메뉴 건너뛰기




Volumn 516, Issue , 2012, Pages 3-24

In vivo production of thiopeptide variants

Author keywords

Biosynthetic engineering; Micrococcin; Nosiheptide; Polythiazolyl peptides; Posttranslational modification; Site directed mutagenesis; Thiocillin; Thiopeptides; Thiostrepton

Indexed keywords

APRAMYCIN; BACTERIAL VECTOR; CHLORAMPHENICOL; FOSMIDOMYCIN; NOSIHEPTIDE; POLYPEPTIDE ANTIBIOTIC AGENT; THIOCILLIN; THIOSTREPTON A; THIOSTREPTON C; UNCLASSIFIED DRUG;

EID: 84866973856     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/B978-0-12-394291-3.00022-8     Document Type: Chapter
Times cited : (21)

References (85)
  • 1
    • 72249098749 scopus 로고    scopus 로고
    • Generation of thiocillin variants by prepeptide gene replacement and in vivo processing by Bacillus cereus
    • M.G. Acker, A.A. Bowers, and C.T. Walsh Generation of thiocillin variants by prepeptide gene replacement and in vivo processing by Bacillus cereus Journal of the American Chemical Society 131 2009 17563 17565
    • (2009) Journal of the American Chemical Society , vol.131 , pp. 17563-17565
    • Acker, M.G.1    Bowers, A.A.2    Walsh, C.T.3
  • 2
    • 79953207333 scopus 로고    scopus 로고
    • Thiostrepton and derivatives exhibit antimalarial and gametocytocidal activity by dually targeting parasite proteasome and apicoplast
    • M.N. Aminake, S. Schoof, L. Sologub, M. Leubner, M. Kirschner, and H.D. Arndt Thiostrepton and derivatives exhibit antimalarial and gametocytocidal activity by dually targeting parasite proteasome and apicoplast Antimicrobial Agents and Chemotherapy 55 2011 1338 1348
    • (2011) Antimicrobial Agents and Chemotherapy , vol.55 , pp. 1338-1348
    • Aminake, M.N.1    Schoof, S.2    Sologub, L.3    Leubner, M.4    Kirschner, M.5    Arndt, H.D.6
  • 4
    • 8744309111 scopus 로고    scopus 로고
    • New vector for efficient allelic replacement in naturally nontransformable, low-GC-content, gram-positive bacteria
    • DOI 10.1128/AEM.70.11.6887-6891.2004
    • M. Arnaud, A. Chastanet, and M. Débarbouillé New vector for efficient allelic replacement in naturally nontransformable, low-GC-content, Gram-positive bacteria Applied and Environmental Microbiology 70 2004 6887 6891 (Pubitemid 39518603)
    • (2004) Applied and Environmental Microbiology , vol.70 , Issue.11 , pp. 6887-6891
    • Arnaud, M.1    Chastanet, A.2    Debarbouille, M.3
  • 5
    • 68049109443 scopus 로고    scopus 로고
    • An improved synthesis of pyridine-thiazole cores of thiopeptide antibiotics
    • V.S. Aulakh, and M.A. Ciufolini An improved synthesis of pyridine-thiazole cores of thiopeptide antibiotics The Journal of Organic Chemistry 74 2009 5750 5753
    • (2009) The Journal of Organic Chemistry , vol.74 , pp. 5750-5753
    • Aulakh, V.S.1    Ciufolini, M.A.2
  • 7
    • 23844441838 scopus 로고    scopus 로고
    • Interactions of the N-terminal domain of ribosomal protein L11 with thiostrepton and rRNA
    • DOI 10.1074/jbc.M504182200
    • S.L. Bausch, E. Poliakova, and D.E. Draper Interactions of the N-terminal domain of ribosomal protein L11 with thiostrepton and rRNA The Journal of Biological Chemistry 280 2005 29956 29963 (Pubitemid 41177074)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.33 , pp. 29956-29963
    • Bausch, S.L.1    Poliakova, E.2    Draper, D.E.3
  • 8
    • 0019035882 scopus 로고
    • Effect of nosiheptide as a feed additive in chicks on the quantity, duration, prevalence of excretion, and resistance to antibacterial agents of Salmonella typhimurium; On the proportion of Escherichia coli and other coliforms resistant to antibacterial agents; And on their degree and spectrum of resistance
    • F. Benazet, and J.R. Cartier Effect of nosiheptide as a feed additive in chicks on the quantity, duration, prevalence of excretion, and resistance to antibacterial agents of Salmonella typhimurium; on the proportion of Escherichia coli and other coliforms resistant to antibacterial agents; and on their degree and spectrum of resistance Poultry Science 59 1980 1405 1415
