메뉴 건너뛰기




Volumn 49, Issue 2, 2006, Pages 684-692

Structure-activity study of brassinin derivatives as indoleamine 2,3-dioxygenase inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

1 METHYLTRYPTOPHAN; BRASSININ; BRASSININ DERIVATIVE; INDOLEAMINE 2,3 DIOXYGENASE INHIBITOR; NATURAL PRODUCT; TRYPTOPHAN DERIVATIVE; UNCLASSIFIED DRUG;

EID: 31544482454     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm0508888     Document Type: Article
Times cited : (171)

References (64)
  • 1
    • 16244408626 scopus 로고    scopus 로고
    • Inhibition of indoleamine 2,3-dioxygenase, an immunoregulatory target of the cancer suppression gene Bin1, potentiates cancer chemotherapy
    • (a) Muller, A. J.; DuHadaway, J. B.; Donover, P. S.; Sutanto-Ward, E.; Prendergast, G. C. Inhibition of indoleamine 2,3-dioxygenase, an immunoregulatory target of the cancer suppression gene Bin1, potentiates cancer chemotherapy. Nat. Med. 2005, 11, 312-319.
    • (2005) Nat. Med. , vol.11 , pp. 312-319
    • Muller, A.J.1    DuHadaway, J.B.2    Donover, P.S.3    Sutanto-Ward, E.4    Prendergast, G.C.5
  • 2
    • 0842286646 scopus 로고    scopus 로고
    • IDO and tolerance to tumors
    • (b) Munn, D. H.; Mellor, A. L. IDO and tolerance to tumors. Trends Mol. Med. 2004, 10, 15-18.
    • (2004) Trends Mol. Med. , vol.10 , pp. 15-18
    • Munn, D.H.1    Mellor, A.L.2
  • 3
    • 0142137237 scopus 로고    scopus 로고
    • Evidence for a tumoral immune resistance mechanism based on tryptophan degradation by indoleamine 2,3-dioxygenase
    • (c) Uyttenhove, C.; Pilotte, L.; Theate, I.; Stroobant, V.; Colau, D.; Parmentier, N.; Boon, T.; Van den Eynde, B. J. Evidence for a tumoral immune resistance mechanism based on tryptophan degradation by indoleamine 2,3-dioxygenase. Nat. Med. 2003, 9, 1269-1274.
    • (2003) Nat. Med. , vol.9 , pp. 1269-1274
    • Uyttenhove, C.1    Pilotte, L.2    Theate, I.3    Stroobant, V.4    Colau, D.5    Parmentier, N.6    Boon, T.7    Van Den Eynde, B.J.8
  • 6
    • 0029497024 scopus 로고
    • Chemistry and neurochemistry of the kynurenine pathway of tryptophan metabolism
    • (b) Botting, N. P. Chemistry and neurochemistry of the kynurenine pathway of tryptophan metabolism. Chem. Soc. Rev. 1995, 401-412.
    • (1995) Chem. Soc. Rev. , pp. 401-412
    • Botting, N.P.1
  • 7
    • 31544472763 scopus 로고
    • The reaction mechanism of indoleamine 2,3-dioxygenase
    • (c) Sono, M.; Hayaishi, O. The reaction mechanism of indoleamine 2,3-dioxygenase. Biochem. Rev. 1980, 50, 173-181.
    • (1980) Biochem. Rev. , vol.50 , pp. 173-181
    • Sono, M.1    Hayaishi, O.2
  • 8
    • 0019332211 scopus 로고
    • Indoleamine 2,3-dioxygenase. Equilibrium studies of the tryptophan binding to the ferric, ferrous, and CO-bound enzymes
    • (a) Sono, M.; Taniguchi, T.; Watanabe, Y.; Hayaishi, O. Indoleamine 2,3-dioxygenase. Equilibrium studies of the tryptophan binding to the ferric, ferrous, and CO-bound enzymes. J. Biol. Chem. 1980, 255, 1339-1345.
