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Volumn 12, Issue 5, 2014, Pages 2668-2699

Biosynthetic modularity rules in the bisintercalator family of antitumor compounds

Author keywords

3 hydroxy quinaldic acid; Actinomycete; Antibiotic; Antitumor; Antiviral; Bisintercalator; Depsipeptide; Non ribosomal peptide; Quinoxaline 2 carboxilic acid; Thiodepsipeptide

Indexed keywords

AMINO ACID; ANTINEOPLASTIC AGENT; ECHINOMYCIN; INTERCALATING AGENT; QUINOMYCIN; SW 163; THIOCORALINE; TRIOSTIN; UNCLASSIFIED DRUG; ANTINEOPLASTIC ANTIBIOTIC;

EID: 84901412720     PISSN: None     EISSN: 16603397     Source Type: Journal    
DOI: 10.3390/md12052668     Document Type: Review
Times cited : (17)

References (140)
  • 3
    • 0028953708 scopus 로고
    • Solution structure of a quinomycin bisintercalator-DNA complex
    • Chen, H.; Patel, D.J. Solution structure of a quinomycin bisintercalator-DNA complex. J. Mol. Biol. 1995, 246, 164-179.
    • (1995) J. Mol. Biol. , vol.246 , pp. 164-179
    • Chen, H.1    Patel, D.J.2
  • 4
    • 27744488780 scopus 로고    scopus 로고
    • Molecular signaling cascade in DNA bisintercalator, echinomycin-induced apoptosis of HT-29 cells: Evidence of the apoptotic process via activation of the cytochrome c-ERK-caspase-3 pathway
    • Park, J.Y.; Ryang, Y.S.; Shim, K.Y.; Lee, J.I.; Kim, H.S.; Kim, Y.H.; Kim, S.K. Molecular signaling cascade in DNA bisintercalator, echinomycin-induced apoptosis of HT-29 cells: Evidence of the apoptotic process via activation of the cytochrome c-ERK-caspase-3 pathway. Int. J. Biochem. Cell Biol. 2006, 38, 244-254.
    • (2006) Int. J. Biochem. Cell Biol. , vol.38 , pp. 244-254
    • Park, J.Y.1    Ryang, Y.S.2    Shim, K.Y.3    Lee, J.I.4    Kim, H.S.5    Kim, Y.H.6    Kim, S.K.7
  • 6
    • 9044241840 scopus 로고
    • Studies on quinoxaline antibiotics. II. Isolation and properties of quinomycins A, B and C
    • Yoshida, T.; Katagiri, K.; Yokozawa, S. Studies on quinoxaline antibiotics. II. Isolation and properties of quinomycins A, B and C. J. Antibiot. 1961, 14, 330-334.
    • (1961) J. Antibiot. , vol.14 , pp. 330-334
    • Yoshida, T.1    Katagiri, K.2    Yokozawa, S.3
  • 8
    • 50249171697 scopus 로고    scopus 로고
    • Insecticidal action of Quinomycin A from Streptomyces sp. KN-0647, isolated from a forest soil
    • Liu, H.; Qin, S.; Wang, Y.; Li, W.; Zhang, J. Insecticidal action of Quinomycin A from Streptomyces sp. KN-0647, isolated from a forest soil. World J. Microbiol. Biotechnol. 2008, 24, 2243-2248.
    • (2008) World J. Microbiol. Biotechnol. , vol.24 , pp. 2243-2248
    • Liu, H.1    Qin, S.2    Wang, Y.3    Li, W.4    Zhang, J.5
  • 9
    • 84874321692 scopus 로고    scopus 로고
    • In vitro characterization of echinomycin biosynthesis: Formation and hydroxylation of L-tryptophanyl-S-enzyme and oxidation of (2S,3S) β-hydroxytryptophan
    • Zhang, C.; Kong, L.; Liu, Q.; Lei, X.; Zhu, T.; Yin, J.; Lin, B.; Deng, Z.; You, D. In vitro characterization of echinomycin biosynthesis: formation and hydroxylation of L-tryptophanyl-S-enzyme and oxidation of (2S,3S) β-hydroxytryptophan. PLoS One 2013, 8, e56772.
    • (2013) PLoS One , vol.8
    • Zhang, C.1    Kong, L.2    Liu, Q.3    Lei, X.4    Zhu, T.5    Yin, J.6    Lin, B.7    Deng, Z.8    You, D.9
  • 10
    • 0023912757 scopus 로고
    • Frequent loss and restoration of antibiotic production by Streptomyces lasaliensis
    • Kinashi, H.; Otten, S.L.; Duncan, J.S.; Hutchinson, C.R. Frequent loss and restoration of antibiotic production by Streptomyces lasaliensis. J. Antibiot. 1988, 41, 624-637.
    • (1988) J. Antibiot. , vol.41 , pp. 624-637
    • Kinashi, H.1    Otten, S.L.2    Duncan, J.S.3    Hutchinson, C.R.4
  • 11
    • 79251638546 scopus 로고    scopus 로고
    • Giant linear plasmids in Streptomyces: A treasure trove of antibiotic biosynthetic clusters
    • Kinashi, H. Giant linear plasmids in Streptomyces: A treasure trove of antibiotic biosynthetic clusters. J. Antibiot. 2011, 64, 19-25.
    • (2011) J. Antibiot. , vol.64 , pp. 19-25
    • Kinashi, H.1
  • 12
    • 33846899787 scopus 로고    scopus 로고
    • Bisintercalator natural products with potential therapeutic applications: Isolation, structure determination, synthetic and biological studies
    • DOI 10.1039/b516347c
    • Dawson, S.; Malkinson, J.P.; Paumier, D.; Searcey, M. Bisintercalator natural products with potential therapeutic applications: Isolation, structure determination, synthetic and biological studies. Nat. Prod. Rep. 2007, 24, 109-126. (Pubitemid 46238591)
    • (2007) Natural Product Reports , vol.24 , Issue.1 , pp. 109-126
    • Dawson, S.1    Malkinson, J.P.2    Paumier, D.3    Searcey, M.4
  • 13
    • 77954653156 scopus 로고    scopus 로고
    • Recent developments in bisintercalator natural products
    • Zolova, O.E.; Mady, A.S.; Garneau-Tsodikova, S. Recent developments in bisintercalator natural products. Biopolymers 2010, 93, 777-790.
    • (2010) Biopolymers , vol.93 , pp. 777-790
    • Zolova, O.E.1    Mady, A.S.2    Garneau-Tsodikova, S.3
  • 14
    • 0021074096 scopus 로고
    • Conversion of triostins to quinomycins by protoplasts of Streptomyces echinatus
    • Cornish, A.; Waring, M.J.; Nolan, R.D. Conversion of triostins to quinomycins by protoplasts of Streptomyces echinatus. J. Antibiot. 1983, 36, 1664-1670. (Pubitemid 14182427)
    • (1983) Journal of Antibiotics , vol.36 , Issue.12 , pp. 1664-1670
    • Cornish, A.1    Waring, M.J.2    Nolan, R.D.3
  • 15
    • 32344437742 scopus 로고    scopus 로고
    • Deciphering the biosynthesis pathway of the antitumor thiocoraline from a marine actinomycete and its expression in two Streptomyces species
    • Lombó, F.; Velasco, A.; Castro, A.; de la Calle, F.; Braña, A.F.; Sánchez-Puelles, J.M.; Méndez, C.; Salas, J.A. Deciphering the biosynthesis pathway of the antitumor thiocoraline from a marine actinomycete and its expression in two Streptomyces species. Chembiochem 2006, 7, 366-376.
    • (2006) Chembiochem , vol.7 , pp. 366-376
    • Lombó, F.1    Velasco, A.2    Castro, A.3    De La Calle, F.4    Braña, A.F.5    Sánchez-Puelles, J.M.6    Méndez, C.7    Salas, J.A.8
  • 16
    • 84877279350 scopus 로고    scopus 로고
    • Platforms for antibiotic discovery
    • Lewis, K. Platforms for antibiotic discovery. Nat. Rev. Drug Discov. 2013, 12, 371-387.
