메뉴 건너뛰기




Volumn 47, Issue 2, 2015, Pages 417-428

Lasso-inspired peptides with distinct antibacterial mechanisms

Author keywords

Antibacterial activity; Antimicrobial peptides; Microcin J25; Mode of action; Solid phase peptide synthesis

Indexed keywords

ANTIBIOTIC AGENT; CYSTEINYLGLYCYLALANYLGLYCYLPHENYLALANYLHISTIDINYLVALYLPROPYLCYSTEINYLTYROSYLPHENYLALANYLVALYLGLYCYLARGINYLGLYCYLTHREONYLPROPYLISOLEUCYLSERYLPHENYLALANYLTYROSYLGLYCINE; MICROCIN J25; PEPTIDE 7 21 C; PEPTIDE 8 21 C; PEPTIDE C 1; PEPTIDE C 3; PEPTIDE WK 7 21; RIFAMPICIN; RNA POLYMERASE; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; BACTERIOCIN; MICROCIN;

EID: 84925539859     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-014-1877-x     Document Type: Article
Times cited : (22)

References (47)
  • 2
    • 0037418765 scopus 로고    scopus 로고
    • Chemical modification of microcin J25 with diethylpyrocarbonate and carbodiimide: Evidence for essential histidyl and carboxyl residues
    • 1:CAS:528:DC%2BD3sXitlWhsbc%3D 12659839
    • Bellomio A, Rintoul MR, Morero RD (2003) Chemical modification of microcin J25 with diethylpyrocarbonate and carbodiimide: evidence for essential histidyl and carboxyl residues. Biochem Biophys Res Commun 303(2):458-462
    • (2003) Biochem Biophys Res Commun , vol.303 , Issue.2 , pp. 458-462
    • Bellomio, A.1    Rintoul, M.R.2    Morero, R.D.3
  • 3
    • 8844271864 scopus 로고    scopus 로고
    • The microcin J25 beta-hairpin region is important for antibiotic uptake but not for RNA polymerase and respiration inhibition
    • 1:CAS:528:DC%2BD2cXhtVSrsbvJ 15555591 10.1016/j.bbrc.2004.10.186
    • Bellomio A, Vincent PA, de Arcuri BF, Salomón RA, Morero RD, Farías RN (2004) The microcin J25 beta-hairpin region is important for antibiotic uptake but not for RNA polymerase and respiration inhibition. Biochem Biophys Res Commun 325(4):1454-1458. doi: 10.1016/j.bbrc.2004.10.186
    • (2004) Biochem Biophys Res Commun , vol.325 , Issue.4 , pp. 1454-1458
    • Bellomio, A.1    Vincent, P.A.2    De Arcuri, B.F.3    Salomón, R.A.4    Morero, R.D.5    Farías, R.N.6
  • 4
    • 34249791796 scopus 로고    scopus 로고
    • Microcin J25 has dual and independent mechanisms of action in Escherichia coli: RNA polymerase inhibition and increased superoxide production
    • 1:CAS:528:DC%2BD2sXmt1equrg%3D 1913388 17400747 10.1128/JB.00206-07
    • Bellomio A, Vincent PA, de Arcuri BF, Farías RN, Morero RD (2007) Microcin J25 has dual and independent mechanisms of action in Escherichia coli: RNA polymerase inhibition and increased superoxide production. J Bacteriol 189(11):4180-4186. doi: 10.1128/jb.00206-07
    • (2007) J Bacteriol , vol.189 , Issue.11 , pp. 4180-4186
    • Bellomio, A.1    Vincent, P.A.2    De Arcuri, B.F.3    Farías, R.N.4    Morero, R.D.5
  • 5
    • 0036449410 scopus 로고    scopus 로고
    • Thermolysin-linearized microcin J25 retains the structured core of the native macrocyclic peptide and displays antimicrobial activity
    • 1:CAS:528:DC%2BD3sXht1GlsA%3D%3D 12473117
    • Blond A, Cheminant M, Destoumieux-Garzón D, Ségalas-Milazzo I, Peduzzi J, Goulard C, Rebuffat S (2002) Thermolysin-linearized microcin J25 retains the structured core of the native macrocyclic peptide and displays antimicrobial activity. Eur J Biochem 269(24):6212-6222
    • (2002) Eur J Biochem , vol.269 , Issue.24 , pp. 6212-6222