    • (1980) J. Biol. Chem. , vol.255 , pp. 1339-1345
    • Sono, M.1    Taniguchi, T.2    Watanabe, Y.3    Hayaishi, O.4
  • 9
    • 0024423857 scopus 로고
    • Effects of tryptophan and pH on the kinetics of superoxide radical binding to indoleamine 2,3-dioxygenase studied by pulse radiolysis
    • (b) Kobayashi, K.; Hayashi, K.; Sono, M. Effects of tryptophan and pH on the kinetics of superoxide radical binding to indoleamine 2,3-dioxygenase studied by pulse radiolysis. J. Biol. Chem. 1989, 264, 15280-15283.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15280-15283
    • Kobayashi, K.1    Hayashi, K.2    Sono, M.3
  • 10
    • 23644447237 scopus 로고    scopus 로고
    • Indoleamine 2,3-dioxygenase in cancer: Targeting pathological immune tolerance with small-molecule inhibitors
    • (a) Muller, A. J.; Malachowski, W. P.; Prendergast, G. C. Indoleamine 2,3-dioxygenase in cancer: Targeting pathological immune tolerance with small-molecule inhibitors. Exp. Opin. Ther. Targets 2005, 9, 831-849.
    • (2005) Exp. Opin. Ther. Targets , vol.9 , pp. 831-849
    • Muller, A.J.1    Malachowski, W.P.2    Prendergast, G.C.3
  • 11
    • 30544455181 scopus 로고    scopus 로고
    • A new cancer immunosuppression target: Indoleamine 2,3-dioxygenase (IDO). A review of the IDO mechanism, inhibition and therapeutic applications
    • (b) Malachowski, W. P.; Metz, R.; Prendergast, G. C.; Muller, A. J. A new cancer immunosuppression target: Indoleamine 2,3-dioxygenase (IDO). A review of the IDO mechanism, inhibition and therapeutic applications. Drugs Future 2005, 30, 897.
    • (2005) Drugs Future , vol.30 , pp. 897
    • Malachowski, W.P.1    Metz, R.2    Prendergast, G.C.3    Muller, A.J.4
  • 13
    • 0026347919 scopus 로고
    • 1-Methyl-DL-tryptophan, beta-(3-benzofuranyl)-DL-alanine (the oxygen analogue of tryptophan), and beta-[3-benzo[e]thienyl]-DL-alanine (the sulfur analogue of tryptophan) are competitive inhibitors of indoleamine 2,3-dioxygenase
    • (a) Cady, S. G.; Sono, M. 1-Methyl-DL-tryptophan, beta-(3-benzofuranyl)- DL-alanine (the oxygen analogue of tryptophan), and beta-[3-benzo[e]thienyl]-DL- alanine (the sulfur analogue of tryptophan) are competitive inhibitors of indoleamine 2,3-dioxygenase. Arch. Biochem. Biophys. 1991, 291, 326-333.
    • (1991) Arch. Biochem. Biophys. , vol.291 , pp. 326-333
    • Cady, S.G.1    Sono, M.2
  • 15
    • 0141920764 scopus 로고    scopus 로고
    • The synthesis and biosynthesis of phytoalexins produced by cruciferous plants
    • (a) Pedras, M. S. C.; Jha, M.; Ahiahonu, P. W. K. The synthesis and biosynthesis of phytoalexins produced by cruciferous plants. Curr. Org. Chem. 2003, 7, 635-1647.
    • (2003) Curr. Org. Chem. , vol.7 , pp. 635-1647
    • Pedras, M.S.C.1    Jha, M.2    Ahiahonu, P.W.K.3
  • 16
    • 1042291119 scopus 로고    scopus 로고
    • Tryptophan-derived sulfur-containing phytoalexins: A general overview
    • (b) Ruszkowska, J.; Wrobel, J. T. Tryptophan-derived sulfur-containing phytoalexins: A general overview. Adv. Exp. Med. Biol. 2003, 527, 629-636.
