biosynthetic gene cluster and functional analysis of PepP and PepC. Evidence for a role of PepC in thioether formation. Eur J Biochem 232: 478-489.
    • (1995) Eur J Biochem , vol.232 , pp. 478-489
    • Meyer, C.1    Bierbaum, G.2    Heidrich, C.3    Reis, M.4    Suling, J.5    Iglesias-Wind, M.I.6
  • 68
    • 23844460885 scopus 로고    scopus 로고
    • Purification and characterization of warnericin RB4, anti-Alicyclobacillus bacteriocin, produced by Staphylococcus warneri RB4
    • Minamikawa, M., Kawai, Y., Inoue, N., and Yamazaki, K. (2005) Purification and characterization of warnericin RB4, anti-Alicyclobacillus bacteriocin, produced by Staphylococcus warneri RB4. Curr Microbiol 51: 22-26.
    • (2005) Curr Microbiol , vol.51 , pp. 22-26
    • Minamikawa, M.1    Kawai, Y.2    Inoue, N.3    Yamazaki, K.4
  • 69
    • 0033988560 scopus 로고    scopus 로고
    • MICs of mutacin B-Ny266, nisin A, vancomycin, and oxacillin against bacterial pathogens
    • Mota-Meira, M., LaPointe, G., Lacroix, C., and Lavoie, M.C. (2000) MICs of mutacin B-Ny266, nisin A, vancomycin, and oxacillin against bacterial pathogens. Antimicrob Agents Chemother 44: 24-29.
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 24-29
    • Mota-Meira, M.1    LaPointe, G.2    Lacroix, C.3    Lavoie, M.C.4
  • 70
    • 77953528770 scopus 로고    scopus 로고
    • In vitro biosynthesis of the prepeptide of type-III lantibiotic labyrinthopeptin A2 including formation of a C-C bond as a post-translational modification
    • Müller, W.M., Schmiederer, T., Ensle, P., and Süssmuth, R.D. (2010) In vitro biosynthesis of the prepeptide of type-III lantibiotic labyrinthopeptin A2 including formation of a C-C bond as a post-translational modification. Angew Chem Int Ed Engl 49: 2436-2440.
    • (2010) Angew Chem Int Ed Engl , vol.49 , pp. 2436-2440
    • Müller, W.M.1    Schmiederer, T.2    Ensle, P.3    Süssmuth, R.D.4
  • 71
    • 0025903443 scopus 로고
    • Activity of mersacidin, a novel peptide, compared with that of vancomycin, teicoplanin, and daptomycin
    • Niu, W.W., and Neu, H.C. (1991) Activity of mersacidin, a novel peptide, compared with that of vancomycin, teicoplanin, and daptomycin. Antimicrob Agents Chemother 35: 998-1000.
    • (1991) Antimicrob Agents Chemother , vol.35 , pp. 998-1000
    • Niu, W.W.1    Neu, H.C.2
  • 72
    • 0035122347 scopus 로고    scopus 로고
    • The application of a fermented food ingredient containing 'variacin', a novel antimicrobial produced by Kocuria varians, to control the growth of Bacillus cereus in chilled dairy products
    • O'Mahony, T., Rekhif, N., Cavadini, C., and Fitzgerald, G.F. (2001) The application of a fermented food ingredient containing 'variacin', a novel antimicrobial produced by Kocuria varians, to control the growth of Bacillus cereus in chilled dairy products. J Appl Microbiol 90: 106-114.
    • (2001) J Appl Microbiol , vol.90 , pp. 106-114
    • O'Mahony, T.1    Rekhif, N.2    Cavadini, C.3    Fitzgerald, G.F.4
  • 73
    • 70350170630 scopus 로고    scopus 로고
    • Insights into the mode of action of the two-peptide lantibiotic haloduracin
    • Oman, T.J., and Van Der Donk, W.A. (2009) Insights into the mode of action of the two-peptide lantibiotic haloduracin. ACS Chem Biol 4: 865-874.