    • Blond, A.1    Cheminant, M.2    Destoumieux-Garzón, D.3    Ségalas-Milazzo, I.4    Peduzzi, J.5    Goulard, C.6    Rebuffat, S.7
  • 6
    • 37049074206 scopus 로고
    • A new reagent for the cleavage of fully protected peptides synthesised on 2-chlorotrityl chloride resin
    • Bollhagen R, Schmiedberger M, Barlos K, Grell E (1994) A new reagent for the cleavage of fully protected peptides synthesised on 2-chlorotrityl chloride resin. J Chem Soc Chem Commun 22:2559-2560. doi: 10.1039/C39940002559
    • (1994) J Chem Soc Chem Commun , vol.22 , pp. 2559-2560
    • Bollhagen, R.1    Schmiedberger, M.2    Barlos, K.3    Grell, E.4
  • 7
    • 0029155042 scopus 로고
    • Energy-coupled transport and signal transduction through the gram-negative outer membrane via TonB-ExbB-ExbD-dependent receptor proteins
    • 1:CAS:528:DyaK2MXntFCrsLc%3D 7654405
    • Braun V (1995) Energy-coupled transport and signal transduction through the gram-negative outer membrane via TonB-ExbB-ExbD-dependent receptor proteins. FEMS Microbiol Rev 16(4):295-307
    • (1995) FEMS Microbiol Rev , vol.16 , Issue.4 , pp. 295-307
    • Braun, V.1
  • 8
    • 33748988741 scopus 로고    scopus 로고
    • Tryptophan- and arginine-rich antimicrobial peptides: Structures and mechanisms of action
    • 1:CAS:528:DC%2BD28XhtVanu7rP 16756942 10.1016/j.bbamem.2006.04.006
    • Chan DI, Prenner EJ, Vogel HJ (2006) Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action. Biochim Biophys Acta 1758(9):1184-1202. doi: 10.1016/j.bbamem.2006.04.006
    • (2006) Biochimica et Biophysica Acta , vol.1758 , Issue.9 , pp. 1184-1202
    • Chan, D.I.1    Prenner, E.J.2    Vogel, H.J.3
  • 9
    • 84903478669 scopus 로고    scopus 로고
    • Structure of an antibacterial peptide ATP-binding cassette transporter in a novel outward occluded state
    • 1:CAS:528:DC%2BC2cXpsFCjtr0%3D 4078857 24920594 10.1073/pnas.1320506111
    • Choudhury HG, Tong Z, Mathavan I, Li Y, Iwata S, Zirah S, Rebuffat S, van Veen HW, Beis K (2014) Structure of an antibacterial peptide ATP-binding cassette transporter in a novel outward occluded state. Proc Natl Acad Sci USA 111(25):9145-9150. doi: 10.1073/pnas.1320506111
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.25 , pp. 9145-9150
    • Choudhury, H.G.1    Tong, Z.2    Mathavan, I.3    Li, Y.4    Iwata, S.5    Zirah, S.6    Rebuffat, S.7    Van Veen, H.W.8    Beis, K.9
  • 10
    • 34547570547 scopus 로고    scopus 로고
    • Maturation of McjA precursor peptide into active microcin MccJ25
    • 1:CAS:528:DC%2BD2sXosVShtb0%3D 18019529
    • Clarke DJ, Campopiano DJ (2007) Maturation of McjA precursor peptide into active microcin MccJ25. Org Biomol Chem 5(16):2564-2566
    • (2007) Org Biomol Chem , vol.5 , Issue.16 , pp. 2564-2566
    • Clarke, D.J.1    Campopiano, D.J.2
  • 11
    • 33646271400 scopus 로고    scopus 로고
    • Microcin J25 uptake: His5 of the MccJ25 lariat ring is involved in interaction with the inner membrane MccJ25 transporter protein SbmA
    • de Cristóbal RE, Solbiati JO, Zenoff AM, Vincent PA, Salomón RA, Yuzenkova J, Severinov K, Farías RN (2006) Microcin J25 uptake: His5 of the MccJ25 lariat ring is involved in interaction with the inner membrane MccJ25 transporter protein SbmA. J Bacteriol 188(9):3324-3328. doi: 10.1128/jb.188.9.3324-3328.2006
    • (2006) J Bacteriol , vol.188 , Issue.9 , pp. 3324-3328