    • (2003) Adv. Exp. Med. Biol. , vol.527 , pp. 629-636
    • Ruszkowska, J.1    Wrobel, J.T.2
  • 17
    • 0033979455 scopus 로고    scopus 로고
    • Phytoalexins from crucifers: Synthesis, biosynthesis, and biotransformation
    • (c) Pedras, M. S. C.; Okanga, F. I.; Zaharia, I. L.; Khan, A. Q. Phytoalexins from crucifers: Synthesis, biosynthesis, and biotransformation. Phytochemistry 2000, 53, 161-176.
    • (2000) Phytochemistry , vol.53 , pp. 161-176
    • Pedras, M.S.C.1    Okanga, F.I.2    Zaharia, I.L.3    Khan, A.Q.4
  • 18
    • 14544308311 scopus 로고    scopus 로고
    • Concise syntheses of the crciferous phytoalexins brassilexin, sinalexin, wasalexins and analogues: Expanding the scope of the vilsmeier formylation
    • (a) Pedras, M. S. C.; Jha, M. Concise syntheses of the crciferous phytoalexins brassilexin, sinalexin, wasalexins and analogues: Expanding the scope of the vilsmeier formylation. J. Org. Chem. 2005, 70, 1828-1834.
    • (2005) J. Org. Chem. , vol.70 , pp. 1828-1834
    • Pedras, M.S.C.1    Jha, M.2
  • 19
    • 0031646361 scopus 로고    scopus 로고
    • Phytoalexin accumulation and antifungal compunds from the crucifer wasabi
    • (b) Pedras, M. S. C.; Sorenson, J. L. Phytoalexin accumulation and antifungal compunds from the crucifer wasabi. Phytochemistry 1998, 49, 1959-1963.
    • (1998) Phytochemistry , vol.49 , pp. 1959-1963
    • Pedras, M.S.C.1    Sorenson, J.L.2
  • 21
    • 0141761523 scopus 로고    scopus 로고
    • Antiproliferative and cancer chemopreventive activity of phytoalexins: Focus on indole phytoalexins from crucifers
    • (b) Mezencev, R.; Mojzis, J.; Pilatova, M.; Kutschy, P. Antiproliferative and cancer chemopreventive activity of phytoalexins: Focus on indole phytoalexins from crucifers. Neoplasma 2003, 50, 239-245.
    • (2003) Neoplasma , vol.50 , pp. 239-245
    • Mezencev, R.1    Mojzis, J.2    Pilatova, M.3    Kutschy, P.4
  • 22
    • 0000453259 scopus 로고
    • Simple synthesis of 3-substituted indoles and their application for high yield carbon-14 labeling
    • (a) Schallenberg, J.; Meyer, E. Simple synthesis of 3-substituted indoles and their application for high yield carbon-14 labeling. Z. Naturforsch. 1983, 38b, 108-112.
    • (1983) Z. Naturforsch. , vol.38 B , pp. 108-112
    • Schallenberg, J.1    Meyer, E.2
  • 23
    • 0001760206 scopus 로고
    • A synthesis method of indole-3-methanamine and/or gramine from indole-3-carboxaldehyde, and its application for the syntheses of brassinin, its 4-substituted analogues, and 1,3,4,5-tetrahdyropyrrolo[4,3,2-de]quinoline
    • (b) Yamada, F.; Kobayashi, K.; Shimizu, A.; Aoki, N.; Somei, M. A synthesis method of indole-3-methanamine and/or gramine from indole-3-carboxaldehyde, and its application for the syntheses of brassinin, its 4-substituted analogues, and 1,3,4,5-tetrahdyropyrrolo[4,3,2-de]quinoline. Heterocycles 1993, 36, 2783-2804.