    • (2013) Nat. Rev. Drug Discov. , vol.12 , pp. 371-387
    • Lewis, K.1
  • 18
    • 0030814840 scopus 로고    scopus 로고
    • Thiocoraline, a new depsipeptide with antitumor activity produced by a marine Micromonospora. I. Taxonomy, fermentation, isolation, and biological activities
    • Romero, F.; Espliego, F.; Pérez Baz, J.; García de Quesada, T.; Grávalos, D.; de la Calle, F.; Fernández-Puentes, J.L. Thiocoraline, a new depsipeptide with antitumor activity produced by a marine Micromonospora. I. Taxonomy, fermentation, isolation, and biological activities. J. Antibiot. 1997, 50, 734-737.
    • (1997) J. Antibiot. , vol.50 , pp. 734-737
    • Romero, F.1    Espliego, F.2    Pérez Baz, J.3    García De Quesada, T.4    Grávalos, D.5    De La Calle, F.6    Fernández-Puentes, J.L.7
  • 19
    • 0027410004 scopus 로고
    • Sandramycin, a novel antitumor antibiotic produced by a nocardioides sp. II. Structure determination
    • Matson, J.A.; Colson, K.L.; Belofsky, G.N.; Bleiberg, B.B. Sandramycin, a novel antitumor antibiotic produced by a Nocardioides sp. II. Structure determination. J. Antibiot. 1993, 46, 162-166. (Pubitemid 23075328)
    • (1993) Journal of Antibiotics , vol.46 , Issue.1 , pp. 162-166
    • Matson, J.A.1    Colson, K.L.2    Belofsky, G.N.3    Bleiberg, B.B.4
  • 20
    • 0028197474 scopus 로고
    • A new topoisomerase II inhibitor, BE-22179, produced by a Streptomycete. I. Producing strain, fermentation, isolation and biological activity
    • Okada, H.; Suzuki, H.; Yoshinari, T.; Arakawa, H.; Okura, A.; Suda, H.; Yamada, A.; Uemura, D. A new topoisomerase II inhibitor, BE-22179, produced by a streptomycete. I. Producing strain, fermentation, isolation and biological activity. J. Antibiot. 1994, 47, 129-135. (Pubitemid 24075566)
    • (1994) Journal of Antibiotics , vol.47 , Issue.2 , pp. 129-135
    • Okada, H.1    Suzuki, H.2    Yoshinari, T.3    Arakawa, H.4    Okura, A.5    Suda, H.6    Yamada, A.7    Uemura, D.8
  • 23
    • 0020526851 scopus 로고
    • Intermolecular cross-linking of DNA through bifunctional intercalation of an antitumor antibiotic, luzopeptin A (BBM-928A)
    • Huang, C.H.; Mirabelli, C.K.; Mong, S.; Crooke, S.T. Intermolecular cross-linking of DNA through bifunctional intercalation of an antitumor antibiotic, luzopeptin A (BBM-928A). Cancer Res. 1983, 43, 2718-2724. (Pubitemid 13100538)
    • (1983) Cancer Research , vol.43 , Issue.6 , pp. 2718-2724
    • Huang, C.H.1    Mirabelli, C.K.2    Mong, S.3    Crooke, S.T.4
  • 25
    • 0344830196 scopus 로고    scopus 로고
    • Thiocoraline, a novel depsipeptide with antitumor activity produced by a marine Micromonospora. II. Physico-chemical properties and structure determination
    • Perez Baz, J.; Cañedo, L.M.; Fernández Puentes, J.L.; Silva Elipe, M.V. Thiocoraline, a novel depsipeptide with antitumor activity produced by a marine Micromonospora. II. Physico-chemical properties and structure determination. J. Antibiot. 1997, 50, 738-741.
    • (1997) J. Antibiot. , vol.50 , pp. 738-741
    • Perez Baz, J.1    Cañedo, L.M.2    Fernández Puentes, J.L.3    Silva Elipe, M.V.4
  • 26
    • 62249197483 scopus 로고    scopus 로고
    • Complete sequence of biosynthetic gene cluster responsible for producing triostin A and evaluation of quinomycin-type antibiotics from Streptomyces triostinicus
    • Praseuth, A.P.; Wang, C.C.; Watanabe, K.; Hotta, K.; Oguri, H.; Oikawa, H. Complete sequence of biosynthetic gene cluster responsible for producing triostin A and evaluation of quinomycin-type antibiotics from Streptomyces triostinicus. Biotechnol. Prog. 2008, 24, 1226-1231.
    • (2008) Biotechnol. Prog. , vol.24 , pp. 1226-1231
    • Praseuth, A.P.1    Wang, C.C.2    Watanabe, K.3    Hotta, K.4    Oguri, H.5    Oikawa, H.6
  • 27
    • 67649961441 scopus 로고    scopus 로고
    • Escherichia coli allows efficient modular incorporation of newly isolated quinomycin biosynthetic enzyme into echinomycin biosynthetic pathway for rational design and synthesis of potent antibiotic unnatural natural product
    • Watanabe, K.; Hotta, K.; Nakaya, M.; Praseuth, A.P.; Wang, C.C.; Inada, D.; Takahashi, K.; Fukushi, E.; Oguri, H.; Oikawa, H. Escherichia coli allows efficient modular incorporation of newly isolated quinomycin biosynthetic enzyme into echinomycin biosynthetic pathway for rational design and synthesis of potent antibiotic unnatural natural product. J. Am. Chem. Soc. 2009, 131, 9347-9353.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 9347-9353
    • Watanabe, K.1    Hotta, K.2    Nakaya, M.3    Praseuth, A.P.4    Wang, C.C.5    Inada, D.6    Takahashi, K.7    Fukushi, E.8    Oguri, H.9    Oikawa, H.10
  • 28
    • 0034827133 scopus 로고    scopus 로고
    • SW-163C and E, novel antitumor depsipeptides produced by Streptomyces sp. II. Structure elucidation
    • Takahashi, K.; Koshino, H.; Esumi, Y.; Tsuda, E.; Kurosawa, K. SW-163C and E, novel antitumor depsipeptides produced by Streptomyces sp. II. Structure elucidation. J. Antibiot. 2001, 54, 622-627. (Pubitemid 32894104)
    • (2001) Journal of Antibiotics , vol.54 , Issue.8 , pp. 622-627
    • Takahashi, K.1    Koshino, H.2    Esumi, Y.3    Tsuda, E.4    Kurosawa, K.5
  • 31
    • 0014072341 scopus 로고
    • Influence of isoleucine upon quinomycin biosynthesis by Streptomyces sp. 732
    • Yoshida, T.; Katagiri, K. Influence of isoleucine upon quinomycin biosynthesis by Streptomyces sp. 732. J. Bacteriol. 1967, 93, 1327-1331.
    • (1967) J. Bacteriol. , vol.93 , pp. 1327-1331
    • Yoshida, T.1    Katagiri, K.2
  • 32
    • 0032483551 scopus 로고    scopus 로고
    • Synthesis of Acyclic Precursors to (3S,4S)-4-Hydroxy-2,3,4, 5-tetrahydropyridazine-3-carboxylic Acid and Incorporation into a Luzopeptin/Quinoxapeptin Dipeptide
    • Boger, D.L.; Schüle, G. Synthesis of Acyclic Precursors to (3S,4S)-4-Hydroxy-2,3,4, 5-tetrahydropyridazine-3-carboxylic Acid and Incorporation into a Luzopeptin/Quinoxapeptin Dipeptide. J. Org. Chem. 1998, 63, 6421-6424.
    • (1998) J. Org. Chem. , vol.63 , pp. 6421-6424
    • Boger, D.L.1    Schüle, G.2
  • 33
    • 0033549831 scopus 로고    scopus 로고
    • Total Synthesis of Quinoxapeptin A-C: Establishment of Absolute Stereochemistry
    • Boger, D.L.; Ledeboer, M.W.; Kume, M.; Jin, Q. Total Synthesis of Quinoxapeptin A-C: Establishment of Absolute Stereochemistry. Angew. Chem. Int. Ed. Engl. 1999, 38, 2424-2426.
