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Volumn 86, Issue 2, 2010, Pages 85-102

Recent development of two chitinase inhibitors, Argifin and Argadin, produced by soil microorganisms

Author keywords

Argadin; Argifin; Chitinase inhibitor; In situ click chemistry; Rational molecular design; Solid phase synthesis

Indexed keywords

ALGAE; FUNGI; HEXAPODA; INVERTEBRATA;

EID: 77951926872     PISSN: 03862208     EISSN: 13492896     Source Type: Journal    
DOI: 10.2183/pjab.86.85     Document Type: Review
Times cited : (37)

References (70)
  • 1
    • 0030787924 scopus 로고    scopus 로고
    • Regulation of chitin synthase activity in the dimorphic fungus Benjaminiella poitrasii by external osmotic pressure
    • Deshpande, M.V., ODonnell, R. and Gooday, G.W. (1997) Regulation of chitin synthase activity in the dimorphic fungus Benjaminiella poitrasii by external osmotic pressure. FEMS Microbiol. Lett. 152, 327-332.
    • (1997) FEMS Microbiol. Lett. , vol.152 , pp. 327-332
    • Deshpande, M.V.1    ODonnell, R.2    Gooday, G.W.3
  • 3
    • 0027308860 scopus 로고
    • Transmission-blocking activity of a chitinase inhibitor and activation of malarial parasite chitinase by mosquito protease
    • Shahabuddin, M., Toyoshima, T., Aikawa, M. and Kaslow, D.C. (1993) Transmission-blocking activity of a chitinase inhibitor and activation of malarial parasite chitinase by mosquito protease. Proc. Natl. Acad. Sci. USA 90, 4266-4270.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4266-4270
    • Shahabuddin, M.1    Toyoshima, T.2    Aikawa, M.3    Kaslow, D.C.4
  • 4
    • 0034142181 scopus 로고    scopus 로고
    • Oral administration of chitindown-regulates serum IgE levels and lung eosinophilia in the allergic mouse
    • Shibata, Y., Foster, L.A., Bradfield, J.F. and Myrvik, Q.N. (2000) Oral administration of chitindown-regulates serum IgE levels and lung eosinophilia in the allergic mouse. J. Immunol. 164, 1314-1321.
    • (2000) J. Immunol. , vol.164 , pp. 1314-1321
    • Shibata, Y.1    Foster, L.A.2    Bradfield, J.F.3    Myrvik, Q.N.4
  • 5
    • 0031866632 scopus 로고    scopus 로고
    • The molecular biology of chitin digestion
    • Cohen-Kupiec, R. and Chet, I. (1998) The molecular biology of chitin digestion. Curr. Opin. Biotechnol. 9, 270-277.
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 270-277
    • Cohen-Kupiec, R.1    Chet, I.2
  • 6
    • 2842523841 scopus 로고    scopus 로고
    • Nucleotide sequences of genes encoding allosamidin-sensitive and -insensitive chitinases produced by allosamidin-producing Streptomyces
    • Matsuura, H., Okamoto, S., Anamnart, S., Wang, Q.Q., Zhou, Z.Y., Nihira, T. et al. (2003) Nucleotide sequences of genes encoding allosamidin-sensitive and -insensitive chitinases produced by allosamidin-producing Streptomyces. Biosci. Biotechnol. Biochem. 67, 2002-2005.
    • (2003) Biosci. Biotechnol. Biochem. , vol.67 , pp. 2002-2005
    • Matsuura, H.1    Okamoto, S.2    Anamnart, S.3    Wang, Q.Q.4    Zhou, Z.Y.5    Nihira, T.6
  • 7
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino-acid-sequence similarities
    • Henrissat, B. and Bairoch, A. (1993) New families in the classification of glycosyl hydrolases based on amino-acid-sequence similarities. Biochem. J. 293, 781-788.
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 8
    • 0030595119 scopus 로고    scopus 로고
    • The 1.8 angstrom resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18