    • (1993) Heterocycles , vol.36 , pp. 2783-2804
    • Yamada, F.1    Kobayashi, K.2    Shimizu, A.3    Aoki, N.4    Somei, M.5
  • 25
    • 0036881621 scopus 로고    scopus 로고
    • Intramolecular Mannich reaction of 2-oxotryptamine and homologues with oxo reagents yielding spiro compounds. Part II
    • Dornyei, G.; Incze, M,; Kajtar-Peredy, M.; Szantgay, C. Intramolecular Mannich reaction of 2-oxotryptamine and homologues with oxo reagents yielding spiro compounds. Part II. Collect. Czech. Chem. Commun. 2002, 67, 1669-1680.
    • (2002) Collect. Czech. Chem. Commun. , vol.67 , pp. 1669-1680
    • Dornyei, G.1    Incze, M.2    Kajtar-Peredy, M.3    Szantgay, C.4
  • 26
    • 31544439009 scopus 로고
    • Antimalarials. Aliphatic amino ketones and alcohols
    • Lutz, R. E.; Wilson, J. W. Antimalarials. Aliphatic amino ketones and alcohols. J. Org. Chem. 1947, 12, 767-770.
    • (1947) J. Org. Chem. , vol.12 , pp. 767-770
    • Lutz, R.E.1    Wilson, J.W.2
  • 27
    • 0742320254 scopus 로고    scopus 로고
    • Rhodium-(II) catalyzed intramolecular insertion of carbenoids derived from 2-pyrrolyl and 3-indolyl α-diazo-β-ketoesters and α-diazoketones
    • Cuevas-Yanez, E.; Muchowski, J. M.; Cruz-Almanza, R. Rhodium-(II) catalyzed intramolecular insertion of carbenoids derived from 2-pyrrolyl and 3-indolyl α-diazo-β-ketoesters and α-diazoketones. Tetrahedron 2004, 60, 1505-1511,
    • (2004) Tetrahedron , vol.60 , pp. 1505-1511
    • Cuevas-Yanez, E.1    Muchowski, J.M.2    Cruz-Almanza, R.3
  • 29
    • 0024581581 scopus 로고
    • The roles of superoxide anion and methylene blue in the reductive activation of indoleamine 2,3-dioxygenase by ascorbic acid or by xanthine oxidase-hypoxanthine
    • Sono, M. The roles of superoxide anion and methylene blue in the reductive activation of indoleamine 2,3-dioxygenase by ascorbic acid or by xanthine oxidase-hypoxanthine. J. Biol. Chem. 1989, 264, 1616-1622.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1616-1622
    • Sono, M.1
  • 30
    • 0017645082 scopus 로고
    • Indoleamine 2,3-dioxygenase: Potassium superoxide as substrate
    • Ohnishi, T.; Hirata, F.; Hayaishi, O. Indoleamine 2,3-dioxygenase: Potassium superoxide as substrate. J. Biol. Chem. 1977, 252, 4643-4647.
    • (1977) J. Biol. Chem. , vol.252 , pp. 4643-4647
    • Ohnishi, T.1    Hirata, F.2    Hayaishi, O.3
  • 31
    • 0035873436 scopus 로고    scopus 로고
    • Antioxidnnts inhibit indoleamine 2,3-dioxygenase in IFN-g-activated human macrophages: Posttranslational regulation by pyrrolidine dithiocarbamate
    • For leading examples of metalloenzyme inhibition by a dithiocarbamate, see (a) Thomas, S. R.; Salahifar, H.; Mashima, R.; Hunt, N. H.; Richardson, D. R.; Stocker, R. Antioxidnnts inhibit indoleamine 2,3-dioxygenase in IFN-g-activated human macrophages: Posttranslational regulation by pyrrolidine dithiocarbamate. J. Immunol. 2001, 166, 6332-6340.