    • (1999) Angew. Chem. Int. Ed. Engl. , vol.38 , pp. 2424-2426
    • Boger, D.L.1    Ledeboer, M.W.2    Kume, M.3    Jin, Q.4
  • 34
    • 14844362054 scopus 로고    scopus 로고
    • Molecular mechanisms underlying nonribosomal peptide synthesis: Approaches to new antibiotics
    • DOI 10.1021/cr0301191
    • Sieber, S.A.; Marahiel, M.A. Molecular mechanisms underlying nonribosomal peptide synthesis: Approaches to new antibiotics. Chem. Rev. 2005, 105, 715-738. (Pubitemid 40351638)
    • (2005) Chemical Reviews , vol.105 , Issue.2 , pp. 715-738
    • Sieber, S.A.1    Marahiel, M.A.2
  • 36
    • 1642496907 scopus 로고    scopus 로고
    • The biosynthesis of glycopeptide antibiotics - A model for complex, non-ribosomally synthesized, peptidic secondary metabolites
    • Süssmuth, R.D.; Wohlleben, W. The biosynthesis of glycopeptide antibiotics - A model for complex, non-ribosomally synthesized, peptidic secondary metabolites. Appl. Microbiol. Biotechnol. 2004, 63, 344-350.
    • (2004) Appl. Microbiol. Biotechnol. , vol.63 , pp. 344-350
    • Süssmuth, R.D.1    Wohlleben, W.2
  • 38
    • 0032501971 scopus 로고    scopus 로고
    • Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carder protein domains in peptide synthetases
    • DOI 10.1021/bi9719861
    • Quadri, L.E.; Weinreb, P.H.; Lei, M.; Nakano, M.M.; Zuber, P.; Walsh, C.T. Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases. Biochemistry 1998, 37, 1585-1595. (Pubitemid 28093674)
    • (1998) Biochemistry , vol.37 , Issue.6 , pp. 1585-1595
    • Quadri, L.E.N.1    Weinreb, P.H.2    Lei, M.3    Nakano, M.M.4    Zuber, P.5    Walsh, C.T.6
  • 39
    • 0033179468 scopus 로고    scopus 로고
    • The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases
    • DOI 10.1016/S1074-5521(99)80082-9
    • Stachelhaus, T.; Mootz, H.D.; Marahiel, M.A. The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases. Chem. Biol. 1999, 6, 493-505. (Pubitemid 29380764)
    • (1999) Chemistry and Biology , vol.6 , Issue.8 , pp. 493-505
    • Stachelhaus, T.1    Mootz, H.D.2    Marahiel, M.A.3
  • 40
    • 0034013269 scopus 로고    scopus 로고
    • Predictive, structure-based model of amino acid recognition by nonribosomal peptide synthetase adenylation domains
    • DOI 10.1016/S1074-5521(00)00091-0
    • Challis, G.L.; Ravel, J.; Townsend, C.A. Predictive, structure-based model of amino acid recognition by nonribosomal peptide synthetase adenylation domains. Chem. Biol. 2000, 7, 211-224. (Pubitemid 30147205)
    • (2000) Chemistry and Biology , vol.7 , Issue.3 , pp. 211-224
    • Challis, G.L.1    Ravel, J.2    Townsend, C.A.3
  • 41
    • 84901391902 scopus 로고
    • The biosynthesis of the quinoxaline antibiotic, triostin, by Streptomyces S-2-2 1. On the role of quinoxaline-2-carboxylic acid
    • University Park Press: Baltimore, MD, USA
    • Yoshida, T.; Kimura, Y.; Katagiri, K. The biosynthesis of the quinoxaline antibiotic, triostin, by Streptomyces S-2-2 1. On the role of quinoxaline-2-carboxylic acid. In Progress in Antimicrobial and Anticancer Chemotherapy; University Park Press: Baltimore, MD, USA, 1970; pp. 1160-1165.
    • (1970) Progress in Antimicrobial and Anticancer Chemotherapy , pp. 1160-1165
    • Yoshida, T.1    Kimura, Y.2    Katagiri, K.3
  • 42
    • 0021984156 scopus 로고
    • Incorporation of fluorotryptophan into triostin antibiotics by Streptomyces triostinicus
    • Cornish, A.; Fox, K.R.; Santikarn, S.; Waring, M.J.; Williams, D.H. Incorporation of fluorotryptophan into triostin antibiotics by Streptomyces triostinicus. J. Gen. Microbiol. 1985, 131, 561-570.
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 561-570
    • Cornish, A.1    Fox, K.R.2    Santikarn, S.3    Waring, M.J.4    Williams, D.H.5
  • 45
    • 33750344073 scopus 로고    scopus 로고
    • Identification and stereochemical assignment of the beta- hydroxytryptophan intermediate in the echinomycin biosynthetic pathway
    • DOI 10.1021/ol061738+
    • Koketsu, K.; Oguri, H.; Watanabe, K.; Oikawa, H. Identification and stereochemical assignment of the beta-hydroxytryptophan intermediate in the echinomycin biosynthetic pathway. Org. Lett. 2006, 8, 4719-4722. (Pubitemid 44629444)
    • (2006) Organic Letters , vol.8 , Issue.21 , pp. 4719-4722
    • Koketsu, K.1    Oguri, H.2    Watanabe, K.3    Oikawa, H.4
  • 46
    • 43949096904 scopus 로고    scopus 로고
    • Characterization of TioF, a tryptophan 2,3-dioxygenase involved in 3-hydroxyquinaldic acid formation during thiocoraline biosynthesis
    • DOI 10.1039/b801391h
    • Sheoran, A.; King, A.; Velasco, A.; Pero, J.M.; Garneau-Tsodikova, S. Characterization of TioF, a tryptophan 2,3-dioxygenase involved in 3-hydroxyquinaldic acid formation during thiocoraline biosynthesis. Mol. Biosyst. 2008, 4, 622-628. (Pubitemid 351706306)
    • (2008) Molecular BioSystems , vol.4 , Issue.6 , pp. 622-628
    • Sheoran, A.1    King, A.2    Velasco, A.3    Pero, J.M.4    Garneau-Tsodikova, S.5
  • 47
    • 79251631449 scopus 로고    scopus 로고
    • Involvement of common intermediate 3-hydroxy-L-kynurenine in chromophore biosynthesis of quinomycin family antibiotics
    • Hirose, Y.; Watanabe, K.; Minami, A.; Nakamura, T.; Oguri, H.; Oikawa, H. Involvement of common intermediate 3-hydroxy-L-kynurenine in chromophore biosynthesis of quinomycin family antibiotics. J. Antibiot. 2011, 64, 117-122.
    • (2011) J. Antibiot. , vol.64 , pp. 117-122
    • Hirose, Y.1    Watanabe, K.2    Minami, A.3    Nakamura, T.4    Oguri, H.5    Oikawa, H.6
  • 48
    • 84878622154 scopus 로고    scopus 로고
    • Tryptophan metabolism: Entering the field of aging and age-related pathologies
    • van der Goot, A.T.; Nollen, E.A. Tryptophan metabolism: Entering the field of aging and age-related pathologies. Trends Mol. Med. 2013, 19, 336-344.
    • (2013) Trends Mol. Med. , vol.19 , pp. 336-344
    • Van Der Goot, A.T.1    Nollen, E.A.2
  • 49
    • 0021191712 scopus 로고
    • Directed biosynthesis of novel derivatives of echinomycin by Streptomyces echinatus. I. Effect of exogenous analogues of quinoxaline-2-carboxylic acid on the fermentation
    • Gauvreau, D.; Waring, M.J. Directed biosynthesis of novel derivatives of echinomycin by Streptomyces echinatus. I. Effect of exogenous analogues of quinoxaline-2-carboxylic acid on the fermentation. Can. J. Microbiol. 1984, 30, 439-450. (Pubitemid 14078630)
    • (1984) Canadian Journal of Microbiology , vol.30 , Issue.4 , pp. 439-450
    • Gauvreau, D.1    Waring, M.J.2
  • 50
    • 0025260970 scopus 로고
    • Biosynthesis of quinoxaline antibiotics: Purification and characterization of the quinoxaline-2-carboxylic acid activating enzyme from streptomyces triostinicus
    • Glund, K.; Schlumbohm, W.; Bapat, M.; Keller, U. Biosynthesis of quinoxaline antibiotics: Purification and characterization of the quinoxaline-2-carboxylic acid activating enzyme from Streptomyces triostinicus. Biochemistry 1990, 29, 3522-3527. (Pubitemid 20136045)
    • (1990) Biochemistry , vol.29 , Issue.14 , pp. 3522-3527
    • Glund, K.1    Schlumbohm, W.2    Bapat, M.3    Keller, U.4
  • 52
    • 79960251826 scopus 로고    scopus 로고
    • Molecular cloning and identification of the laspartomycin biosynthetic gene cluster from Streptomyces viridochromogenes
    • Wang, Y.; Chen, Y.; Shen, Q.; Yin, X. Molecular cloning and identification of the laspartomycin biosynthetic gene cluster from Streptomyces viridochromogenes. Gene 2011, 483, 11-21.