    • (2009) ACS Chem Biol , vol.4 , pp. 865-874
    • Oman, T.J.1    Van Der Donk, W.A.2
  • 74
  • 75
    • 47249108199 scopus 로고    scopus 로고
    • The importance of the leader sequence for directing lanthionine formation in lacticin 481
    • Patton, G.C., Paul, M., Cooper, L.E., Chatterjee, C., and Van Der Donk, W.A. (2008) The importance of the leader sequence for directing lanthionine formation in lacticin 481. Biochemistry 47: 7342-7351.
    • (2008) Biochemistry , vol.47 , pp. 7342-7351
    • Patton, G.C.1    Paul, M.2    Cooper, L.E.3    Chatterjee, C.4    Van Der Donk, W.A.5
  • 76
    • 17044457776 scopus 로고    scopus 로고
    • Inducible production and cellular location of the epidermin biosynthetic enzyme EpiB using an improved staphylococcal expression system
    • Peschel, A., Ottenwälder, B., and Götz, F. (1996) Inducible production and cellular location of the epidermin biosynthetic enzyme EpiB using an improved staphylococcal expression system. FEMS Microbiol Lett 137: 279-284.
    • (1996) FEMS Microbiol Lett , vol.137 , pp. 279-284
    • Peschel, A.1    Ottenwälder, B.2    Götz, F.3
  • 78
    • 69049102140 scopus 로고    scopus 로고
    • A comparison of the activities of lacticin 3147 and nisin against drug-resistant Staphylococcus aureus and Enterococcus species
    • Piper, C., Draper, L.A., Cotter, P.D., Ross, R.P., and Hill, C. (2009b) A comparison of the activities of lacticin 3147 and nisin against drug-resistant Staphylococcus aureus and Enterococcus species. J Antimicrob Chemother 63: 546-551.
    • (2009) J Antimicrob Chemother , vol.63 , pp. 546-551
    • Piper, C.1    Draper, L.A.2    Cotter, P.D.3    Ross, R.P.4    Hill, C.5
  • 80
    • 34648825064 scopus 로고    scopus 로고
    • Dissection and modulation of the four distinct activities of nisin by mutagenesis of rings A and B and by C-terminal truncation
    • Rink, R., Wierenga, J., Kuipers, A., Kluskens, L.D., Driessen, A.J., Kuipers, O.P., and Moll, G.N. (2007b) Dissection and modulation of the four distinct activities of nisin by mutagenesis of rings A and B and by C-terminal truncation. Appl Environ Microbiol 73: 5809-5816.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 5809-5816
    • Rink, R.1    Wierenga, J.2    Kuipers, A.3    Kluskens, L.D.4    Driessen, A.J.5    Kuipers, O.P.6    Moll, G.N.7
  • 82
    • 0029093410 scopus 로고
    • Improvement of solubility and stability of the antimicrobial peptide nisin by protein engineering
    • Rollema, H.S., Kuipers, O.P., Both, P., De Vos, W.M., and Siezen, R.J. (1995) Improvement of solubility and stability of the antimicrobial peptide nisin by protein engineering. Appl Environ Microbiol 61: 2873-2878.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 2873-2878
    • Rollema, H.S.1    Kuipers, O.P.2    Both, P.3    De Vos, W.M.4    Siezen, R.J.5
  • 83
    • 0037113945 scopus 로고    scopus 로고
    • Preservation and fermentation: past, present and future
    • Ross, R.P., Morgan, S., and Hill, C. (2002) Preservation and fermentation: past, present and future. Int J Food Microbiol 79: 3-16.
    • (2002) Int J Food Microbiol , vol.79 , pp. 3-16
    • Ross, R.P.1    Morgan, S.2    Hill, C.3
  • 84
    • 55449108542 scopus 로고    scopus 로고
    • Multiple activities of natural agents such as defensins and bacteriocins suggest a change in strategy when developing new antimicrobials
    • Sahl, H., and Bierbaum, G. (2008) Multiple activities of natural agents such as defensins and bacteriocins suggest a change in strategy when developing new antimicrobials. Microbe 3: 467-473.