    • (2001) J. Immunol. , vol.166 , pp. 6332-6340
    • Thomas, S.R.1    Salahifar, H.2    Mashima, R.3    Hunt, N.H.4    Richardson, D.R.5    Stocker, R.6
  • 32
    • 0035807147 scopus 로고    scopus 로고
    • Copper-specific chelators as synergists to herbicides: I. Amphiphilic dithiocarbamates, synthesis, transport through lipid bilayers, and inhibition of Cu/Zn superoxide dismutase activity
    • (b) Warshawsky, A.; Rogachev, I.; Patil, Y.; Baszkin, A.; Weiner, L.; Gressel, J. Copper-specific chelators as synergists to herbicides: I. Amphiphilic dithiocarbamates, synthesis, transport through lipid bilayers, and inhibition of Cu/Zn superoxide dismutase activity. Langmuir 2001, 17, 5621-5635.
    • (2001) Langmuir , vol.17 , pp. 5621-5635
    • Warshawsky, A.1    Rogachev, I.2    Patil, Y.3    Baszkin, A.4    Weiner, L.5    Gressel, J.6
  • 33
    • 0034119438 scopus 로고    scopus 로고
    • Metabolism of 3-methylindole by porcine liver microsomes: Responsible cytochrome P450 enzymes
    • (c) Diaz, G. J.; Squires, E. J. Metabolism of 3-methylindole by porcine liver microsomes: Responsible cytochrome P450 enzymes. Toxicol Sci. 2000, 55, 284-292.
    • (2000) Toxicol. Sci. , vol.55 , pp. 284-292
    • Diaz, G.J.1    Squires, E.J.2
  • 34
    • 0037193066 scopus 로고    scopus 로고
    • Micelle mediated methodology for the determination of free and bound iron in wines by flame atomic absorption spectrometry
    • For general leading references on metal chelation by dithiocarbamates, see (a) Paleologos, E. K.; Giokas, D. L.; Tzouwara-Karayanni, S. M.; Karayannis, M. I. Micelle mediated methodology for the determination of free and bound iron in wines by flame atomic absorption spectrometry. Anal. Chim. Acta 2002, 485, 241-248.
    • (2002) Anal. Chim. Acta , vol.485 , pp. 241-248
    • Paleologos, E.K.1    Giokas, D.L.2    Tzouwara-Karayanni, S.M.3    Karayannis, M.I.4
  • 35
    • 0036683674 scopus 로고    scopus 로고
    • Copper uptake is required for pyrrolidine dithiocarbamate-mediated oxidation and protein level increase of p53 in cells
    • (b) Furuta, S.; Ortiz, F.; Sun, X. Z.; Wu, H.-H.; Mason, A.; Momand, J. Copper uptake is required for pyrrolidine dithiocarbamate-mediated oxidation and protein level increase of p53 in cells. Biochem. J. 2002, 365, 639-648.
    • (2002) Biochem. J. , vol.365 , pp. 639-648
    • Furuta, S.1    Ortiz, F.2    Sun, X.Z.3    Wu, H.-H.4    Mason, A.5    Momand, J.6
  • 36
    • 0034675345 scopus 로고    scopus 로고
    • Pyrrolidine dithiocarbamate inhibits TNF-α-dependent activation of NP-kB by increasing intracellular copper level in human aortic smooth muscle cells
    • (c) Iseki, A,; Kambe, F.; Okumura, K.; Miwata, S.; Yamamoto, R.; Hayakawa, T.; Seo, H. Pyrrolidine dithiocarbamate inhibits TNF-α-dependent activation of NP-kB by increasing intracellular copper level in human aortic smooth muscle cells. Biochem. Biophys. Res. Commun. 2000, 276, 88-92.
    • (2000) Biochem. Biophys. Res. Commun. , vol.276 , pp. 88-92
    • Iseki, A.1    Kambe, F.2    Okumura, K.3    Miwata, S.4    Yamamoto, R.5    Hayakawa, T.6    Seo, H.7
  • 37
    • 0000852065 scopus 로고    scopus 로고
    • Pyrrolidine dithiocarbamate induces bovine cerebral endothelial cell death by increasing the intracellular zinc level
    • (d) Kim, C. H.; Kim, J. H.; Xu, J.; Hsu, C. Y.; Ahn, Y. S. Pyrrolidine dithiocarbamate induces bovine cerebral endothelial cell death by increasing the intracellular zinc level. J. Neurochem. 1999, 72, 1586-1592.