    • (2011) Gene , vol.483 , pp. 11-21
    • Wang, Y.1    Chen, Y.2    Shen, Q.3    Yin, X.4
  • 53
    • 80052595178 scopus 로고    scopus 로고
    • Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in Staphylococcus aureus
    • doi:10.1186/1471-2180-11-199
    • Beasley, F.C.; Cheung, J.; Heinrichs, D.E. Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in Staphylococcus aureus. BMC Microbiol. 2011, 11, doi:10.1186/1471-2180-11-199.
    • (2011) BMC Microbiol. , vol.11
    • Beasley, F.C.1    Cheung, J.2    Heinrichs, D.E.3
  • 54
    • 43749099439 scopus 로고    scopus 로고
    • Identification of a novel beta-replacement reaction in the biosynthesis of 2,3-diaminobutyric acid in peptidylnucleoside mureidomycin A
    • DOI 10.1039/b802585a
    • Lam, W.H.; Rychli, K.; Bugg, T.D. Identification of a novel beta-replacement reaction in the biosynthesis of 2,3-diaminobutyric acid in peptidylnucleoside mureidomycin A. Org. Biomol. Chem. 2008, 6, 1912-1917. (Pubitemid 351693235)
    • (2008) Organic and Biomolecular Chemistry , vol.6 , Issue.11 , pp. 1912-1917
    • Lam, W.-H.1    Rychli, K.2    Bugg, T.D.H.3
  • 55
    • 33645392725 scopus 로고    scopus 로고
    • Biosynthesis of pipecolic acid by RapL, a lysine cyclodeaminase encoded in the rapamycin gene cluster
    • Gatto, G.J., Jr.; Boyne, M.T., II; Kelleher, N.L.; Walsh, C.T. Biosynthesis of pipecolic acid by RapL, a lysine cyclodeaminase encoded in the rapamycin gene cluster. J. Am. Chem. Soc. 2006, 128, 3838-3847.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 3838-3847
    • Gatto Jr., G.J.1    Boyne II, M.T.2    Kelleher, N.L.3    Walsh, C.T.4
  • 56
    • 84884353163 scopus 로고    scopus 로고
    • Enhancement of FK506 production by engineering secondary pathways of Streptomyces tsukubaensis and exogenous feeding strategies
    • Huang, D.; Xia, M.; Li, S.; Wen, J.; Jia, X. Enhancement of FK506 production by engineering secondary pathways of Streptomyces tsukubaensis and exogenous feeding strategies. J. Ind. Microbiol. Biotechnol. 2013, 40, 1023-1037.
    • (2013) J. Ind. Microbiol. Biotechnol. , vol.40 , pp. 1023-1037
    • Huang, D.1    Xia, M.2    Li, S.3    Wen, J.4    Jia, X.5
  • 57
    • 0037139606 scopus 로고    scopus 로고
    • Characterization of virginiamycin S biosynthetic genes from Streptomyces virginiae
    • DOI 10.1016/S0378-1119(02)00424-9, PII S0378111902004249
    • Namwat, W.; Kamioka, Y.; Kinoshita, H.; Yamada, Y.; Nihira, T. Characterization of virginiamycin S biosynthetic genes from Streptomyces virginiae. Gene 2002, 286, 283-290. (Pubitemid 34273884)
    • (2002) Gene , vol.286 , Issue.2 , pp. 283-290
    • Namwat, W.1    Kamioka, Y.2    Kinoshita, H.3    Yamada, Y.4    Nihira, T.5
  • 58
    • 77949558085 scopus 로고    scopus 로고
    • Discovery of 23 natural tubulysins from Angiococcus disciformis An d48 and Cystobacter SBCb004
    • Chai, Y.; Pistorius, D.; Ullrich, A.; Weissman, K.J.; Kazmaier, U.; Müller, R. Discovery of 23 natural tubulysins from Angiococcus disciformis An d48 and Cystobacter SBCb004. Chem. Biol. 2010, 17, 296-309.
    • (2010) Chem. Biol. , vol.17 , pp. 296-309
    • Chai, Y.1    Pistorius, D.2    Ullrich, A.3    Weissman, K.J.4    Kazmaier, U.5    Müller, R.6
  • 59
    • 79960771427 scopus 로고    scopus 로고
    • Piperazic acid-containing natural products: Isolation, biological relevance and total synthesis
    • Oelke, A.J.; France, D.J.; Hofmann, T.; Wuitschik, G.; Ley, S.V. Piperazic acid-containing natural products: Isolation, biological relevance and total synthesis. Nat. Prod. Rep. 2011, 28, 1445-1471.
    • (2011) Nat. Prod. Rep. , vol.28 , pp. 1445-1471
    • Oelke, A.J.1    France, D.J.2    Hofmann, T.3    Wuitschik, G.4    Ley, S.V.5
  • 60
    • 79951595684 scopus 로고    scopus 로고
    • Cloning, sequencing and characterization of the biosynthetic gene cluster of sanglifehrin A, a potent cyclophilin inhibitor
    • Qu, X.; Jiang, N.; Xu, F.; Shao, L.; Tang, G.; Wilkinson, B.; Liu, W. Cloning, sequencing and characterization of the biosynthetic gene cluster of sanglifehrin A, a potent cyclophilin inhibitor. Mol. Biosyst. 2011, 7, 852-861.
    • (2011) Mol. Biosyst. , vol.7 , pp. 852-861
    • Qu, X.1    Jiang, N.2    Xu, F.3    Shao, L.4    Tang, G.5    Wilkinson, B.6    Liu, W.7
  • 62
    • 15744381452 scopus 로고    scopus 로고
    • Functional cross-talk between fatty acid synthesis and nonribosomal peptide synthesis in quinoxaline antibiotic-producing streptomycetes
    • DOI 10.1074/jbc.M411026200
    • Schmoock, G.; Pfennig, F.; Jewiarz, J.; Schlumbohm, W.; Laubinger, W.; Schauwecker, F.; Keller, U. Functional cross-talk between fatty acid synthesis and nonribosomal peptide synthesis in quinoxaline antibiotic-producing streptomycetes. J. Biol. Chem. 2005, 280, 4339-4349. (Pubitemid 41741354)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.6 , pp. 4339-4349
    • Schmoock, G.1    Pfennig, F.2    Jewiarz, J.3    Schlumbohm, W.4    Laubinger, W.5    Schauwecker, F.6    Keller, U.7
  • 63
    • 61349111371 scopus 로고    scopus 로고
    • TioS T-TE - A prototypical thioesterase responsible for cyclodimerization of the quinoline- and quinoxaline-type class of chromodepsipeptides
    • Robbel, L.; Hoyer, K.M.; Marahiel, M.A. TioS T-TE - A prototypical thioesterase responsible for cyclodimerization of the quinoline- and quinoxaline-type class of chromodepsipeptides. FEBS J. 2009, 276, 1641-1653.
    • (2009) FEBS J. , vol.276 , pp. 1641-1653
    • Robbel, L.1    Hoyer, K.M.2    Marahiel, M.A.3
  • 64
    • 49449114802 scopus 로고    scopus 로고
    • Enzymatic macrolactonization in the presence of DNA leading to triostin A analogs
    • Koketsu, K.; Oguri, H.; Watanabe, K.; Oikawa, H. Enzymatic macrolactonization in the presence of DNA leading to triostin A analogs. Chem. Biol. 2008, 15, 818-828.