    • (1980) Poultry Science , vol.59 , pp. 1405-1415
    • Benazet, F.1    Cartier, J.R.2
  • 9
    • 0018832015 scopus 로고
    • Nosiheptide, a sulfur-containing peptide antibiotic isolated from Streptomyces actuosus 40037
    • F. Benazet, M. Cartier, J. Florent, C. Godard, G. Jung, and J. Lunel Nosiheptide, a sulfur-containing peptide antibiotic isolated from Streptomyces actuosus 40037 Experientia 36 1980 414 416 (Pubitemid 10081644)
    • (1980) Experientia , vol.36 , Issue.4 , pp. 414-416
    • Benazet, F.1    Cartier, M.2    Florent, J.3
  • 10
    • 78349285987 scopus 로고    scopus 로고
    • Nucleoid occlusion prevents cell division during replication fork arrest in Bacillus subtilis
    • R. Bernard, K.A. Marquis, and D.Z. Rudner Nucleoid occlusion prevents cell division during replication fork arrest in Bacillus subtilis Molecular Microbiology 78 2010 866 882
    • (2010) Molecular Microbiology , vol.78 , pp. 866-882
    • Bernard, R.1    Marquis, K.A.2    Rudner, D.Z.3
  • 11
    • 68949154568 scopus 로고    scopus 로고
    • FoxM1 is a general target for proteasome inhibitors
    • U.G. Bhat, M. Halasi, and A.L. Gartel FoxM1 is a general target for proteasome inhibitors PloS One 4 2009 e6593
    • (2009) PloS One , vol.4 , pp. 6593
    • Bhat, U.G.1    Halasi, M.2    Gartel, A.L.3
  • 12
    • 0026645203 scopus 로고
    • Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp
    • M. Bierman, R. Logan, K. O'Brien, E.T. Seno, R.N. Rao, and B.E. Schoner Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp Gene 116 1992 43 49
    • (1992) Gene , vol.116 , pp. 43-49
    • Bierman, M.1    Logan, R.2    O'Brien, K.3    Seno, E.T.4    Rao, R.N.5    Schoner, B.E.6
  • 14
    • 77952836412 scopus 로고    scopus 로고
    • Manipulation of thiocillin variants by prepeptide gene replacement: Structure, conformation, and activity of heterocycle substitution mutants
    • A.A. Bowers, M.G. Acker, A. Koglin, and C.T. Walsh Manipulation of thiocillin variants by prepeptide gene replacement: Structure, conformation, and activity of heterocycle substitution mutants Journal of the American Chemical Society 132 2010 7519 7527
    • (2010) Journal of the American Chemical Society , vol.132 , pp. 7519-7527
    • Bowers, A.A.1    Acker, M.G.2    Koglin, A.3    Walsh, C.T.4
  • 15
    • 77956244429 scopus 로고    scopus 로고
    • Genetic interception and structural characterization of thiopeptide cyclization precursors from Bacillus cereus
    • A.A. Bowers, C.T. Walsh, and M.G. Acker Genetic interception and structural characterization of thiopeptide cyclization precursors from Bacillus cereus Journal of the American Chemical Society 132 2010 12182 12184
    • (2010) Journal of the American Chemical Society , vol.132 , pp. 12182-12184
    • Bowers, A.A.1    Walsh, C.T.2    Acker, M.G.3
  • 17
    • 0036301166 scopus 로고    scopus 로고
    • Initiation factor IF2, thiostrepton and micrococcin prevent the binding of elongation factor G to the Escherichia coli ribosome
    • DOI 10.1016/S0022-2836(02)00235-8
    • D.M. Cameron, J. Thompson, P.E. March, and A.E. Dahlberg Initiation factor IF2, thiostrepton and micrococcin prevent the binding of elongation factor G to the Escherichia coli ribosome Journal of Molecular Biology 319 2002 27 35 (Pubitemid 34729484)
    • (2002) Journal of Molecular Biology , vol.319 , Issue.1 , pp. 27-35
    • Cameron, D.M.1    Thompson, J.2    March, P.E.3    Dahlberg, A.E.4
  • 19
    • 0343238149 scopus 로고    scopus 로고
    • 1 is secreted by the food-borne bacterium Staphylococcus equorum WS 2733 and inhibits Listeria monocytogenes on soft cheese
    • DOI 10.1128/AEM.66.6.2378-2384.2000
    • 1 is secreted by the food-borne bacterium Staphylococcus equorum WS 2733 and inhibits Listeria monocytogenes on soft cheese Applied and Environmental Microbiology 66 2000 2378 2384 (Pubitemid 30353941)
    • (2000) Applied and Environmental Microbiology , vol.66 , Issue.6 , pp. 2378-2384
    • Carnio, M.C.1    Holtzel, A.2    Rudolf, M.3    Henle, T.4    Jung, G.5    Scherer, S.6
  • 20
    • 1642305331 scopus 로고