    • (1999) J. Neurochem. , vol.72 , pp. 1586-1592
    • Kim, C.H.1    Kim, J.H.2    Xu, J.3    Hsu, C.Y.4    Ahn, Y.S.5
  • 38
    • 0017397028 scopus 로고
    • Intracellular utilization of superoxide anion by indoleamine 2,3-dioxygenase of rabbit enterocytes
    • Interestingly, there is a report of IDO acceleration in the presence of diethyldithiocarbamate. The acceleration results from inhibition of superoxide dismutase, which can remove superoxide, an IDO activator, Tanigucchi, T.; Hirata, F.; Hayaishi, O. Intracellular utilization of superoxide anion by indoleamine 2,3-dioxygenase of rabbit enterocytes. J. Biol. Chem. 1977, 252, 2774-2776.
    • (1977) J. Biol. Chem. , vol.252 , pp. 2774-2776
    • Tanigucchi, T.1    Hirata, F.2    Hayaishi, O.3
  • 39
    • 7244259205 scopus 로고    scopus 로고
    • Pyrrolidine dithiocarbamate inhibits translocation of nuclear factor kappa-B in neurons and protects against brain ischemia with a wide therapeutic time window
    • (a) Nurmi, A.; Vartiainen, N.; Pihlaja, R.; Goldsteins, G.; Yrjaenheikki, J.; Koistinaho, J. Pyrrolidine dithiocarbamate inhibits translocation of nuclear factor kappa-B in neurons and protects against brain ischemia with a wide therapeutic time window. J. Neurochem. 2004, 91, 755-765.
    • (2004) J. Neurochem. , vol.91 , pp. 755-765
    • Nurmi, A.1    Vartiainen, N.2    Pihlaja, R.3    Goldsteins, G.4    Yrjaenheikki, J.5    Koistinaho, J.6
  • 41
    • 0031572429 scopus 로고    scopus 로고
    • In vivo inhibition of nuclear factor-B activation prevents inducible nitric oxide synthase expression and systemic hypotension in a rat model of septic shock
    • (c) Liu, S. F.; Ye, X.; Malik, A. B. In vivo inhibition of nuclear factor-B activation prevents inducible nitric oxide synthase expression and systemic hypotension in a rat model of septic shock. J. Immunol. 1997, 159, 3976-3983.
    • (1997) J. Immunol. , vol.159 , pp. 3976-3983
    • Liu, S.F.1    Ye, X.2    Malik, A.B.3
  • 43
    • 0026590541 scopus 로고
    • Dithiocarbamates as potent inhibitors of nuclear factor B activation in intact cells
    • (e) Schreck, R.; Meier, B.; Mannel, D. N.; Droge, W.; Baeuerle, P. A. Dithiocarbamates as potent inhibitors of nuclear factor B activation in intact cells. J. Exp. Med. 1992, 175, 1181-1194.
    • (1992) J. Exp. Med. , vol.175 , pp. 1181-1194
    • Schreck, R.1    Meier, B.2    Mannel, D.N.3    Droge, W.4    Baeuerle, P.A.5
  • 44
    • 31544466135 scopus 로고    scopus 로고
    • note
    • Calculations with 1 and 22 showed an almost identical change (slightly more negative) in ESP and NBO charges vs 32 and 33.
  • 45
    • 0345114077 scopus 로고
    • Hard and soft acids and bases
    • Pearson, R. G. Hard and soft acids and bases. J. Am. Chem. Soc. 1963, 85, 3533-3539.
    • (1963) J. Am. Chem. Soc. , vol.85 , pp. 3533-3539
    • Pearson, R.G.1
  • 46
    • 0024332546 scopus 로고
    • Enzyme kinetic and spectroscopic studies of inhibitor and effector interactions with indoleamine 2,3-dioxygenase. 1. Norharman and 4-phenylimidazole binding to the enzyme as inhibitors and heme ligands
    • Sono, M.; Cady, S. G. Enzyme kinetic and spectroscopic studies of inhibitor and effector interactions with indoleamine 2,3-dioxygenase. 1. Norharman and 4-phenylimidazole binding to the enzyme as inhibitors and heme ligands. Biochemistry 1989, 28, 5392-5399.