    • Terwisscha van Scheltinga, A.C., Hennig, M. and Dijkstra, B.W. (1996) The 1.8 angstrom resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18. J. Mol. Biol. 262, 243-257.
    • (1996) J. Mol. Biol. , vol.262 , pp. 243-257
    • Terwisscha van Scheltinga, A.C.1    Hennig, M.2    Dijkstra, B.W.3
  • 10
    • 33645692133 scopus 로고    scopus 로고
    • Kinetic characterization of recombinant human acidic mammalian chitinase
    • Chou, Y.-T., Yao, S., Czerwinski, R., Fleming, M., Krykbaev, R., Xuan, D. et al. (2006) Kinetic characterization of recombinant human acidic mammalian chitinase. Biochemistry 45, 4444-4454.
    • (2006) Biochemistry , vol.45 , pp. 4444-4454
    • Chou, Y.-T.1    Yao, S.2    Czerwinski, R.3    Fleming, M.4    Krykbaev, R.5    Xuan, D.6
  • 12
    • 2942668626 scopus 로고    scopus 로고
    • Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation
    • Zhu, Z., Zheng, T., Homer, R.J., Kim, Y.-K., Chen, N.Y., Cohn, L. et al. (2004) Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation. Science 304, 1678-1682.
    • (2004) Science , vol.304 , pp. 1678-1682
    • Zhu, Z.1    Zheng, T.2    Homer, R.J.3    Kim, Y.-K.4    Chen, N.Y.5    Cohn, L.6
  • 13
    • 0000602126 scopus 로고
    • The structure of allosamidin, a novel insect chitinase inhibitor, produced by Streptomyces sp
    • Sakuda, S., Isogai, A., Matsumoto, S., Suzuki A. and Koseki, K. (1986) The structure of allosamidin, a novel insect chitinase inhibitor, produced by Streptomyces sp. Tetrahedron Lett. 27, 2475-2478.
    • (1986) Tetrahedron Lett. , vol.27 , pp. 2475-2478
    • Sakuda, S.1    Isogai, A.2    Matsumoto, S.3    Suzuki, A.4    Koseki, K.5
  • 14
    • 0023110718 scopus 로고
    • Search for microbial insect growth regulators, II. Allosamidin, a novel insect chitinase inhibitor
    • Sakuda, S., Isogai, A., Matsumoto, S. and Suzuki, A. (1987) Search for microbial insect growth regulators, II. Allosamidin, a novel insect chitinase inhibitor. J. Antibiot. 40, 296-300.
    • (1987) J. Antibiot. , vol.40 , pp. 296-300
    • Sakuda, S.1    Isogai, A.2    Matsumoto, S.3    Suzuki, A.4
  • 15
    • 0028828695 scopus 로고
    • Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and x-ray structure of a complex with allosamidin evidence for substrate assisted catalysis
    • Terwisscha van Scheltinga, A.C., Armand, S., Kalk, K.H., Isogai, A., Henrissat, B. and Dijkstra, B.W. (1995) Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and x-ray structure of a complex with allosamidin evidence for substrate assisted catalysis. Biochemistry 34, 15619-15623.
    • (1995) Biochemistry , vol.34 , pp. 15619-15623
    • Terwisscha van Scheltinga, A.C.1    Armand, S.2    Kalk, K.H.3    Isogai, A.4    Henrissat, B.5    Dijkstra, B.W.6
  • 17
    • 0028936559 scopus 로고
    • Styloguanidines, new chitinase inhibitors from the marine sponge Stylotella aurantium
    • Kato, T., Shizuri, Y., Izumida, H., Yokoyama, A. and Endo, M. (1995) Styloguanidines, new chitinase inhibitors from the marine sponge Stylotella aurantium. Tetrahedron Lett. 36, 2133-2136.
    • (1995) Tetrahedron Lett. , vol.36 , pp. 2133-2136
    • Kato, T.1    Shizuri, Y.2    Izumida, H.3    Yokoyama, A.4    Endo, M.5
  • 18
    • 0030050683 scopus 로고    scopus 로고
    • A novel chitinase inhibitor from a marine bacterium, Pseudomonas sp
    • Izumida, H., Imamura, N. and Sano, H. (1996) A novel chitinase inhibitor from a marine bacterium, Pseudomonas sp. J. Antibiot. 49, 76-80.
    • (1996) J. Antibiot. , vol.49 , pp. 76-80