    • Zootechnical evaluation of a new antibiotic, nosiheptide, using swine
    • M. Casteels, H. Bekaert, and F.X. Buysse Zootechnical evaluation of a new antibiotic, nosiheptide, using swine Revue de l'Agriculture (Brussels) 33 1980 1069 1078
    • (1980) Revue de l'Agriculture (Brussels) , vol.33 , pp. 1069-1078
    • Casteels, M.1    Bekaert, H.2    Buysse, F.X.3
  • 21
    • 14844340728 scopus 로고    scopus 로고
    • Biosynthesis and mode of action of lantibiotics
    • DOI 10.1021/cr030105v
    • C. Chatterjee, M. Paul, L. Xie, and W.A. van der Donk Biosynthesis and mode of action of lantibiotics Chemical Reviews 105 2005 633 683 (Pubitemid 40356090)
    • (2005) Chemical Reviews , vol.105 , Issue.2 , pp. 633-683
    • Chatterjee, C.1    Paul, M.2    Xie, L.3    Van Der Donk, W.A.4
  • 22
    • 0033180232 scopus 로고    scopus 로고
    • Antibiotic inhibitors of organellar protein synthesis in Plasmodium falciparum
    • B. Clough, K. Rangachari, M. Strath, P.R. Preiser, and R.J.M. Wilson Antibiotic inhibitors of organellar protein synthesis in Plasmodium falciparum Protist 150 1999 189 195 (Pubitemid 29442459)
    • (1999) Protist , vol.150 , Issue.2 , pp. 189-195
    • Clough, B.1    Rangachari, K.2    Strath, M.3    Preiser, P.R.4    Wilson, R.J.M.5
  • 23
    • 0030915683 scopus 로고    scopus 로고
    • Thiostrepton binds to malarial plastid rRNA
    • DOI 10.1016/S0014-5793(97)00241-X, PII S001457939700241X
    • B. Clough, M. Strath, P. Preiser, P. Denny, and I.R. Wilson Thiostrepton binds to malarial plastid rRNA FEBS Letters 406 1997 123 125 (Pubitemid 27156972)
    • (1997) FEBS Letters , vol.406 , Issue.1-2 , pp. 123-125
    • Clough, B.1    Strath, M.2    Preiser, P.3    Denny, P.4    Wilson, I.R.5
  • 26
    • 77953547312 scopus 로고    scopus 로고
    • Moving posttranslational modifications forward to biosynthesize the glycosylated thiopeptide nocathiacin i in Nocardia sp. ATCC 202099
    • Y. Ding, Y. Yu, H. Pan, H. Guo, Y. Li, and W. Liu Moving posttranslational modifications forward to biosynthesize the glycosylated thiopeptide nocathiacin I in Nocardia sp. ATCC 202099 Molecular BioSystems 6 2010 1180 1185
    • (2010) Molecular BioSystems , vol.6 , pp. 1180-1185
    • Ding, Y.1    Yu, Y.2    Pan, H.3    Guo, H.4    Li, Y.5    Liu, W.6
  • 27
    • 0024349978 scopus 로고
    • Antibiotic interactions at the GTPase-associated centre within Escherichia coli 23S rRNA
    • J. Egebjerg, S. Douthwaite, and R.A. Garrett Antibiotic interactions at the GTPase-associated centre within Escherichia coli 23S rRNA The EMBO Journal 8 1989 607 611 (Pubitemid 19274981)
    • (1989) EMBO Journal , vol.8 , Issue.2 , pp. 607-611
    • Egebjerg, J.1    Douthwaite, S.2    Garrett, R.A.3
  • 28
    • 78149447364 scopus 로고    scopus 로고
    • Isolation and characterization of the gene cluster for biosynthesis of the thiopeptide antibiotic TP-1161
    • K. Engelhardt, K.F. Degnes, and S.B. Zotchev Isolation and characterization of the gene cluster for biosynthesis of the thiopeptide antibiotic TP-1161 Applied and Environmental Microbiology 76 2010 7093 7101
    • (2010) Applied and Environmental Microbiology , vol.76 , pp. 7093-7101
    • Engelhardt, K.1    Degnes, K.F.2    Zotchev, S.B.3
  • 29
    • 34247136117 scopus 로고
    • A new antibiotic of bacterial origin
    • A.T. Fuller A new antibiotic of bacterial origin Nature 175 1955 722
    • (1955) Nature , vol.175 , pp. 722
    • Fuller, A.T.1
  • 30
    • 0022351923 scopus 로고
    • Positive selection procedure for entrapment of insertion sequence elements in gram-negative bacteria
    • P. Gay, D. Le Coq, M. Steinmetz, T. Berkelman, and C.I. Kado Positive selection procedure for entrapment of insertion sequence elements in Gram-negative bacteria Journal of Bacteriology 164 1985 918 921 (Pubitemid 16191873)
    • (1985) Journal of Bacteriology , vol.164 , Issue.2 , pp. 918-921
    • Gay, P.1    Le Coq, D.2    Steinmetz, M.3
  • 31
    • 0037452723 scopus 로고    scopus 로고
    • PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin
    • DOI 10.1073/pnas.0337542100
    • B. Gust, G.L. Challis, K. Fowler, T. Kieser, and K.F. Chater PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin Proceedings of the National Academy of Sciences of the United States of America 100 2003 1541 1546 (Pubitemid 36254483)
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , Issue.4 , pp. 1541-1546
    • Gust, B.1    Challis, G.L.2    Fowler, K.3    Kieser, T.4    Chater, K.F.5
  • 32
    • 41549163979 scopus 로고    scopus 로고
    • Translational Regulation via L11: Molecular Switches on the Ribosome Turned On and Off by Thiostrepton and Micrococcin
    • DOI 10.1016/j.molcel.2008.01.009, PII S1097276508000440
    • J.M. Harms, D.N. Wilson, F. Schluenzen, S.R. Connell, T. Stachelhaus, and Z. Zaborowska Translational regulation via L11: Molecular switches on the ribosome turned on and off by thiostrepton and micrococcin Molecular Cell 30 2008 26 38 (Pubitemid 351470144)
    • (2008) Molecular Cell , vol.30 , Issue.1 , pp. 26-38
    • Harms, J.M.1    Wilson, D.N.2    Schluenzen, F.3    Connell, S.R.4    Stachelhaus, T.5    Zaborowska, Z.6    Spahn, C.M.T.7    Fucini, P.8
  • 33
    • 0034635128 scopus 로고    scopus 로고
    • Structure of an EF-Tu complex with a thiazolyl peptide antibiotic determined at 2.35 A resolution: Atomic basis for GE2270A inhibition of EF- Tu
    • DOI 10.1021/bi9913597
    • S.E. Heffron, and F. Jurnak Structure of an EF-Tu complex with a thiazolyl peptide antibiotic determined at 2.35 Å resolution: Atomic basis for GE2270A inhibition of EF-Tu Biochemistry 39 2000 37 45 (Pubitemid 30033317)
    • (2000) Biochemistry , vol.39 , Issue.1 , pp. 37-45
    • Heffron, S.E.1    Jurnak, F.2
  • 34
    • 80052111561 scopus 로고    scopus 로고
    • The transcription factor FOXM1 is a cellular target of the natural product thiostrepton
    • N.S. Hegde, D.A. Sanders, R. Rodriguez, and S. Balasubramanian The transcription factor FOXM1 is a cellular target of the natural product thiostrepton Nature Chemistry 3 2011 725 731
    • (2011) Nature Chemistry , vol.3 , pp. 725-731
    • Hegde, N.S.1    Sanders, D.A.2    Rodriguez, R.3    Balasubramanian, S.4
  • 38
    • 67749113468 scopus 로고    scopus 로고
    • Thiostrepton biosynthesis: Prototype for a new family of bacteriocins
    • W.L. Kelly, L. Pan, and C. Li Thiostrepton biosynthesis: Prototype for a new family of bacteriocins Journal of the American Chemical Society 131 2009 4327 4334
    • (2009) Journal of the American Chemical Society , vol.131 , pp. 4327-4334
    • Kelly, W.L.1    Pan, L.2    Li, C.3
  • 41
    • 0042415065 scopus 로고    scopus 로고
    • Structural basis for contrasting activities of ribosome binding thiazole antibiotics
    • DOI 10.1016/S1074-5521(03)00173-X
    • G. Lentzen, R. Klinck, N. Matassova, F. Aboul-ela, and A.I.H. Murchie Structural basis for contrasting activities of ribosome binding thiazole antibiotics Chemistry & Biology 10 2003 769 778 (Pubitemid 37089852)
    • (2003) Chemistry and Biology , vol.10 , Issue.8 , pp. 769-778
    • Lentzen, G.1    Klinck, R.2    Matassova, N.3    Aboul-Ela, F.4    Murchie, A.I.H.5
  • 42
    • 76249088902 scopus 로고    scopus 로고
    • Recent advances in thiopeptide antibiotic biosynthesis
    • C. Li, and W.L. Kelly Recent advances in thiopeptide antibiotic biosynthesis Natural Product Reports 27 2010 153 164
    • (2010) Natural Product Reports , vol.27 , pp. 153-164
    • Li, C.1    Kelly, W.L.2
  • 44
    • 0029923954 scopus 로고    scopus 로고
    • From peptide precursors to oxazole and thiazole-containing peptide antibiotics: Microcin B17 synthase
    • DOI 10.1126/science.274.5290.1188
    • Y.M. Li, J.C. Milne, L.L. Madison, R. Kolter, and C.T. Walsh From peptide precursors to oxazole and thiazole-containing peptide antibiotics: Microcin B17 synthase Science 274 1996 1188 1193 (Pubitemid 26389284)
    • (1996) Science , vol.274 , Issue.5290 , pp. 1188-1193
    • Li, Y.-M.1    Milne, J.C.2    Madison, L.L.3    Kolter, R.4    Walsh, C.T.5
  • 45
    • 78650115990 scopus 로고    scopus 로고