    • De Cristóbal, R.E.1    Solbiati, J.O.2    Zenoff, A.M.3    Vincent, P.A.4    Salomón, R.A.5    Yuzenkova, J.6    Severinov, K.7    Farías, R.N.8
  • 12
    • 0034932730 scopus 로고    scopus 로고
    • Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25
    • 1:CAS:528:DC%2BD3MXlsVens70%3D 95349 11443089 10.1128/JB.183.15.4543-4550.2001
    • Delgado MA, Rintoul MR, Farías RN, Salomón RA (2001) Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25. J Bacteriol 183(15):4543-4550. doi: 10.1128/jb.183.15.4543-4550.2001
    • (2001) J Bacteriol , vol.183 , Issue.15 , pp. 4543-4550
    • Delgado, M.A.1    Rintoul, M.R.2    Farías, R.N.3    Salomón, R.A.4
  • 13
    • 23644448769 scopus 로고    scopus 로고
    • The iron-siderophore transporter FhuA is the receptor for the antimicrobial peptide microcin J25: Role of the microcin Val11-Pro16 beta-hairpin region in the recognition mechanism
    • Destoumieux-Garzón D, Duquesne S, Peduzzi J, Goulard C, Desmadril M, Letellier L, Rebuffat S, Boulanger P (2005) The iron-siderophore transporter FhuA is the receptor for the antimicrobial peptide microcin J25: role of the microcin Val11-Pro16 beta-hairpin region in the recognition mechanism. Biochem J 389(Pt 3):869-876. doi: 10.1042/bj20042107
    • (2005) Biochem J , vol.389 , pp. 869-876
    • Destoumieux-Garzón, D.1    Duquesne, S.2    Peduzzi, J.3    Goulard, C.4    Desmadril, M.5    Letellier, L.6    Rebuffat, S.7    Boulanger, P.8
  • 14
    • 84863011911 scopus 로고    scopus 로고
    • Sequence determinants governing the topology and biological activity of a lasso peptide, microcin J25
    • 1:CAS:528:DC%2BC38Xhtl2gs7g%3D 22287061 10.1002/cbic.201100702
    • Ducasse R, Yan K-P, Goulard C, Blond A, Li Y, Lescop E, Guittet E, Rebuffat S, Zirah S (2012) Sequence determinants governing the topology and biological activity of a lasso peptide, microcin J25. ChemBioChem 13(3):371-380. doi: 10.1002/cbic.201100702
    • (2012) ChemBioChem , vol.13 , Issue.3 , pp. 371-380
    • Ducasse, R.1    Yan, K.-P.2    Goulard, C.3    Blond, A.4    Li, Y.5    Lescop, E.6    Guittet, E.7    Rebuffat, S.8    Zirah, S.9
  • 15
    • 79954850696 scopus 로고    scopus 로고
    • Microcin J25 membrane interaction: Selectivity toward gel phase
    • 1:CAS:528:DC%2BC3MXkvFaks70%3D 21376012 10.1016/j.bbamem.2011.02.018
    • Dupuy F, Morero R (2011) Microcin J25 membrane interaction: selectivity toward gel phase. Biochim Biophys Acta 1808(6):1764-1771. doi: 10.1016/j.bbamem.2011.02.018
    • (2011) Biochim Biophys Acta , vol.1808 , Issue.6 , pp. 1764-1771
    • Dupuy, F.1    Morero, R.2
  • 16
    • 69949103728 scopus 로고    scopus 로고
    • Proton motive force dissipation precludes interaction of microcin J25 with RNA polymerase, but enhances reactive oxygen species overproduction
    • 1:CAS:528:DC%2BD1MXhtFamsrvP 19616604 10.1016/j.bbagen.2009.07.006
    • Dupuy FG, Chirou MV, de Arcuri BF, Minahk CJ, Morero RD (2009) Proton motive force dissipation precludes interaction of microcin J25 with RNA polymerase, but enhances reactive oxygen species overproduction. Biochim Biophys Acta 1790(10):1307-1313. doi: 10.1016/j.bbagen.2009.07.006
    • (2009) Biochim Biophys Acta , vol.1790 , Issue.10 , pp. 1307-1313
    • Dupuy, F.G.1    Chirou, M.V.2    De Arcuri, B.F.3    Minahk, C.J.4    Morero, R.D.5
  • 17