    • (1989) Biochemistry , vol.28 , pp. 5392-5399
    • Sono, M.1    Cady, S.G.2
  • 47
    • 0001204586 scopus 로고
    • Rotational barrier in dithiocarbamate esters
    • Holloway, C. E.; Gitlitz, M. H. Rotational barrier in dithiocarbamate esters. Can. J. Chem. 1967, 45, 2659-2663.
    • (1967) Can. J. Chem. , vol.45 , pp. 2659-2663
    • Holloway, C.E.1    Gitlitz, M.H.2
  • 48
    • 0000570827 scopus 로고
    • Novel sulfur-containing phytoalexins from the Chinese cabbage Brassica campestris L. ssp. pekinensis (Cruciferae)
    • Takasugi, M.; Monde, K.; Katsui, N.; Shirata, A. Novel sulfur-containing phytoalexins from the Chinese cabbage Brassica campestris L. ssp. pekinensis (Cruciferae). Bull. Chem. Soc. Jpn. 1988, 61, 285-289.
    • (1988) Bull. Chem. Soc. Jpn. , vol.61 , pp. 285-289
    • Takasugi, M.1    Monde, K.2    Katsui, N.3    Shirata, A.4
  • 49
    • 0001645281 scopus 로고    scopus 로고
    • Probing the phytopathogenic blackleg fungus with a phytoalexin homolog
    • (a) Pedras, M. S. C.; Okanga, F. I. Probing the phytopathogenic blackleg fungus with a phytoalexin homolog. J. Org. Chem. 1998, 63, 416-417.
    • (1998) J. Org. Chem. , vol.63 , pp. 416-417
    • Pedras, M.S.C.1    Okanga, F.I.2
  • 50
    • 0034011327 scopus 로고    scopus 로고
    • Metabolism of analogues of the phytoalexin brassinin by plant pathogenic fungi
    • (b) Pedras, M. S. C.; Okanga, F. I. Metabolism of analogues of the phytoalexin brassinin by plant pathogenic fungi. Can. J. Chem. 2000, 78, 338-346.
    • (2000) Can. J. Chem. , vol.78 , pp. 338-346
    • Pedras, M.S.C.1    Okanga, F.I.2
  • 51
    • 4644340309 scopus 로고    scopus 로고
    • Detoxification of the cruciferous phytoalexin brassinin in sclerotinia sclerotiorum requires an inducible glucosyltransferase
    • Pedras, M. S. C.; Ahiahonu, P. W. K.; Hossain, M. Detoxification of the cruciferous phytoalexin brassinin in sclerotinia sclerotiorum requires an inducible glucosyltransferase. Phytochemistry 2004, 65, 2685-2694.
    • (2004) Phytochemistry , vol.65 , pp. 2685-2694
    • Pedras, M.S.C.1    Ahiahonu, P.W.K.2    Hossain, M.3
  • 52
    • 0034695535 scopus 로고    scopus 로고
    • 1-(Methyldithiocarbonyl)imidazole: A useful thiocarbonyl transfer reagent for synthesis of substituted thioureas
    • (a) Mohanta, P. K.; Dhar, S.; Samal, S. K.; Ila, H.; Junjappa, H. 1-(Methyldithiocarbonyl)imidazole: A useful thiocarbonyl transfer reagent for synthesis of substituted thioureas. Tetrahedron 2000, 56, 629-637.
    • (2000) Tetrahedron , vol.56 , pp. 629-637
    • Mohanta, P.K.1    Dhar, S.2    Samal, S.K.3    Ila, H.4    Junjappa, H.5
  • 53
    • 37049173147 scopus 로고
    • The associating effect of the hydrogen atom. XV. The S-H-N bond. Esters of thion- and dithiocarbamic acids
    • (b) Burrows, A. A.; Hunter, L. The associating effect of the hydrogen atom. XV. The S-H-N bond. Esters of thion- and dithiocarbamic acids. J. Chem. Soc., Abstr. 1952, 4118-4122.