    • (2008) Chem. Biol. , vol.15 , pp. 818-828
    • Koketsu, K.1    Oguri, H.2    Watanabe, K.3    Oikawa, H.4
  • 66
    • 77955800751 scopus 로고    scopus 로고
    • Transannular disulfide formation in gliotoxin biosynthesis and its role in self-resistance of the human pathogen Aspergillus fumigatus
    • Scharf, D.H.; Remme, N.; Heinekamp, T.; Hortschansky, P.; Brakhage, A.A.; Hertweck, C. Transannular disulfide formation in gliotoxin biosynthesis and its role in self-resistance of the human pathogen Aspergillus fumigatus. J. Am. Chem. Soc. 2010, 132, 10136-10141.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 10136-10141
    • Scharf, D.H.1    Remme, N.2    Heinekamp, T.3    Hortschansky, P.4    Brakhage, A.A.5    Hertweck, C.6
  • 69
    • 0037126848 scopus 로고    scopus 로고
    • The 1.6-A crystal structure of the copper(II)-bound bleomycin complexed with the bleomycin-binding protein from bleomycin-producing Streptomyces verticillus
    • DOI 10.1074/jbc.M103278200
    • Sugiyama, M.; Kumagai, T.; Hayashida, M.; Maruyama, M.; Matoba, Y. The 1.6-A crystal structure of the copper(II)-bound bleomycin complexed with the bleomycin-binding protein from bleomycin-producing Streptomyces verticillus. J. Biol. Chem. 2002, 277, 2311-2320. (Pubitemid 34968818)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.3 , pp. 2311-2320
    • Sugiyama, M.1    Kumagai, T.2    Hayashida, M.3    Maruyama, M.4    Matoba, Y.5
  • 70
    • 0016352541 scopus 로고
    • Echinomycin: A bifunctional intercalating antibiotic
    • Waring, M.J.; Wakelin, L.P. Echinomycin: A bifunctional intercalating antibiotic. Nature 1974, 252, 653-657.
    • (1974) Nature , vol.252 , pp. 653-657
    • Waring, M.J.1    Wakelin, L.P.2
  • 71
    • 0022414532 scopus 로고
    • The role of the cyclic depsipeptide rings in antibiotics
    • Takusagawa, F. The role of the cyclic depsipeptide rings in antibiotics. J. Antibiot. 1985, 38, 1596-1604. (Pubitemid 16217850)
    • (1985) Journal of Antibiotics , vol.38 , Issue.11 , pp. 1596-1604
    • Takusagawa, F.1
  • 72
    • 0021773061 scopus 로고
    • Sequence preferences in the binding to DNA of triostin A and TANDEM as reported by DNase I footprinting
    • Low, C.M.; Olsen, R.K.; Waring, M.J. Sequence preferences in the binding to DNA of triostin A and TANDEM as reported by DNase I footprinting. FEBS Lett. 1984, 176, 414-420.
    • (1984) FEBS Lett. , vol.176 , pp. 414-420
    • Low, C.M.1    Olsen, R.K.2    Waring, M.J.3
  • 73
    • 0030840016 scopus 로고    scopus 로고
    • Binding of two novel bisdaunorubicins to DNA studied by NMR spectroscopy
    • DOI 10.1021/bi970842j
    • Robinson, H.; Priebe, W.; Chaires, J.B.; Wang, A.H. Binding of two novel bisdaunorubicins to DNA studied by NMR spectroscopy. Biochemistry 1997, 36, 8663-8670. (Pubitemid 27342510)
    • (1997) Biochemistry , vol.36 , Issue.29 , pp. 8663-8670
    • Robinson, H.1    Priebe, W.2    Chaires, J.B.3    Wang, A.H.-J.4
  • 74
    • 0028864424 scopus 로고
    • Studies of base pair kinetics by NMR measurement of proton exchange
    • Guéron, M.; Leroy, J.L. Studies of base pair kinetics by NMR measurement of proton exchange. Methods Enzymol. 1995, 261, 383-413.
    • (1995) Methods Enzymol. , vol.261 , pp. 383-413
    • Guéron, M.1    Leroy, J.L.2
  • 77
    • 34347249592 scopus 로고    scopus 로고
    • 4 reactions and electrospray ionization tandem mass spectrometry
    • DOI 10.1021/ac070145p
    • Mazzitelli, C.L.; Brodbelt, J.S. Probing ligand binding to duplex DNA using KMnO4 reactions and electrospray ionization tandem mass spectrometry. Anal. Chem. 2007, 79, 4636-4647. (Pubitemid 46999581)
    • (2007) Analytical Chemistry , vol.79 , Issue.12 , pp. 4636-4647
    • Mazzitelli, C.L.1    Brodbelt, J.S.2
  • 78
    • 0031985812 scopus 로고    scopus 로고
    • Synthesis of key sandramycin analogs: Systematic examination of the intercalation chromophore
    • DOI 10.1016/S0968-0896(97)10014-1, PII S0968089697100141
    • Boger, D.L.; Chen, J.H.; Saionz, K.W.; Jin, Q. Synthesis of key sandramycin analogs: Systematic examination of the intercalation chromophore. Bioorg. Med. Chem. 1998, 6, 85-102. (Pubitemid 28051308)
    • (1998) Bioorganic and Medicinal Chemistry , vol.6 , Issue.1 , pp. 85-102
    • Boger, D.L.1    Chen, J.-H.2    Saionz, K.W.3    Jin, Q.4
  • 79
    • 33846446394 scopus 로고    scopus 로고
    • Screening of Threading Bis-Intercalators Binding to Duplex DNA by Electrospray Ionization Tandem Mass Spectrometry
    • DOI 10.1016/j.jasms.2006.09.021, PII S1044030506008403
    • Mazzitelli, C.L.; Chu, Y.; Reczek, J.J.; Iverson, B.L.; Brodbelt, J.S. Screening of threading bis-intercalators binding to duplex DNA by electrospray ionization tandem mass spectrometry. J. Am. Soc. Mass Spectrom. 2007, 18, 311-321. (Pubitemid 46150098)
    • (2007) Journal of the American Society for Mass Spectrometry , vol.18 , Issue.2 , pp. 311-321
    • Mazzitelli, C.L.1    Chu, Y.2    Reczek, J.J.3    Iverson, B.L.4    Brodbelt, J.S.5
  • 80
    • 84888088152 scopus 로고    scopus 로고
    • Non-covalent duplex to duplex crosslinking of DNA in solution revealed by single molecule force spectroscopy
    • Rackham, B.D.; Howell, L.A.; Round, A.N.; Searcey, M. Non-covalent duplex to duplex crosslinking of DNA in solution revealed by single molecule force spectroscopy. Org. Biomol. Chem. 2013, 11, 8340-8347.
    • (2013) Org. Biomol. Chem. , vol.11 , pp. 8340-8347
    • Rackham, B.D.1    Howell, L.A.2    Round, A.N.3    Searcey, M.4
  • 82
    • 0018149852 scopus 로고
    • Interaction between synthetic analogues of quinoxaline antibiotics and nucleic acids. Changes in mechanism and specificity related to structural alterations
    • Lee, J.S.; Waring, M.J. Interaction between synthetic analogues of quinoxaline antibiotics and nucleic acids. Changes in mechanism and specificity related to structural alterations. Biochem. J. 1978, 173, 129-144. (Pubitemid 8368286)
    • (1978) Biochemical Journal , vol.173 , Issue.1 , pp. 129-144
    • Lee, J.S.1    Waring, M.J.2
  • 84
    • 0025863112 scopus 로고
    • The DNA sequence at echinomycin binding sites determines the structural changes induced by drug binding: NMR studies of echinomycin binding to [d(ACGTACGT)]2 and [d(TCGATCGA)]2
    • Gilbert, D.E.; Feigon, J. The DNA sequence at echinomycin binding sites determines the structural changes induced by drug binding: NMR studies of echinomycin binding to [d(ACGTACGT)]2 and [d(TCGATCGA)]2. Biochemistry 1991, 30, 2483-2494.