    • 78349259753 scopus 로고    scopus 로고
    • An experimental and computational investigation of spontaneous lasso formation in microcin J25
    • 1:CAS:528:DC%2BC3cXhtlKkurzK 2965945 21044604 10.1016/j.bpj.2010.08.073
    • Ferguson AL, Zhang S, Dikiy I, Panagiotopoulos AZ, Debenedetti PG, James Link A (2010) An experimental and computational investigation of spontaneous lasso formation in microcin J25. Biophys J 99(9):3056-3065. doi: 10.1016/j.bpj.2010.08.073
    • (2010) Biophys J , vol.99 , Issue.9 , pp. 3056-3065
    • Ferguson, A.L.1    Zhang, S.2    Dikiy, I.3    Panagiotopoulos, A.Z.4    Debenedetti, P.G.5    James Link, A.6
  • 18
    • 0025232814 scopus 로고
    • Solid-phase peptide-synthesis utilizing 9-fluorenylmethoxycarbonyl amino-acids
    • 1:CAS:528:DyaK3cXksVWhsbg%3D 2191922
    • Fields GB, Noble RL (1990) Solid-phase peptide-synthesis utilizing 9-fluorenylmethoxycarbonyl amino-acids. Int J Pept Protein Res 35(3):161-214
    • (1990) Int J Pept Protein Res , vol.35 , Issue.3 , pp. 161-214
    • Fields, G.B.1    Noble, R.L.2
  • 19
    • 10744227640 scopus 로고    scopus 로고
    • Binding of pediocin PA-1 with anionic lipid induces model membrane destabilization
    • 1:CAS:528:DC%2BD3sXptVyktb4%3D 262285 14602640 10.1128/AEM.69.11.6777-6784.2003
    • Gaussier H, Lefèvre T, Subirade M (2003) Binding of pediocin PA-1 with anionic lipid induces model membrane destabilization. Appl Environ Microbiol 69(11):6777-6784. doi: 10.1128/AEM.69.11.6777-6784.2003
    • (2003) Appl Environ Microbiol , vol.69 , Issue.11 , pp. 6777-6784
    • Gaussier, H.1    Lefèvre, T.2    Subirade, M.3
  • 20
    • 37349104237 scopus 로고    scopus 로고
    • Alternative mechanisms of action of cationic antimicrobial peptides on bacteria
    • 1:CAS:528:DC%2BD2sXhtlKmtrbF 10.1586/14787210.5.6.951
    • Hale JD, Hancock RE (2007) Alternative mechanisms of action of cationic antimicrobial peptides on bacteria. Exp Rev Anti-infect Ther 5(6):951-959. doi: 10.1586/14787210.5.6.951
    • (2007) Exp Rev Anti-infect Ther , vol.5 , Issue.6 , pp. 951-959
    • Hale, J.D.1    Hancock, R.E.2
  • 21
    • 75749156624 scopus 로고    scopus 로고
    • Antimicrobial properties of aqueous extracts from three medicinal plants growing wild in arid regions of Tunisia
    • Hammami R, Zouhir A, Hamida JB, Neffati M, Vergoten G, Naghmouchi K, Fliss I (2009) Antimicrobial properties of aqueous extracts from three medicinal plants growing wild in arid regions of Tunisia. Pharm Biol 47(5):452-457. doi: 10.1080/13880200902822604
    • (2009) Pharm Biol , vol.47 , Issue.5 , pp. 452-457
    • Hammami, R.1    Zouhir, A.2    Hamida, J.B.3    Neffati, M.4    Vergoten, G.5    Naghmouchi, K.6    Fliss, I.7
  • 22
    • 0029808080 scopus 로고    scopus 로고
    • Strandedness discrimination in peptide-polynucleotide complexes
    • 1:CAS:528:DyaK28XltVKkurk%3D 8702670 10.1074/jbc.271.33.19675
    • Johnson NP, Mazarguil H, Lopez A (1996) Strandedness discrimination in peptide-polynucleotide complexes. J Biol Chem 271(33):19675-19679. doi: 10.1074/jbc.271.33.19675
    • (1996) J Biol Chem , vol.271 , Issue.33 , pp. 19675-19679
    • Johnson, N.P.1    Mazarguil, H.2    Lopez, A.3
  • 23
    • 0034584873 scopus 로고    scopus 로고
    • The use of circular dichroism in the investigation of protein structure and function
    • 1:CAS:528:DC%2BD3MXns1ehtw%3D%3D 12369905