    • Heterologous production of thiostrepton A and biosynthetic engineering of thiostrepton analogs
    • C. Li, F. Zhang, and W.L. Kelly Heterologous production of thiostrepton A and biosynthetic engineering of thiostrepton analogs Molecular BioSystems 7 2011 82 90
    • (2011) Molecular BioSystems , vol.7 , pp. 82-90
    • Li, C.1    Zhang, F.2    Kelly, W.L.3
  • 46
    • 83455261993 scopus 로고    scopus 로고
    • Mutagenesis of the thiostrepton precursor peptide at Thr7 impacts both biosynthesis and function
    • C. Li, F. Zhang, and W.L. Kelly Mutagenesis of the thiostrepton precursor peptide at Thr7 impacts both biosynthesis and function Chemical Communications 48 2012 558 560
    • (2012) Chemical Communications , vol.48 , pp. 558-560
    • Li, C.1    Zhang, F.2    Kelly, W.L.3
  • 47
    • 60549109637 scopus 로고    scopus 로고
    • Thiopeptide biosynthesis featuring ribosomally synthesized precursor peptides and conserved posttranslational modifications
    • R. Liao, L. Duan, C. Lei, H. Pan, Y. Ding, and Q. Zhang Thiopeptide biosynthesis featuring ribosomally synthesized precursor peptides and conserved posttranslational modifications Chemistry & Biology 16 2009 141 147
    • (2009) Chemistry & Biology , vol.16 , pp. 141-147
    • Liao, R.1    Duan, L.2    Lei, C.3    Pan, H.4    Ding, Y.5    Zhang, Q.6
  • 48
    • 79952262668 scopus 로고    scopus 로고
    • Thiostrepton maturation involving a deesterification-amidation way to process the C-terminally methylated peptide backbone
    • R. Liao, and W. Liu Thiostrepton maturation involving a deesterification-amidation way to process the C-terminally methylated peptide backbone Journal of the American Chemical Society 133 2011 2852 2855
    • (2011) Journal of the American Chemical Society , vol.133 , pp. 2852-2855
    • Liao, R.1    Liu, W.2
  • 49
    • 0031030313 scopus 로고    scopus 로고
    • Inhibition of Plasmodium falciparum protein synthesis. Targeting the plastid-like organelle with thiostrepton
    • DOI 10.1074/jbc.272.4.2046
    • G.A. McConkey, M.J. Rogers, and T.F. McCutchan Inhibition of Plasmodium falciparum protein synthesis. Targeting the plastid-like organelle with thiostrepton The Journal of Biological Chemistry 272 1997 2046 2049 (Pubitemid 27058476)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.4 , pp. 2046-2049
    • McConkey, G.A.1    Rogers, M.J.2    McCutchan, T.F.3
  • 50
  • 53
    • 72449161144 scopus 로고    scopus 로고
    • Nocardithiocin, a novel thiopeptide antibiotic, produced by pathogenic Nocardia pseudobrasiliensis IFM 0757
    • A. Mukai, T. Fukai, Y. Hoshino, K. Yazawa, K. Harada, and Y. Mikami Nocardithiocin, a novel thiopeptide antibiotic, produced by pathogenic Nocardia pseudobrasiliensis IFM 0757 The Journal of Antibiotics 62 2009 613 619
    • (2009) The Journal of Antibiotics , vol.62 , pp. 613-619
    • Mukai, A.1    Fukai, T.2    Hoshino, Y.3    Yazawa, K.4    Harada, K.5    Mikami, Y.6
  • 54
    • 0024341196 scopus 로고
    • A vector system with temperature-sensitive replication for gene disruption and mutational cloning in streptomycetes
    • DOI 10.1007/BF00259605
    • G. Muth, B. Nussbaumer, W. Wohlleben, and A. Pühler A vector system with temperature-sensitive replication for gene disruption and mutational cloning in Streptomycetes Molecular & General Genetics 219 1989 341 348 (Pubitemid 20009286)
    • (1989) Molecular and General Genetics , vol.219 , Issue.3 , pp. 341-348
    • Muth, G.1    Nussbaumer, B.2    Wohlleben, W.3    Puhler, A.4
  • 55
    • 77953139013 scopus 로고    scopus 로고
    • Semi-synthetic analogues of thiostrepton delimit the critical nature of tail region modifications in the control of protein biosynthesis and antibacterial activity
    • C.L. Myers, P.C. Hang, G. Ng, J. Yuen, and J.F. Honek Semi-synthetic analogues of thiostrepton delimit the critical nature of tail region modifications in the control of protein biosynthesis and antibacterial activity Bioorganic & Medicinal Chemistry 18 2010 4231 4237
    • (2010) Bioorganic & Medicinal Chemistry , vol.18 , pp. 4231-4237