    • Izumida, H.1    Imamura, N.2    Sano, H.3
  • 19
    • 0029793429 scopus 로고    scopus 로고
    • The effect of chitinase inhibitors, cyclo(Arg-Pro) against cell separation of Saccharomyces cerevisiae and the morphological change of Candida albicans
    • Izumida, H., Nishijima, M., Takadera, T., Nomoto, A.M. and Sano, H. (1996) The effect of chitinase inhibitors, cyclo(Arg-Pro) against cell separation of Saccharomyces cerevisiae and the morphological change of Candida albicans. J. Antibiot. 49, 829-831.
    • (1996) J. Antibiot. , vol.49 , pp. 829-831
    • Izumida, H.1    Nishijima, M.2    Takadera, T.3    Nomoto, A.M.4    Sano, H.5
  • 20
    • 0036166502 scopus 로고    scopus 로고
    • Psammaplin A, a chitinase inhibitor isolated from the Fijian marine sponge Aplysinella rhax
    • Tabudravu, J.N., Eijsink, V.G.H, Gooday, G.W., Jaspars, M., Komander, D., Legg, M. et al. (2002) Psammaplin A, a chitinase inhibitor isolated from the Fijian marine sponge Aplysinella rhax. Bioorg. Med. Chem. 10, 1123-1128.
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 1123-1128
    • Tabudravu, J.N.1    Eijsink, V.G.H.2    Gooday, G.W.3    Jaspars, M.4    Komander, D.5    Legg, M.6
  • 21
    • 0000055673 scopus 로고
    • Phenolic constituents of Psammaplysilla
    • Quinoa, E. and Crews, P. (1987) Phenolic constituents of Psammaplysilla. Tetrahedron Lett. 28, 3229-3232.
    • (1987) Tetrahedron Lett. , vol.28 , pp. 3229-3232
    • Quinoa, E.1    Crews, P.2
  • 22
    • 0023236004 scopus 로고
    • Brominated tyrosine metabolites from an unidentified sponge
    • Arabshahi, L. and Schmitz, F.J. (1987) Brominated tyrosine metabolites from an unidentified sponge. J. Org. Chem. 52, 3584-3586.
    • (1987) J. Org. Chem. , vol.52 , pp. 3584-3586
    • Arabshahi, L.1    Schmitz, F.J.2
  • 23
    • 0011229661 scopus 로고    scopus 로고
    • (ed. Muzzarelli, R.A.A.). Atec Edizioni, Italy
    • Sampson, M.N. and Gooday, G.W. (1996) In Chitin Enzymology. Vol. 2 (ed. Muzzarelli, R.A.A.). Atec Edizioni, Italy, p. 227.
    • (1996) Chitin Enzymology , vol.2 , pp. 227
    • Sampson, M.N.1    Gooday, G.W.2
  • 25
    • 0033920903 scopus 로고    scopus 로고
    • Argifin, a new chitinase inhibitor, produced by Gliocladium sp. FTD-0668. I. Taxonomy, fermentation, and biological activities
    • Ōmura, S., Arai, N., Yamaguchi, Y., Masuma, R., Iwai, Y., Namikoshi, M. et al. (2000) Argifin, a new chitinase inhibitor, produced by Gliocladium sp. FTD-0668. I. Taxonomy, fermentation, and biological activities. J. Antibiot. 53, 603-608.
    • (2000) J. Antibiot. , vol.53 , pp. 603-608
    • Ōmura, S.1    Arai, N.2    Yamaguchi, Y.3    Masuma, R.4    Iwai, Y.5    Namikoshi, M.6
  • 26
    • 0033923739 scopus 로고    scopus 로고
    • Argifin, a new chitinase inhibitor, produced by Gliocladium sp. FTD-0668. II. Isolation, physico-chemical properties and structure elucidation
    • Arai, N., Shiomi, K., Yamaguchi, Y., Masuma, R., Iwai, Y., Namikoshi, M. et al. (2000) Argifin, a new chitinase inhibitor, produced by Gliocladium sp. FTD-0668. II. Isolation, physico-chemical properties and structure elucidation. J. Antibiot. 53, 609-614.
    • (2000) J. Antibiot. , vol.53 , pp. 609-614
    • Arai, N.1    Shiomi, K.2    Yamaguchi, Y.3    Masuma, R.4    Iwai, Y.5    Namikoshi, M.6
  • 27
    • 0034719795 scopus 로고    scopus 로고
    • Structure of argifin, a new chitinase inhibitor produced by Gliocladium sp
    • Shiomi, K., Arai, N., Iwai, Y., Turberg, A., Kölbl, H. and Ōmura, S. (2000) Structure of argifin, a new chitinase inhibitor produced by Gliocladium sp. Tetrahedron Lett. 41, 2141-2143.