    • Kelly SM, Price NC (2000) The use of circular dichroism in the investigation of protein structure and function. Curr Protein Pept Sci 1(4):349-384
    • (2000) Curr Protein Pept Sci , vol.1 , Issue.4 , pp. 349-384
    • Kelly, S.M.1    Price, N.C.2
  • 24
    • 44049109194 scopus 로고    scopus 로고
    • Linear analogues of human β-defensin 3: Concepts for design of antimicrobial peptides with reduced cytotoxicity to mammalian cells
    • 1:CAS:528:DC%2BD1cXltlemsb0%3D 18350527 10.1002/cbic.200700560
    • Liu S, Zhou L, Li J, Suresh A, Verma C, Foo YH, Yap EPH, Tan DTH, Beuerman RW (2008) Linear analogues of human β-defensin 3: concepts for design of antimicrobial peptides with reduced cytotoxicity to mammalian cells. ChemBioChem 9(6):964-973. doi: 10.1002/cbic.200700560
    • (2008) ChemBioChem , vol.9 , Issue.6 , pp. 964-973
    • Liu, S.1    Zhou, L.2    Li, J.3    Suresh, A.4    Verma, C.5    Foo, Y.H.6    Yap, E.P.H.7    Tan, D.T.H.8    Beuerman, R.W.9
  • 25
    • 34250017796 scopus 로고    scopus 로고
    • Efficacy of microcin J25 in biomatrices and in a mouse model of Salmonella infection
    • 1:CAS:528:DC%2BD2sXltVKgsrY%3D 17353221 10.1093/jac/dkm009
    • Lopez FE, Vincent PA, Zenoff AM, Salomón RA, Farías RN (2007) Efficacy of microcin J25 in biomatrices and in a mouse model of Salmonella infection. J Antimicrob Chemother 59(4):676-680. doi: 10.1093/jac/dkm009
    • (2007) J Antimicrob Chemother , vol.59 , Issue.4 , pp. 676-680
    • Lopez, F.E.1    Vincent, P.A.2    Zenoff, A.M.3    Salomón, R.A.4    Farías, R.N.5
  • 26
    • 0035856589 scopus 로고    scopus 로고
    • The antibacterial action of microcin J25: Evidence for disruption of cytoplasmic membrane energization in Salmonella newport
    • 1:CAS:528:DC%2BD3MXos1Kitrk%3D 11731133 10.1111/j.1574-6968.2001.tb10895.x
    • Rintoul MR, de Arcuri BF, Salomón RA, FarI'as RN, Morero RD (2001) The antibacterial action of microcin J25: evidence for disruption of cytoplasmic membrane energization in Salmonella newport. FEMS Microbiol Lett 204(2):265-270. doi: 10.1111/j.1574-6968.2001.tb10895.x
    • (2001) FEMS Microbiol Lett , vol.204 , Issue.2 , pp. 265-270
    • Rintoul, M.R.1    De Arcuri, B.F.2    Salomón, R.A.3    Fari'As, R.N.4    Morero, R.D.5
  • 27
    • 2942696237 scopus 로고    scopus 로고
    • Antibacterial peptide microcin J25 inhibits transcription by binding within and obstructing the RNA polymerase secondary channel
    • 1:CAS:528:DC%2BD2cXlslemtr8%3D 2754415 15200952 10.1016/j.molcel.2004.06.010
    • Mukhopadhyay J, Sineva E, Knight J, Levy RM, Ebright RH (2004) Antibacterial peptide microcin J25 inhibits transcription by binding within and obstructing the RNA polymerase secondary channel. Mol Cell 14(6):739-751. doi: 10.1016/j.molcel.2004.06.010
    • (2004) Mol Cell , vol.14 , Issue.6 , pp. 739-751
    • Mukhopadhyay, J.1    Sineva, E.2    Knight, J.3    Levy, R.M.4    Ebright, R.H.5
  • 28
    • 48349125030 scopus 로고    scopus 로고
    • Microcin J25 induces the opening of the mitochondrial transition pore and cytochrome c release through superoxide generation
    • Niklison Chirou M, Bellomio A, Dupuy F, Arcuri B, Minahk C, Morero R (2008) Microcin J25 induces the opening of the mitochondrial transition pore and cytochrome c release through superoxide generation. FEBS J 275(16):4088-4096. doi: 10.1111/j.1742-4658.2008.06550.x