    • Myers, C.L.1    Hang, P.C.2    Ng, G.3    Yuen, J.4    Honek, J.F.5
  • 56
    • 0037300530 scopus 로고    scopus 로고
    • YM-266183 and YM-266184, novel thiopeptide antibiotics produced by Bacillus cereus isolated from a marine sponge. I. Taxonomy, fermentation, Isolation, physico-chemical properties and biological properties
    • K. Nagai, K. Kamigiri, N. Arao, K. Suzumura, Y. Kawano, and M. Yamaoka YM-266183 and YM-266184, novel thiopeptide antibiotics produced by Bacillus cereus isolated from a marine sponge. I. Taxonomy, fermentation, isolation, physico-chemical properties and biological properties The Journal of Antibiotics 56 2003 123 128 (Pubitemid 36372794)
    • (2003) Journal of Antibiotics , vol.56 , Issue.2 , pp. 123-128
    • Nagai, K.1    Kamigiri, K.2    Arao, N.3    Suzumura, K.-I.4    Kawano, Y.5    Yamaoka, M.6    Zhang, H.7    Watanabe, M.8    Suzuki, K.9
  • 60
    • 23744439852 scopus 로고    scopus 로고
    • Total synthesis of thiostrepton. Assembly of key building blocks and completion of the synthesis
    • DOI 10.1021/ja052934z
    • K.C. Nicolaou, M. Zak, B.S. Safina, A.A. Estrada, S.H. Lee, and M. Nevalainen Total synthesis of thiostrepton. Assembly of key building blocks and completion of the synthesis Journal of the American Chemical Society 127 2005 11176 11183 (Pubitemid 41129894)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.31 , pp. 11176-11183
    • Nicolaou, K.C.1    Zak, M.2    Safina, B.S.3    Estrada, A.A.4    Lee, S.H.5    Nevalainen, M.6
  • 61
    • 79951993444 scopus 로고    scopus 로고
    • Thiazole antibiotic thiostrepton synergize with bortezomib to induce apoptosis in cancer cells
    • B. Pandit, and A.L. Gartel Thiazole antibiotic thiostrepton synergize with bortezomib to induce apoptosis in cancer cells PloS One 6 2011 e17110
    • (2011) PloS One , vol.6 , pp. 17110
    • Pandit, B.1    Gartel, A.L.2
  • 62
    • 33744951325 scopus 로고    scopus 로고
    • Structural basis of the action of pulvomycin and GE2270 A on elongation factor Tu
    • DOI 10.1021/bi0525122
    • A. Parmeggiani, I.M. Krab, S. Okamura, R.C. Nielsen, J. Nyborg, and P. Nissen Structural basis of the action of pulvomycin and GE2270 A on elongation factor Tu Biochemistry 45 2006 6846 6857 (Pubitemid 43856670)
    • (2006) Biochemistry , vol.45 , Issue.22 , pp. 6846-6857
    • Parmeggiani, A.1    Krab, I.M.2    Okamura, S.3    Nielsen, R.C.4    Nyborg, J.5    Nissen, P.6
  • 63
    • 0032548821 scopus 로고    scopus 로고
    • The antibiotic thiostrepton inhibits a functional transition within protein L11 at the ribosomal GTPase centre
    • DOI 10.1006/jmbi.1997.1541
    • B.T. Porse, I. Leviev, A.S. Mankin, and R.A. Garrett The antibiotic thiostrepton inhibits a functional transition within protein L11 at the ribosomal GTPase centre Journal of Molecular Biology 276 1998 391 404 (Pubitemid 28085328)
    • (1998) Journal of Molecular Biology , vol.276 , Issue.2 , pp. 391-404
    • Porse, B.T.1    Leviev, I.2    Mankin, A.S.3    Garrett, R.A.4
  • 64
    • 0017622981 scopus 로고
    • Structure of nosiheptide, a polythiazole-containing antibiotic
    • T. Prange, A. Ducruix, C. Pascard, and J. Lunel Structure of nosiheptide, a polythiazole-containing antibiotic Nature 265 1977 189 190
    • (1977) Nature , vol.265 , pp. 189-190
    • Prange, T.1    Ducruix, A.2    Pascard, C.3    Lunel, J.4
  • 65
    • 17344375809 scopus 로고    scopus 로고
    • Studies on the biosynthesis of thiostrepton: 4-(1- hydroxyethyl) quinoline-2-carboxylate as a free intermediate on the pathway to the quinaldic acid moiety
    • DOI 10.1016/0968-0896(96)00126-5
    • N.D. Priestley, T.M. Smith, P.R. Shipley, and H.G. Floss Studies on the biosynthesis of thiostrepton: 4-(1-hydroxyethyl)quinoline-2-carboxylate as a free intermediate on the pathway to the quinaldic acid moiety Bioorganic & Medicinal Chemistry 4 1996 1135 1147 (Pubitemid 27377814)
    • (1996) Bioorganic and Medicinal Chemistry , vol.4 , Issue.7 , pp. 1135-1147
    • Priestley, N.D.1    Smith, T.M.2    Shipley, P.R.3    Floss, H.G.4
  • 67