    • (2008) Microbe , vol.3 , pp. 467-473
    • Sahl, H.1    Bierbaum, G.2
  • 85
    • 0029055380 scopus 로고
    • Biosynthesis and biological activities of lantibiotics with unique post-translational modifications
    • Sahl, H., Jack, R., and Bierbaum, G. (1995) Biosynthesis and biological activities of lantibiotics with unique post-translational modifications. Eur J Biochem 230: 827-853.
    • (1995) Eur J Biochem , vol.230 , pp. 827-853
    • Sahl, H.1    Jack, R.2    Bierbaum, G.3
  • 87
    • 15844418684 scopus 로고    scopus 로고
    • Biosynthesis of lantibiotic nisin. Posttranslational modification of its prepeptide occurs at a multimeric membrane-associated lanthionine synthetase complex
    • Siegers, K., Heinzmann, S., and Entian, K.D. (1996) Biosynthesis of lantibiotic nisin. Posttranslational modification of its prepeptide occurs at a multimeric membrane-associated lanthionine synthetase complex. J Biol Chem 271: 12294-12301.
    • (1996) J Biol Chem , vol.271 , pp. 12294-12301
    • Siegers, K.1    Heinzmann, S.2    Entian, K.D.3
  • 88
    • 39149093008 scopus 로고    scopus 로고
    • Use of nisin and other bacteriocins for preservation of dairy products
    • Sobrino-Lopez, A., and Martin-Belloso, O. (2008) Use of nisin and other bacteriocins for preservation of dairy products. Int Dairy J 18: 329-343.
    • (2008) Int Dairy J , vol.18 , pp. 329-343
    • Sobrino-Lopez, A.1    Martin-Belloso, O.2
  • 89
    • 0017595190 scopus 로고
    • Gardimycin, a new antibiotic inhibiting peptidoglycan synthesis
    • Somma, S., Merati, W., and Parenti, F. (1977) Gardimycin, a new antibiotic inhibiting peptidoglycan synthesis. Antimicrob Agents Chemother 11: 396-401.
    • (1977) Antimicrob Agents Chemother , vol.11 , pp. 396-401
    • Somma, S.1    Merati, W.2    Parenti, F.3
  • 90
    • 0038155138 scopus 로고    scopus 로고
    • Construction of an expression system for site-directed mutagenesis of the lantibiotic mersacidin
    • Szekat, C., Jack, R.W., Skutlarek, D., Farber, H., and Bierbaum, G. (2003) Construction of an expression system for site-directed mutagenesis of the lantibiotic mersacidin. Appl Environ Microbiol 69: 3777-3783.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 3777-3783
    • Szekat, C.1    Jack, R.W.2    Skutlarek, D.3    Farber, H.4    Bierbaum, G.5
  • 91
    • 3442892702 scopus 로고    scopus 로고
    • Prevention of streptococcal pharyngitis by anti-Streptococcus pyogenes bacteriocin-like inhibitory substances (BLIS) produced by Streptococcus salivarius
    • Tagg, J.R. (2004) Prevention of streptococcal pharyngitis by anti-Streptococcus pyogenes bacteriocin-like inhibitory substances (BLIS) produced by Streptococcus salivarius. Indian J Med Res 119 (Suppl.): 13-16.
    • (2004) Indian J Med Res , vol.119 , Issue.SUPPL. , pp. 13-16
    • Tagg, J.R.1
  • 93
    • 0033811439 scopus 로고    scopus 로고
    • Lantibiotic biosynthesis: interactions between prelacticin 481 and its putative modification enzyme, LctM
    • Uguen, P., Le, J.P., and Dufour, A. (2000) Lantibiotic biosynthesis: interactions between prelacticin 481 and its putative modification enzyme, LctM. J Bacteriol 182: 5262-5266.
    • (2000) J Bacteriol , vol.182 , pp. 5262-5266
    • Uguen, P.1    Le, J.P.2    Dufour, A.3
  • 94
    • 0030804834 scopus 로고    scopus 로고
    • Influence of charge differences in the C-terminal part of nisin on antimicrobial activity and signaling capacity
    • Van Kraaij, C., Breukink, E., Rollema, H.S., Siezen, R.J., Demel, R.A., De, B., and Kuipers, O.P. (1997) Influence of charge differences in the C-terminal part of nisin on antimicrobial activity and signaling capacity. Eur J Biochem 247: 114-120.