    • (2008) FEBS J , vol.275 , Issue.16 , pp. 4088-4096
    • Niklison Chirou, M.1    Bellomio, A.2    Dupuy, F.3    Arcuri, B.4    Minahk, C.5    Morero, R.6
  • 29
    • 79953852240 scopus 로고    scopus 로고
    • Sequence diversity in the lasso peptide framework: Discovery of functional microcin J25 variants with multiple amino acid substitutions
    • 1:CAS:528:DC%2BC3MXivFyhurk%3D 21391585 10.1021/ja1109634
    • Pan SJ, Link AJ (2011) Sequence diversity in the lasso peptide framework: discovery of functional microcin J25 variants with multiple amino acid substitutions. J Am Chem Soc 133(13):5016-5023. doi: 10.1021/ja1109634
    • (2011) J Am Chem Soc , vol.133 , Issue.13 , pp. 5016-5023
    • Pan, S.J.1    Link, A.J.2
  • 30
    • 79951870980 scopus 로고    scopus 로고
    • Computational design of the lasso peptide antibiotic microcin J25
    • 1:CAS:528:DC%2BC3MXitlejsLg%3D 3038460 21106549 10.1093/protein/gzq108
    • Pan SJ, Cheung WL, Fung HK, Floudas CA, Link AJ (2011) Computational design of the lasso peptide antibiotic microcin J25. Protein Eng Des Sel 24(3):275-282. doi: 10.1093/protein/gzq108
    • (2011) Protein Eng des Sel , vol.24 , Issue.3 , pp. 275-282
    • Pan, S.J.1    Cheung, W.L.2    Fung, H.K.3    Floudas, C.A.4    Link, A.J.5
  • 31
    • 0032989894 scopus 로고    scopus 로고
    • A cyclic peptide analogue of the loop III region of platelet-derived growth factor-BB is a synthetic antigen for the native protein
    • 1:CAS:528:DyaK1MXitVSrt7k%3D 10195443 10.1111/j.1399-3011.1999.tb01618.x
    • Patel G, Husman W, Jehanli AM, Deadman JJ, Green D, Kakkar VV, Brennand DM (1999) A cyclic peptide analogue of the loop III region of platelet-derived growth factor-BB is a synthetic antigen for the native protein. J Pept Res 53(1):68-74. doi: 10.1111/j.1399-3011.1999.tb01618.x
    • (1999) J Pept Res , vol.53 , Issue.1 , pp. 68-74
    • Patel, G.1    Husman, W.2    Jehanli, A.M.3    Deadman, J.J.4    Green, D.5    Kakkar, V.V.6    Brennand, D.M.7
  • 32
    • 54449095128 scopus 로고    scopus 로고
    • Systematic structure-activity analysis of microcin J25
    • 1:CAS:528:DC%2BD1cXhtVyisLnL 2533079 18632663 10.1074/jbc.M803995200
    • Pavlova O, Mukhopadhyay J, Sineva E, Ebright RH, Severinov K (2008) Systematic structure-activity analysis of microcin J25. J Biol Chem 283(37):25589-25595. doi: 10.1074/jbc.M803995200
    • (2008) J Biol Chem , vol.283 , Issue.37 , pp. 25589-25595
    • Pavlova, O.1    Mukhopadhyay, J.2    Sineva, E.3    Ebright, R.H.4    Severinov, K.5
  • 33
    • 0141919822 scopus 로고    scopus 로고
    • Microcin J25 has a threaded sidechain-to-backbone ring structure and not a head-to-tail cyclized backbone
    • 1:CAS:528:DC%2BD3sXntlyqt7o%3D 14531690 10.1021/ja0367703
    • Rosengren KJ, Clark RJ, Daly NL, Göransson U, Jones A, Craik DJ (2003) Microcin J25 has a threaded sidechain-to-backbone ring structure and not a head-to-tail cyclized backbone. J Am Chem Soc 125(41):12464-12474. doi: 10.1021/ja0367703
    • (2003) J Am Chem Soc , vol.125 , Issue.41 , pp. 12464-12474
    • Rosengren, K.J.1    Clark, R.J.2    Daly, N.L.3    Göransson, U.4    Jones, A.5    Craik, D.J.6
  • 34
    • 0033771074 scopus 로고    scopus 로고
    • Antibacterial activity evaluation of microcin J25 against diarrheagenic Escherichia coli
    • 1:CAS:528:DC%2BD3cXnt1ClsL0%3D 92352 11010926