    • 33750338042 scopus 로고    scopus 로고
    • Identification of a chemical inhibitor of the oncogenic transcription factor forkhead box M1
    • DOI 10.1158/0008-5472.CAN-06-1576
    • S.K. Radhakrishnan, U.G. Bhat, D.E. Hughes, I.-C. Wang, R.H. Costa, and A.L. Gartel Identification of a chemical inhibitor of the oncogenic transcription factor forkhead box M1 Cancer Research 66 2006 9731 9735 (Pubitemid 44623674)
    • (2006) Cancer Research , vol.66 , Issue.19 , pp. 9731-9735
    • Radhakrishnan, S.K.1    Bhat, U.G.2    Hughes, D.E.3    Wang, I.-C.4    Costa, R.H.5    Gartel, A.L.6
  • 68
    • 0030791711 scopus 로고    scopus 로고
    • Interaction of thiostrepton with an RNA fragment derived from the plastid-encoded ribosomal RNA of the malaria parasite
    • M.J. Rogers, Y.V. Bukhman, T.F. McCutchan, and D.E. Draper Interaction of thiostrepton with an RNA fragment derived from the plastid-encoded ribosomal RNA of the malaria parasite RNA 3 1997 815 820 (Pubitemid 27332732)
    • (1997) RNA , vol.3 , Issue.8 , pp. 815-820
    • Rogers, M.J.1    Bukhman, Y.V.2    McCutchan, T.F.3    Draper, D.E.4
  • 69
    • 0031917769 scopus 로고    scopus 로고
    • The antibiotic micrococcin is a potent inhibitor of growth and protein synthesis in the malaria parasite
    • M.J. Rogers, E. Cundliffe, and T.F. McCutchan The antibiotic micrococcin is a potent inhibitor of growth and protein synthesis in the malaria parasite Antimicrobial Agents and Chemotherapy 42 1998 715 716 (Pubitemid 28114837)
    • (1998) Antimicrobial Agents and Chemotherapy , vol.42 , Issue.3 , pp. 715-716
    • Rogers, M.J.1    Cundliffe, E.2    McCutchan, T.F.3
  • 71
    • 0029061955 scopus 로고
    • An improved system for gene replacement and xylE fusion analysis in Pseudomonas aeruginosa
    • H.P. Schweizer, and T.T. Hoang An improved system for gene replacement and xylE fusion analysis in Pseudomonas aeruginosa Gene 158 1995 15 22
    • (1995) Gene , vol.158 , pp. 15-22
    • Schweizer, H.P.1    Hoang, T.T.2
  • 72
    • 0017078825 scopus 로고
    • Isolation of three new antibiotics, thiocillins I, II and III, related to micrococcin P. Studies on antibiotics from the genus Bacillus. VIII
    • J. Shoji, H. Hinoo, Y. Wakisaka, K. Koizumi, M. Mayama, and S. Matsura Isolation of three new antibiotics, thiocillins I, II and III, related to micrococcin P. Studies on antibiotics from the genus Bacillus. VIII The Journal of Antibiotics 29 1976 366 374
    • (1976) The Journal of Antibiotics , vol.29 , pp. 366-374
    • Shoji, J.1    Hinoo, H.2    Wakisaka, Y.3    Koizumi, K.4    Mayama, M.5    Matsura, S.6
  • 73
    • 71149087158 scopus 로고    scopus 로고
    • Identification of distinct thiopeptide-antibiotic precursor lead compounds using translation machinery assays
    • A.L. Starosta, H. Qin, A. Mikolajka, G.Y. Leung, K. Schwinghammer, and K.C. Nicolaou Identification of distinct thiopeptide-antibiotic precursor lead compounds using translation machinery assays Chemistry & Biology 16 2009 1087 1096
    • (2009) Chemistry & Biology , vol.16 , pp. 1087-1096
    • Starosta, A.L.1    Qin, H.2    Mikolajka, A.3    Leung, G.Y.4    Schwinghammer, K.5    Nicolaou, K.C.6
  • 74
    • 0007564038 scopus 로고
    • Micrococcin, an antibacterial substance formed by a strain of Micrococcus
    • T.L. Su Micrococcin, an antibacterial substance formed by a strain of Micrococcus British Journal of Experimental Pathology 29 1948 473 481
    • (1948) British Journal of Experimental Pathology , vol.29 , pp. 473-481
    • Su, T.L.1
  • 75
    • 0018497597 scopus 로고
    • Binding of thiostrepton to a complex of 23-S rRNA with ribosomal protein L11
    • J. Thompson, E. Cundliffe, and M. Stark Binding of thiostrepton to a complex of 23-S rRNA with ribosomal protein L11 European Journal of Biochemistry 98 1979 261 265
    • (1979) European Journal of Biochemistry , vol.98 , pp. 261-265
    • Thompson, J.1    Cundliffe, E.2    Stark, M.3
  • 76
    • 0017657017 scopus 로고
    • Streptomyces laurentii, a new species producing thiostrepton