    • (1991) Biochemistry , vol.30 , pp. 2483-2494
    • Gilbert, D.E.1    Feigon, J.2
  • 85
    • 0021192920 scopus 로고
    • Echinomycin binding sites on DNA
    • Van Dyke, M.M.; Dervan, P.B. Echinomycin binding sites on DNA. Science 1984, 225, 1122-1127. (Pubitemid 14029093)
    • (1984) Science , vol.225 , Issue.4667 , pp. 1122-1127
    • Van Dyke, M.M.1    Dervan, P.B.2
  • 87
    • 0014434367 scopus 로고
    • Effect of olivomycin and echinomycin on initiation and growth of RNA chains catalyzed by RNA polymerase
    • Gause, G.G., Jr.; Loshkareva, N.P.; Zbarsky, I.B. Effect of olivomycin and echinomycin on initiation and growth of RNA chains catalyzed by RNA polymerase. Biochim. Biophys. Acta 1968, 166, 752-754.
    • (1968) Biochim. Biophys. Acta , vol.166 , pp. 752-754
    • Gause Jr., G.G.1    Loshkareva, N.P.2    Zbarsky, I.B.3
  • 88
    • 0034056690 scopus 로고    scopus 로고
    • 2] complexes
    • DOI 10.1107/S0907444999016790
    • Takusagawa, H.L.; Takusagawa, F. Crystallization and preliminary X-ray diffraction studies of d(ACGTAGCTACGT)2:[actinomycin D, (echinomycin)2] and d(ACGTAGCTACGT)2: [actinomycin D, (triostin A)2] complexes. Acta Crystallogr. D Biol. Crystallogr. 2000, 56, 344-347. (Pubitemid 30147186)
    • (2000) Acta Crystallographica Section D: Biological Crystallography , vol.56 , Issue.3 , pp. 344-347
    • Takusagawa, H.L.1    Takusagawa, F.2
  • 89
    • 0035977628 scopus 로고    scopus 로고
    • Total syntheses of thiocoraline and BE-22179 and assessment of their DNA binding and biological properties
    • DOI 10.1021/ja003602r
    • Boger, D.L.; Ichikawa, S.; Tse, W.C.; Hedrick, M.P.; Jin, Q. Total syntheses of thiocoraline and BE-22179 and assessment of their DNA binding and biological properties. J. Am. Chem. Soc. 2001, 123, 561-568. (Pubitemid 32105998)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.4 , pp. 561-568
    • Boger, D.L.1    Ichikawa, S.2    Tse, W.C.3    Hedrick, M.P.4    Jin, Q.5
  • 90
    • 38349148467 scopus 로고    scopus 로고
    • Investigation of DNA-binding properties of organic molecules using quantitative structure-activity relationship (QSAR) models
    • Verma, R.P.; Hansch, C. Investigation of DNA-binding properties of organic molecules using quantitative structure-activity relationship (QSAR) models. J. Pharm. Sci. 2008, 97, 88-110.
    • (2008) J. Pharm. Sci. , vol.97 , pp. 88-110
    • Verma, R.P.1    Hansch, C.2
  • 91
    • 0033051824 scopus 로고    scopus 로고
    • DNA binding properties of key sandramycin analogues: Systematic examination of the intercalation chromophore
    • DOI 10.1016/S0968-0896(98)00206-5, PII S0968089698002065
    • Boger, D.L.; Saionz, K.W. DNA binding properties of key sandramycin analogues: Systematic examination of the intercalation chromophore. Bioorg. Med. Chem. 1999, 7, 315-321. (Pubitemid 29117094)
    • (1999) Bioorganic and Medicinal Chemistry , vol.7 , Issue.2 , pp. 315-321
    • Boger, D.L.1    Saionz, K.W.2
  • 92
    • 0026598551 scopus 로고
    • Proton exchange in DNA-luzopeptin and DNA-echinomycin bisintercalation complexes: Rates and processes of base-pair opening
    • Leroy, J.L.; Gao, X.L.; Misra, V.; Guéron, M.; Patel, D.J. Proton exchange in DNA-luzopeptin and DNA-echinomycin bisintercalation complexes: Rates and processes of base-pair opening. Biochemistry 1992, 31, 1407-1415.
    • (1992) Biochemistry , vol.31 , pp. 1407-1415
    • Leroy, J.L.1    Gao, X.L.2    Misra, V.3    Guéron, M.4    Patel, D.J.5
  • 93
    • 0037403508 scopus 로고    scopus 로고
    • The binding mode of the DNA bisintercalator luzopeptin investigated using atomic force microscopy
    • DOI 10.1016/S1047-8477(03)00015-7
    • Berge, T.; Haken, E.L.; Waring, M.J.; Henderson, R.M. The binding mode of the DNA bisintercalator luzopeptin investigated using atomic force microscopy. J. Struct. Biol. 2003, 142, 241-246. (Pubitemid 36444666)
    • (2003) Journal of Structural Biology , vol.142 , Issue.2 , pp. 241-246
    • Berge, T.1    Haken, E.L.2    Waring, M.J.3    Henderson, R.M.4
  • 94
    • 0033745893 scopus 로고    scopus 로고
    • DNA recognition by quinoline antibiotics: Use of base-modified DNA molecules to investigate determinants of sequence-specific binding of luzopeptin
    • Bailly, C.; Crow, S.; Minnock, A.; Waring, M.J. DNA recognition by quinoline antibiotics: Use of base-modified DNA molecules to investigate determinants of sequence-specific binding of luzopeptin. Nucleosides Nucleotides Nucleic Acids 2000, 19, 1337-1353.
    • (2000) Nucleosides Nucleotides Nucleic Acids , vol.19 , pp. 1337-1353
    • Bailly, C.1    Crow, S.2    Minnock, A.3    Waring, M.J.4
  • 95
    • 0025858691 scopus 로고
    • Solution structure of the luzopeptin-DNA complex
    • Zhang, X.L.; Patel, D.J. Solution structure of the luzopeptin-DNA complex. Biochemistry 1991, 30, 4026-4041.
    • (1991) Biochemistry , vol.30 , pp. 4026-4041
    • Zhang, X.L.1    Patel, D.J.2
  • 96
    • 0021931261 scopus 로고
    • Effects of structural modifications of antitumor antibiotics (luzopeptins) on the interactions with deoxyribonucleic acid
    • Huang, C.H.; Crooke, S.T. Effects of structural modifications of antitumor antibiotics (luzopeptins) on the interactions with deoxyribonucleic acid. Cancer Res. 1985, 45, 3768-3773. (Pubitemid 15226456)
    • (1985) Cancer Research , vol.45 , Issue.8 , pp. 3768-3773
    • Huang, C.-H.1    Crooke, S.T.2
  • 98
    • 0026718484 scopus 로고
    • Echinomycin (NSC 526417) in recurrent and metastatic nonsquamous cell carcinoma of the cervix. A phase II trial of the Gynecologic Oncology Group
    • Muss, H.B.; Blessing, J.A.; Hanjani, P.; Malfetano, J.H.; Kemp, G.M.; Webster, K. Echinomycin (NSC 526417) in recurrent and metastatic nonsquamous cell carcinoma of the cervix. A phase II trial of the Gynecologic Oncology Group. Am. J. Clin. Oncol. 1992, 15, 363-364.
    • (1992) Am. J. Clin. Oncol. , vol.15 , pp. 363-364
    • Muss, H.B.1    Blessing, J.A.2    Hanjani, P.3    Malfetano, J.H.4    Kemp, G.M.5    Webster, K.6
  • 99
    • 0024508518 scopus 로고
    • UK-63,052 complex, new quinomycin antibiotics from Streptomyces braegensis subsp. Japonicus; taxonomy, fermentation, isolation, characterisation and antimicrobial activity
    • Rance, M.J.; Ruddock, J.C.; Pacey, M.S.; Cullen, W.P.; Huang, L.H.; Jefferson, M.T.; Whipple, E.B.; Maeda, H.; Tone, J. UK-63,052 complex, new quinomycin antibiotics from Streptomyces braegensis subsp. japonicus; taxonomy, fermentation, isolation, characterisation and antimicrobial activity. J. Antibiot. 1989, 42, 206-217.