    • Sable S, Pons AM, Gendron-Gaillard S, Cottenceau G (2000) Antibacterial activity evaluation of microcin J25 against diarrheagenic Escherichia coli. Appl Environ Microbiol 66(10):4595-4597
    • (2000) Appl Environ Microbiol , vol.66 , Issue.10 , pp. 4595-4597
    • Sable, S.1    Pons, A.M.2    Gendron-Gaillard, S.3    Cottenceau, G.4
  • 35
    • 0027369822 scopus 로고
    • The FhuA protein is involved in microcin 25 uptake
    • 206939 8244949
    • Salomón RA, Farías RN (1993) The FhuA protein is involved in microcin 25 uptake. J Bacteriol 175(23):7741-7742
    • (1993) J Bacteriol , vol.175 , Issue.23 , pp. 7741-7742
    • Salomón, R.A.1    Farías, R.N.2
  • 36
    • 0029045349 scopus 로고
    • The peptide antibiotic microcin 25 is imported through the TonB pathway and the SbmA protein
    • 177028 7768835
    • Salomón RA, Farías RN (1995) The peptide antibiotic microcin 25 is imported through the TonB pathway and the SbmA protein. J Bacteriol 177(11):3323-3325
    • (1995) J Bacteriol , vol.177 , Issue.11 , pp. 3323-3325
    • Salomón, R.A.1    Farías, R.N.2
  • 37
    • 18944379638 scopus 로고    scopus 로고
    • Structure-activity analysis of microcin J25: Distinct parts of the threaded lasso molecule are responsible for interaction with bacterial RNA polymerase
    • 1:CAS:528:DC%2BD2MXks12ntbc%3D 1112051 15901712 10.1128/JB.187.11.3859-3863.2005
    • Semenova E, Yuzenkova Y, Peduzzi J, Rebuffat S, Severinov K (2005) Structure-activity analysis of microcin J25: distinct parts of the threaded lasso molecule are responsible for interaction with bacterial RNA polymerase. J Bacteriol 187(11):3859-3863. doi: 10.1128/jb.187.11.3859-3863.2005
    • (2005) J Bacteriol , vol.187 , Issue.11 , pp. 3859-3863
    • Semenova, E.1    Yuzenkova, Y.2    Peduzzi, J.3    Rebuffat, S.4    Severinov, K.5
  • 38
    • 51249099169 scopus 로고    scopus 로고
    • FTIR studies of temperature influence on the DPPG model membrane
    • 1:CAS:528:DC%2BD1cXhtFenurjN 10.1016/j.molstruc.2008.02.039
    • Severcan F, Dorohoi DO (2008) FTIR studies of temperature influence on the DPPG model membrane. J Mol Struct 887(1-3):117-121. doi: 10.1016/j.molstruc.2008.02.039
    • (2008) J Mol Struct , vol.887 , Issue.1-3 , pp. 117-121
    • Severcan, F.1    Dorohoi, D.O.2
  • 39
    • 0030006825 scopus 로고    scopus 로고
    • Genetic analysis of plasmid determinants for microcin J25 production and immunity
    • 1:CAS:528:DyaK28XjsFGltrw%3D 178142 8655570
    • Solbiati JO, Ciaccio M, Farías RN, Salomón RA (1996) Genetic analysis of plasmid determinants for microcin J25 production and immunity. J Bacteriol 178(12):3661-3663
    • (1996) J Bacteriol , vol.178 , Issue.12 , pp. 3661-3663
    • Solbiati, J.O.1    Ciaccio, M.2    Farías, R.N.3    Salomón, R.A.4
  • 40
    • 84862817125 scopus 로고    scopus 로고
    • Synthetic peptides derived from the sequence of a lasso peptide microcin J25 show antibacterial activity
    • 1:CAS:528:DC%2BC38XhvFeis7k%3D 22304849 10.1016/j.bmc.2011.12.061
    • Soudy R, Wang L, Kaur K (2012) Synthetic peptides derived from the sequence of a lasso peptide microcin J25 show antibacterial activity. Bioorg Med Chem 20(5):1794-1800. doi: 10.1016/j.bmc.2011.12.061
    • (2012) Bioorg Med Chem , vol.20 , Issue.5 , pp. 1794-1800
    • Soudy, R.1    Wang, L.2    Kaur, K.3
  • 41
    • 1642546383 scopus 로고    scopus 로고