    • (1997) Eur J Biochem , vol.247 , pp. 114-120
    • Van Kraaij, C.1    Breukink, E.2    Rollema, H.S.3    Siezen, R.J.4    Demel, R.A.5    De, B.6    Kuipers, O.P.7
  • 95
    • 70349385058 scopus 로고    scopus 로고
    • Streptococcal bacteriocins and the case for Streptococcus salivarius as model oral probiotics
    • Wescombe, P.A., Heng, N.C.K., Burton, J.P., Chilcott, C.N., and Tagg, J.R. (2009) Streptococcal bacteriocins and the case for Streptococcus salivarius as model oral probiotics. Future Microbiol 4: 819-835.
    • (2009) Future Microbiol , vol.4 , pp. 819-835
    • Wescombe, P.A.1    Heng, N.C.K.2    Burton, J.P.3    Chilcott, C.N.4    Tagg, J.R.5
  • 96
    • 0035910508 scopus 로고    scopus 로고
    • Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity
    • Wiedemann, I., Breukink, E., Van Kraaij, C., Kuipers, O.P., Bierbaum, G., De Kruijff, B., and Sahl, H.G. (2001) Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity. J Biol Chem 276: 1772-1779.
    • (2001) J Biol Chem , vol.276 , pp. 1772-1779
    • Wiedemann, I.1    Breukink, E.2    Van Kraaij, C.3    Kuipers, O.P.4    Bierbaum, G.5    De Kruijff, B.6    Sahl, H.G.7
  • 97
    • 33748506881 scopus 로고    scopus 로고
    • The mode of action of the lantibiotic lacticin 3147 - a complex mechanism involving specific interaction of two peptides and the cell wall precursor lipid II
    • Wiedemann, I., Bottiger, T., Bonelli, R.R., Wiese, A., Hagge, S.O., Gutsmann, T., et al. (2006a) The mode of action of the lantibiotic lacticin 3147 - a complex mechanism involving specific interaction of two peptides and the cell wall precursor lipid II. Mol Microbiol 61: 285-296.
    • (2006) Mol Microbiol , vol.61 , pp. 285-296
    • Wiedemann, I.1    Bottiger, T.2    Bonelli, R.R.3    Wiese, A.4    Hagge, S.O.5    Gutsmann, T.6
  • 99
    • 35848941716 scopus 로고    scopus 로고
    • Lantibiotics: peptides of diverse structure and function
    • Willey, J.M., and Van Der Donk, W.A. (2007) Lantibiotics: peptides of diverse structure and function. Annu Rev Microbiol 61: 477-501.
    • (2007) Annu Rev Microbiol , vol.61 , pp. 477-501
    • Willey, J.M.1    Van Der Donk, W.A.2
  • 102
    • 3142701459 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the hinge region of nisinZ and properties of nisinZ mutants
    • Yuan, J., Zhang, Z.Z., Chen, X.Z., Yang, W., and Huan, L.D. (2004) Site-directed mutagenesis of the hinge region of nisinZ and properties of nisinZ mutants. Appl Microbiol Biotechnol 64: 806-815.
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 806-815
    • Yuan, J.1    Zhang, Z.Z.2    Chen, X.Z.3    Yang, W.4    Huan, L.D.5
  • 103
    • 0031005553 scopus 로고    scopus 로고
    • The three-dimensional solution structure of the lantibiotic murein-biosynthesis-inhibitor actagardine determined by NMR
    • Zimmermann, N., and Jung, G. (1997) The three-dimensional solution structure of the lantibiotic murein-biosynthesis-inhibitor actagardine determined by NMR. Eur J Biochem 246: 809-819.
    • (1997) Eur J Biochem , vol.246 , pp. 809-819
    • Zimmermann, N.1    Jung, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.