    • (1952) J. Chem. Soc., Abstr. , pp. 4118-4122
    • Burrows, A.A.1    Hunter, L.2
  • 55
    • 0028836030 scopus 로고
    • Three sulphur-containing stress metabolites from Japanese radish
    • Monde, K.; Takasugi, M.; Shirata, A. Three sulphur-containing stress metabolites from Japanese radish. Phytochemistry 1995, 39, 581-586.
    • (1995) Phytochemistry , vol.39 , pp. 581-586
    • Monde, K.1    Takasugi, M.2    Shirata, A.3
  • 56
    • 0000971081 scopus 로고
    • A new synthesis of the thiazole fragment of vitamin B1
    • Londergan, T. E.; Hause, N. L.; Schmitz, W. R. A new synthesis of the thiazole fragment of vitamin B1. J. Am. Chem. Soc. 1953, 75, 4456-4458.
    • (1953) J. Am. Chem. Soc. , vol.75 , pp. 4456-4458
    • Londergan, T.E.1    Hause, N.L.2    Schmitz, W.R.3
  • 59
    • 0011083499 scopus 로고
    • Intermolecular interactions from a natural bond orbital, donor-receptor viewpoint
    • (b) Reed, A. E.; Curtiss, L. A.; Weinhold, F. Intermolecular interactions from a natural bond orbital, donor-receptor viewpoint. Chem. Rev. 1988, 88, 899.
    • (1988) Chem. Rev. , vol.88 , pp. 899
    • Reed, A.E.1    Curtiss, L.A.2    Weinhold, F.3
  • 60
    • 33748545144 scopus 로고
    • Influence of polarization functions on MO hydrogenation energies
    • First-row elements: Hahrihan, P. C.; Pople, J. A. Influence of polarization functions on MO hydrogenation energies. Theor. Chim. Acta 1973, 28, 213.
    • (1973) Theor. Chim. Acta , vol.28 , pp. 213
    • Hahrihan, P.C.1    Pople, J.A.2
  • 61
    • 33645949559 scopus 로고
    • Self-consistent molecular orbital methods. XXIII. A polarization-type basis set for second-row elements
    • Second-row elements: Francl, M. M.; Pietro, W. J.; Hehre, W. J.; Binkley, J. S.; Defrees, D. J.; Pople, J. A.; Gordon, M. S. Self-consistent molecular orbital methods. XXIII. A polarization-type basis set for second-row elements. J. Chem. Phys. 1982, 77, 3654.
    • (1982) J. Chem. Phys. , vol.77 , pp. 3654
    • Francl, M.M.1    Pietro, W.J.2    Hehre, W.J.3    Binkley, J.S.4    Defrees, D.J.5    Pople, J.A.6    Gordon, M.S.7
  • 62
    • 84988098098 scopus 로고
    • Atomic charges derived from electrostatic potentials: A detailed study
    • (a) Chirlian, L. E.; Francl, M. M. Atomic charges derived from electrostatic potentials: A detailed study. J. Comput. Chem. 1987, 8, 894.
    • (1987) J. Comput. Chem. , vol.8 , pp. 894
    • Chirlian, L.E.1    Francl, M.M.2
  • 63
    • 84986513567 scopus 로고
    • Determining atom-centered monopoles from molecular electrostatic potentials. The need for high sampling density in formamide conformational analysis
    • (b) Breneman, C. M.; Wiberg, K. B. Determining atom-centered monopoles from molecular electrostatic potentials. The need for high sampling density in formamide conformational analysis. J. Comput. Chem. 1990, 11, 361.
    • (1990) J. Comput. Chem. , vol.11 , pp. 361
    • Breneman, C.M.1    Wiberg, K.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.