    • W.H. Trejo, L.D. Dean, J. Pluscec, E. Meyers, and W.E. Brown Streptomyces laurentii, a new species producing thiostrepton The Journal of Antibiotics 30 1977 639 643 (Pubitemid 8185891)
    • (1977) Journal of Antibiotics , vol.30 , Issue.8 , pp. 639-643
    • Trejo, W.H.1    Dean, L.D.2    Pluscec, J.3
  • 77
    • 33750373154 scopus 로고    scopus 로고
    • Elaboration of an electroporation protocol for Bacillus cereus ATCC 14579
    • DOI 10.1016/j.mimet.2006.05.005, PII S016770120600159X
    • N. Turgeon, C. Laflamme, J. Ho, and C. Duchaine Elaboration of an electroporation protocol for Bacillus cereus ATCC 14579 Journal of Microbiological Methods 67 2006 543 548 (Pubitemid 44633473)
    • (2006) Journal of Microbiological Methods , vol.67 , Issue.3 , pp. 543-548
    • Turgeon, N.1    Laflamme, C.2    Ho, J.3    Duchaine, C.4
  • 78
    • 77049246278 scopus 로고
    • Thiostrepton, a new antibiotic. II. Isolation and chemical characterization
    • J. Vandeputte, and J.D. Dutcher Thiostrepton, a new antibiotic. II. Isolation and chemical characterization Antibiotics Annual 3 1955 560 561
    • (1955) Antibiotics Annual , vol.3 , pp. 560-561
    • Vandeputte, J.1    Dutcher, J.D.2
  • 79
    • 77953117821 scopus 로고    scopus 로고
    • Identification and analysis of the biosynthetic gene cluster encoding the thiopeptide antibiotic cyclothiazomycin in Streptomyces hygroscopicus 10-22
    • J. Wang, Y. Yu, K. Tang, W. Liu, X. He, and X. Huang Identification and analysis of the biosynthetic gene cluster encoding the thiopeptide antibiotic cyclothiazomycin in Streptomyces hygroscopicus 10-22 Applied and Environmental Microbiology 76 2010 2335 2344
    • (2010) Applied and Environmental Microbiology , vol.76 , pp. 2335-2344
    • Wang, J.1    Yu, Y.2    Tang, K.3    Liu, W.4    He, X.5    Huang, X.6
  • 82
    • 80051981726 scopus 로고    scopus 로고
    • Identification of the thiazolyl peptide GE37468 gene cluster from Streptomyces ATCC 55365 and heterologous expression in Streptomyces lividans
    • T.S. Young, and C.T. Walsh Identification of the thiazolyl peptide GE37468 gene cluster from Streptomyces ATCC 55365 and heterologous expression in Streptomyces lividans Proceedings of the National Academy of Sciences of the United States of America 108 2011 13053 13058
    • (2011) Proceedings of the National Academy of Sciences of the United States of America , vol.108 , pp. 13053-13058
    • Young, T.S.1    Walsh, C.T.2
  • 83
    • 70350170631 scopus 로고    scopus 로고
    • Nosiheptide biosynthesis featuring a unique indole side ring formation on the characteristic thiopeptide framework
    • Y. Yu, L. Duan, Q. Zhang, R. Liao, Y. Ding, and H. Pan Nosiheptide biosynthesis featuring a unique indole side ring formation on the characteristic thiopeptide framework ACS Chemical Biology 4 2009 855 864
    • (2009) ACS Chemical Biology , vol.4 , pp. 855-864
    • Yu, Y.1    Duan, L.2    Zhang, Q.3    Liao, R.4    Ding, Y.5    Pan, H.6
  • 84
    • 78649262383 scopus 로고    scopus 로고
    • NosA catalyzing carboxyl-terminal amide formation in nosiheptide maturation via an enamine dealkylation on the serine-extended precursor peptide
    • Y. Yu, H. Guo, Q. Zhang, L. Duan, Y. Ding, and R. Liao NosA catalyzing carboxyl-terminal amide formation in nosiheptide maturation via an enamine dealkylation on the serine-extended precursor peptide Journal of the American Chemical Society 132 2010 16324 16326
    • (2010) Journal of the American Chemical Society , vol.132 , pp. 16324-16326
    • Yu, Y.1    Guo, H.2    Zhang, Q.3    Duan, L.4    Ding, Y.5    Liao, R.6
  • 85
    • 79951845926 scopus 로고    scopus 로고
    • Radical-mediated enzymatic carbon chain fragmentation-recombination
    • Q. Zhang, Y. Li, D. Chen, Y. Yu, L. Duan, and B. Shen Radical-mediated enzymatic carbon chain fragmentation-recombination Nature Chemical Biology 7 2011 154 160
    • (2011) Nature Chemical Biology , vol.7 , pp. 154-160
    • Zhang, Q.1    Li, Y.2    Chen, D.3    Yu, Y.4    Duan, L.5    Shen, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.