    • (1989) J. Antibiot. , vol.42 , pp. 206-217
    • Rance, M.J.1    Ruddock, J.C.2    Pacey, M.S.3    Cullen, W.P.4    Huang, L.H.5    Jefferson, M.T.6    Whipple, E.B.7    Maeda, H.8    Tone, J.9
  • 101
    • 60449108971 scopus 로고    scopus 로고
    • Structure-activity studies of echinomycin antibiotics against drug-resistant and biofilm-forming Staphylococcus aureus and Enterococcus faecalis
    • Socha, A.M.; Laplante, K.L.; Russell, D.J.; Rowley, D.C. Structure-activity studies of echinomycin antibiotics against drug-resistant and biofilm-forming Staphylococcus aureus and Enterococcus faecalis. Bioorg. Med. Chem. Lett. 2009, 19, 1504-1507.
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 1504-1507
    • Socha, A.M.1    Laplante, K.L.2    Russell, D.J.3    Rowley, D.C.4
  • 102
    • 37549042011 scopus 로고    scopus 로고
    • In vitro and in vivo activities of echinomycin against clinical isolates of Staphylococcus aureus
    • Park, Y.S.; Shin, W.S.; Kim, S.K. In vitro and in vivo activities of echinomycin against clinical isolates of Staphylococcus aureus. J. Antimicrob. Chemother. 2008, 61, 163-168.
    • (2008) J. Antimicrob. Chemother. , vol.61 , pp. 163-168
    • Park, Y.S.1    Shin, W.S.2    Kim, S.K.3
  • 103
    • 8844258137 scopus 로고    scopus 로고
    • In vitro antibacterial activity of echinomycin and a novel analogue, YK2000, against vancomycin-resistant enterococci
    • DOI 10.1016/j.ijantimicag.2004.03.018, PII S0924857904001803
    • Kim, J.B.; Lee, G.S.; Kim, Y.B.; Kim, S.K.; Kim, Y.H. In vitro antibacterial activity of echinomycin and a novel analogue, YK2000, against vancomycin-resistant enterococci. Int. J. Antimicrob. Agents 2004, 24, 613-615. (Pubitemid 39536119)
    • (2004) International Journal of Antimicrobial Agents , vol.24 , Issue.6 , pp. 613-615
    • Kim, J.-B.1    Lee, G.-S.2    Kim, Y.-B.3    Kim, S.-K.4    Kim, Y.H.5
  • 104
    • 0017722807 scopus 로고
    • Selective inhibition of influenza virus protein synthesis by inhibitors of DNA function
    • Minor, P.D.; Dimmock, N.J. Selective inhibition of influenza virus protein synthesis by inhibitors of DNA function. Virology 1977, 78, 393-406. (Pubitemid 8115888)
    • (1977) Virology , vol.78 , Issue.2 , pp. 393-406
    • Minor, P.D.1    Dimmock, N.J.2
  • 106
    • 84872312322 scopus 로고    scopus 로고
    • Antiamoebic properties of the actinomycete metabolites echinomycin A and tirandamycin A
    • Espinosa, A.; Socha, A.M.; Ryke, E.; Rowley, D.C. Antiamoebic properties of the actinomycete metabolites echinomycin A and tirandamycin A. Parasitol. Res. 2012, 111, 2473-2477.
    • (2012) Parasitol. Res. , vol.111 , pp. 2473-2477
    • Espinosa, A.1    Socha, A.M.2    Ryke, E.3    Rowley, D.C.4
  • 108
    • 0142166332 scopus 로고    scopus 로고
    • Targeting HIF-1 for cancer therapy
    • Semenza, G.L. Targeting HIF-1 for cancer therapy. Nat. Rev. Cancer. 2003, 3, 721-732. (Pubitemid 37328811)
    • (2003) Nature Reviews Cancer , vol.3 , Issue.10 , pp. 721-732
    • Semenza, G.L.1
  • 109
    • 79959955993 scopus 로고    scopus 로고
    • Cancer therapeutic agents targeting hypoxia-inducible factor-1
    • Wang, R.; Zhou, S.; Li, S. Cancer therapeutic agents targeting hypoxia-inducible factor-1. Curr. Med. Chem. 2011, 18, 3168-3189.
    • (2011) Curr. Med. Chem. , vol.18 , pp. 3168-3189
    • Wang, R.1    Zhou, S.2    Li, S.3
  • 110
    • 84883289329 scopus 로고    scopus 로고
    • Effects of the HIF1 inhibitor, echinomycin, on growth and NOTCH signalling in leukaemia cells
    • Yonekura, S.; Itoh, M.; Okuhashi, Y.; Takahashi, Y.; Ono, A.; Nara, N.; Tohda, S. Effects of the HIF1 inhibitor, echinomycin, on growth and NOTCH signalling in leukaemia cells. Anticancer Res. 2013, 33, 3099-3103.
    • (2013) Anticancer Res. , vol.33 , pp. 3099-3103
    • Yonekura, S.1    Itoh, M.2    Okuhashi, Y.3    Takahashi, Y.4    Ono, A.5    Nara, N.6    Tohda, S.7
  • 111
    • 84875228064 scopus 로고    scopus 로고
    • Echinomycin in the prevention of heterotopic ossification - An experimental antibiotic agent shows promising results in a murine model
    • Zimmermann, S.M.; Würgler-Hauri, C.C.; Wanner, G.A.; Simmen, H.P.; Werner, C.M. Echinomycin in the prevention of heterotopic ossification - An experimental antibiotic agent shows promising results in a murine model. Injury 2013, 44, 570-575.
    • (2013) Injury , vol.44 , pp. 570-575
    • Zimmermann, S.M.1    Würgler-Hauri, C.C.2    Wanner, G.A.3    Simmen, H.P.4    Werner, C.M.5
  • 112
    • 33845872560 scopus 로고    scopus 로고
    • The short-term effects on restenosis and thrombosis of echinomycin-eluting stents topcoated with a hydrophobic heparin-containing polymer
    • DOI 10.1016/j.biomaterials.2006.11.020, PII S0142961206009860
    • Lee, Y.K.; Hyung Park, J.; Tae Moon, H.; Yun Lee, D.; Han Yun, J.; Byun, Y. The short-term effects on restenosis and thrombosis of echinomycin-eluting stents topcoated with a hydrophobic heparin-containing polymer. Biomaterials 2007, 28, 1523-1530. (Pubitemid 46027247)
    • (2007) Biomaterials , vol.28 , Issue.8 , pp. 1523-1530
    • Lee, Y.-K.1    Hyung, P.J.2    Tae, M.H.3    Yun, L.D.4    Han, Y.J.5    Byun, Y.6
  • 116
    • 0023582091 scopus 로고
    • In vivo characterization of P388 leukemia resistant to mitomycin C
    • Rose, W.C.; Huftalen, J.B.; Bradner, W.T.; Schurig, J.E. In vivo characterization of P388 leukemia resistant to mitomycin C. In Vivo 1987, 1, 47-52. (Pubitemid 18028316)
    • (1987) In Vivo , vol.1 , Issue.1 , pp. 47-52
    • Rose, W.C.1    Huftalen, J.B.2    Bradner, W.T.3    Schurig, J.E.4
  • 117
    • 0022642441 scopus 로고
    • Effects of luzopeptins on protein B23 translocation and ribosomal RNA synthesis in HeLa cells
    • Yung, B.Y.; Busch, H.; Chan, P.K. Effects of luzopeptins on protein B23 translocation and ribosomal RNA synthesis in HeLa cells. Cancer Res. 1986, 46, 922-925.
    • (1986) Cancer Res. , vol.46 , pp. 922-925
    • Yung, B.Y.1    Busch, H.2    Chan, P.K.3
  • 118
    • 0027422826 scopus 로고
    • In vitro sensitivity of Plasmodium falciparum to drugs that bind DNA or inhibit its synthesis
    • DOI 10.2307/3283622
    • Lee, S.; Inselburg, J. In vitro sensitivity of Plasmodium falciparum to drugs that bind DNA or inhibit its synthesis. J. Parasitol. 1993, 79, 780-782. (Pubitemid 23333675)
    • (1993) Journal of Parasitology , vol.79 , Issue.5 , pp. 780-782
    • Lee, S.1    Inselburg, J.2
  • 119
    • 0023146062 scopus 로고
    • Screening for inhibitors of avian myeloblastosis virus reverse transcriptase and effect on the replication of AIDS-virus
    • Inouye, Y.; Take, Y.; Nakamura, S.; Nakashima, H.; Yamamoto, N.; Kawaguchi, H. Screening for inhibitors of avian myeloblastosis virus reverse transcriptase and effect on the replication of AIDS-virus. J. Antibiot. 1987, 40, 100-104.