    • Computation and analysis of protein circular dichroism spectra
    • B. Ludwig L.J. Michael (eds) 383 Academic Press St Louis 10.1016/S0076-6879(04)83013-1
    • Sreerama N, Woody RW (2004) Computation and analysis of protein circular dichroism spectra. In: Ludwig B, Michael LJ (eds) Methods in enzymology, vol 383. Academic Press, St Louis, pp 318-351. doi: 10.1016/S0076-6879(04)83013-1
    • (2004) Methods in Enzymology , pp. 318-351
    • Sreerama, N.1    Woody, R.W.2
  • 42
    • 12044255356 scopus 로고
    • Disulfide bond formation in peptides by dimethyl-sulfoxide - Scope and applications
    • 1:CAS:528:DyaK3MXkvFaqs7s%3D 10.1021/ja00017a044
    • Tam JP, Wu CR, Liu W, Zhang JW (1991) Disulfide bond formation in peptides by dimethyl-sulfoxide - scope and applications. J Am Chem Soc 113(17):6657-6662. doi: 10.1021/Ja00017a044
    • (1991) J Am Chem Soc , vol.113 , Issue.17 , pp. 6657-6662
    • Tam, J.P.1    Wu, C.R.2    Liu, W.3    Zhang, J.W.4
  • 43
    • 2942722262 scopus 로고    scopus 로고
    • Inhibition of Salmonella enterica serovars by microcin J25
    • 1:CAS:528:DC%2BD2cXltVKnsrs%3D 15212798 10.1111/j.1574-6968.2004.tb09634.x
    • Vincent PA, Delgado MA, Farías RN, Salomón RA (2004) Inhibition of Salmonella enterica serovars by microcin J25. FEMS Microbiol Lett 236(1):103-107. doi: 10.1016/j.femsle.2004.05.027
    • (2004) FEMS Microbiol Lett , vol.236 , Issue.1 , pp. 103-107
    • Vincent, P.A.1    Delgado, M.A.2    Farías, R.N.3    Salomón, R.A.4
  • 44
    • 18044379916 scopus 로고    scopus 로고
    • MccJ25 C-terminal is involved in RNA-polymerase inhibition but not in respiration inhibition
    • 1:CAS:528:DC%2BD2MXjsFGrtbg%3D 15850794 10.1016/j.bbrc.2005.03.220
    • Vincent PA, Bellomio A, de Arcuri BF, Farías RN, Morero RD (2005) MccJ25 C-terminal is involved in RNA-polymerase inhibition but not in respiration inhibition. Biochem Biophys Res Commun 331(2):549-551. doi: 10.1016/j.bbrc.2005.03.220
    • (2005) Biochem Biophys Res Commun , vol.331 , Issue.2 , pp. 549-551
    • Vincent, P.A.1    Bellomio, A.2    De Arcuri, B.F.3    Farías, R.N.4    Morero, R.D.5
  • 45
    • 0141919821 scopus 로고    scopus 로고
    • Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail
    • 1:CAS:528:DC%2BD3sXntlyqt74%3D 14531691 10.1021/ja036756q
    • Wilson K-A, Kalkum M, Ottesen J, Yuzenkova J, Chait BT, Landick R, Muir T, Severinov K, Darst SA (2003) Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail. J Am Chem Soc 125(41):12475-12483. doi: 10.1021/ja036756q
    • (2003) J Am Chem Soc , vol.125 , Issue.41 , pp. 12475-12483
    • Wilson, K.-A.1    Kalkum, M.2    Ottesen, J.3    Yuzenkova, J.4    Chait, B.T.5    Landick, R.6    Muir, T.7    Severinov, K.8    Darst, S.A.9
  • 46
    • 84860232127 scopus 로고    scopus 로고
    • Dissecting the maturation steps of the lasso peptide microcin J25 in vitro
    • 1:CAS:528:DC%2BC38XltVyitrk%3D 22488892 10.1002/cbic.201200016
    • Yan K-P, Li Y, Zirah S, Goulard C, Knappe TA, Marahiel MA, Rebuffat S (2012) Dissecting the maturation steps of the lasso peptide microcin J25 in vitro. ChemBioChem 13(7):1046-1052. doi: 10.1002/cbic.201200016
    • (2012) ChemBioChem , vol.13 , Issue.7 , pp. 1046-1052
    • Yan, K.-P.1    Li, Y.2    Zirah, S.3    Goulard, C.4    Knappe, T.A.5    Marahiel, M.A.6    Rebuffat, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.