    • (1987) J. Antibiot. , vol.40 , pp. 100-104
    • Inouye, Y.1    Take, Y.2    Nakamura, S.3    Nakashima, H.4    Yamamoto, N.5    Kawaguchi, H.6
  • 121
    • 84896771341 scopus 로고    scopus 로고
    • Total Synthesis of Sandramycin and Its Analogues via a Multicomponent Assemblage
    • Katayama, K.; Nakagawa, K.; Takeda, H.; Matsuda, A.; Ichikawa, S. Total Synthesis of Sandramycin and Its Analogues via a Multicomponent Assemblage. Org. Lett. 2014, 16, 428-431.
    • (2014) Org. Lett. , vol.16 , pp. 428-431
    • Katayama, K.1    Nakagawa, K.2    Takeda, H.3    Matsuda, A.4    Ichikawa, S.5
  • 122
    • 84890962563 scopus 로고    scopus 로고
    • Total synthesis of quinaldopeptin and its analogues
    • Ichikawa, S.; Okamura, T.; Matsuda, A. Total synthesis of quinaldopeptin and its analogues. J. Org. Chem. 2013, 78, 12662-12670.
    • (2013) J. Org. Chem. , vol.78 , pp. 12662-12670
    • Ichikawa, S.1    Okamura, T.2    Matsuda, A.3
  • 125
    • 0346729859 scopus 로고    scopus 로고
    • Synthesis and biological activity of new quinoxaline antibiotics of echinomycin analogues
    • DOI 10.1016/j.bmcl.2003.09.086
    • Kim, Y.B.; Kim, Y.H.; Park, J.Y.; Kim, S.K. Synthesis and biological activity of new quinoxaline antibiotics of echinomycin analogues. Bioorg. Med. Chem. Lett. 2004, 14, 541-544. (Pubitemid 38045163)
    • (2004) Bioorganic and Medicinal Chemistry Letters , vol.14 , Issue.2 , pp. 541-544
    • Kim, Y.B.1    Kim, Y.H.2    Park, J.Y.3    Kim, S.K.4
  • 126
    • 78651493376 scopus 로고    scopus 로고
    • Towards echinomycin mimetics by grafting quinoxaline residues on glycophane scaffolds
    • Jarikote, D.V.; Li, W.; Jiang, T.; Eriksson, L.A.; Murphy, P.V. Towards echinomycin mimetics by grafting quinoxaline residues on glycophane scaffolds. Bioorg. Med. Chem. 2011, 19, 826-835.
    • (2011) Bioorg. Med. Chem. , vol.19 , pp. 826-835
    • Jarikote, D.V.1    Li, W.2    Jiang, T.3    Eriksson, L.A.4    Murphy, P.V.5
  • 127
    • 0019139347 scopus 로고
    • Binding of quinoline analogues of echinomycin to deoxyribonucleic acid. Role of the chromophores
    • Fox, K.R.; Gauvreau, D.; Goodwin, D.C.; Waring, M.J. Binding of quinoline analogues of echinomycin to deoxyribonucleic acid. Role of the chromophores. Biochem. J. 1980, 191, 729-742. (Pubitemid 11223632)
    • (1980) Biochemical Journal , vol.191 , Issue.3 , pp. 729-742
    • Fox, K.R.1    Gauvreau, D.2    Goodwin, D.C.3    Waring, M.J.4
  • 128
    • 0020655921 scopus 로고
    • Preparation and DNA-binding properties of substituted triostin antibiotics
    • Cornish, A.; Fox, K.R.; Waring, M.J. Preparation and DNA-binding properties of substituted triostin antibiotics. Antimicrob. Agents Chemother. 1983, 23, 221-231. (Pubitemid 13137527)
    • (1983) Antimicrobial Agents and Chemotherapy , vol.23 , Issue.2 , pp. 221-231
    • Cornish, A.1    Fox, K.R.2    Waring, M.J.3
  • 131
    • 54349091308 scopus 로고    scopus 로고
    • Protection by conformationally restricted mobility: First solid-phase synthesis of triostin A
    • Tulla-Puche, J.; Marcucci, E.; Fermin, M.; Bayó-Puxan, N.; Albericio, F. Protection by conformationally restricted mobility: First solid-phase synthesis of triostin A. Chemistry 2008, 14, 4475-4478.
    • (2008) Chemistry , vol.14 , pp. 4475-4478
    • Tulla-Puche, J.1    Marcucci, E.2    Fermin, M.3    Bayó-Puxan, N.4    Albericio, F.5
  • 133
    • 84892606540 scopus 로고    scopus 로고
    • Thioester bonds in thiocoraline can be replaced with NMe-amide bridges without affecting its DNA-binding properties
    • Zamudio-Vázquez, R.; Albericio, F.; Tulla-Puche, J.; Fox, K.R. Thioester bonds in thiocoraline can be replaced with NMe-amide bridges without affecting its DNA-binding properties. Med. Chem. Lett. 2014, 5, 45-50.
    • (2014) Med. Chem. Lett. , vol.5 , pp. 45-50
    • Zamudio-Vázquez, R.1    Albericio, F.2    Tulla-Puche, J.3    Fox, K.R.4
  • 135
    • 84880180995 scopus 로고    scopus 로고
    • Orthogonal Chemistry for the Synthesis of Thiocoraline-Triostin Hybrids. Exploring their Structure-Activity Relationship
    • Tulla-Puche, J.; Auriemma, S.; Falciani, C.; Albericio, F. Orthogonal Chemistry for the Synthesis of Thiocoraline-Triostin Hybrids. Exploring their Structure-Activity Relationship. J. Med. Chem. 2013, 56, 5587-5600.
    • (2013) J. Med. Chem. , vol.56 , pp. 5587-5600
    • Tulla-Puche, J.1    Auriemma, S.2    Falciani, C.3    Albericio, F.4
  • 138
    • 65349153338 scopus 로고    scopus 로고
    • Diversification of echinomycin molecular structure by way of chemoenzymatic synthesis and heterologous expression of the engineered echinomycin biosynthetic pathway
    • Watanabe, K.; Oguri, H.; Oikawa, H. Diversification of echinomycin molecular structure by way of chemoenzymatic synthesis and heterologous expression of the engineered echinomycin biosynthetic pathway. Curr. Opin. Chem. Biol. 2009, 13, 189-196.
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 189-196
    • Watanabe, K.1    Oguri, H.2    Oikawa, H.3
  • 139
    • 33846998668 scopus 로고    scopus 로고
    • Robust platform for de novo production of heterologous polyketides and nonribosomal peptides in Escherichia coli
    • Watanabe, K.; Oikawa, H. Robust platform for de novo production of heterologous polyketides and nonribosomal peptides in Escherichia coli. Org. Biomol. Chem. 2007, 5, 593-602.
    • (2007) Org. Biomol. Chem. , vol.5 , pp. 593-602
    • Watanabe, K.1    Oikawa, H.2
  • 140
    • 38949101150 scopus 로고    scopus 로고
    • Improved production of triostin A in engineered Escherichia coli with furnished quinoxaline chromophore by design of experiments in small-scale culture
    • DOI 10.1021/bp070298y
    • Praseuth, A.P.; Praseuth, M.B.; Oguri, H.; Oikawa, H.; Watanabe, K.; Wang, C.C. Improved production of triostin A in engineered Escherichia coli with furnished quinoxaline chromophore by design of experiments in small-scale culture. Biotechnol. Prog. 2008, 24, 134-139. (Pubitemid 351231258)
    • (2008) Biotechnology Progress , vol.24 , Issue.1 , pp. 134-139
    • Praseuth, A.P.1    Praseuth, M.B.2    Oguri, H.3    Oikawa, H.4    Watanabe, K.5    Wang, C.C.C.6


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