    • (2000) Tetrahedron Lett. , vol.41 , pp. 2141-2143
    • Shiomi, K.1    Arai, N.2    Iwai, Y.3    Turberg, A.4    Kölbl, H.5    Omura, S.6
  • 28
    • 0037047120 scopus 로고    scopus 로고
    • High-resolution structures of a chitinase complexed with natural product cyclopentapeptide inhibitors: Mimicry of carbohydrate substrate
    • Houston, D.R., Shiomi, K., Arai, N., Ōmura, S., Peter, M.G., Turberg, A. et al. (2002) High-resolution structures of a chitinase complexed with natural product cyclopentapeptide inhibitors: mimicry of carbohydrate substrate. Proc. Natl. Acad. Sci. USA 99, 9127-9132.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9127-9132
    • Houston, D.R.1    Shiomi, K.2    Arai, N.3    Omura, S.4    Peter, M.G.5    Turberg, A.6
  • 29
    • 12344317078 scopus 로고    scopus 로고
    • Specificity and affinity of natural product cyclopentapeptide inhibitors against A. fumigatus, human, and bacterial chitinases
    • Rao, F.V., Houston, D.R., Boot, R.G., Aerts, J.M.F.G., Hodkinson, M., Adams, D.J. et al. (2005) Specificity and affinity of natural product cyclopentapeptide inhibitors against A. fumigatus, human, and bacterial chitinases. Chem. Biol. 12, 65-76.
    • (2005) Chem. Biol. , vol.12 , pp. 65-76
    • Rao, F.V.1    Houston, D.R.2    Boot, R.G.3    Aerts, J.M.F.G.4    Hodkinson, M.5    Adams, D.J.6
  • 30
    • 67649986131 scopus 로고    scopus 로고
    • Chitinase inhibitors: Extraction of the active framework from natural argifin and use of in situ click chemistry
    • Hirose, T., Sunazuka, T., Sugawara, A., Endo, A., Iguchi, K., Yamamoto, T. et al. (2009) Chitinase inhibitors: extraction of the active framework from natural argifin and use of in situ click chemistry. J. Antibiot. 62, 277-282.
    • (2009) J. Antibiot. , vol.62 , pp. 277-282
    • Hirose, T.1    Sunazuka, T.2    Sugawara, A.3    Endo, A.4    Iguchi, K.5    Yamamoto, T.6
  • 31
    • 40749152751 scopus 로고    scopus 로고
    • Structure-based dissection of the natural product cyclopentapeptide chitinase inhibitor argifin
    • Andersen, O.A., Nathubhai, A., Dixon, M.J., Eggleston, I.M. and van Aalten, D.M.F. (2008) Structure-based dissection of the natural product cyclopentapeptide chitinase inhibitor argifin. Chem. Biol. 15, 295-301.
    • (2008) Chem. Biol. , vol.15 , pp. 295-301
    • Andersen, O.A.1    Nathubhai, A.2    Dixon, M.J.3    Eggleston, I.M.4    Van Aalten, D.M.F.5
  • 32
  • 33
    • 70349603842 scopus 로고    scopus 로고
    • Solid-phase total synthesis of the chitinase inhibitor Argadin using a supported acetal resin
    • Hirose, T., Sunazuka, T., Sugawara, A., Noguchi, Y., Tanaka, T., Iguchi, K. et al. (2009) Solid-phase total synthesis of the chitinase inhibitor Argadin using a supported acetal resin. J. Antibiot. 62, 495-500.
    • (2009) J. Antibiot. , vol.62 , pp. 495-500
    • Hirose, T.1    Sunazuka, T.2    Sugawara, A.3    Noguchi, Y.4    Tanaka, T.5    Iguchi, K.6
  • 34
    • 0034956176 scopus 로고    scopus 로고
    • A new strategy for the synthesis of cyclopeptides containing diaminoglutaric acid
    • Bayer, T., Riemer, C. and Kessler, H. (2001) A new strategy for the synthesis of cyclopeptides containing diaminoglutaric acid. J. Peptide Sci. 7, 250-261.
    • (2001) J. Peptide Sci. , vol.7 , pp. 250-261
    • Bayer, T.1    Riemer, C.2    Kessler, H.3
  • 35
    • 70349597048 scopus 로고    scopus 로고
    • Preparation of amidino-urea serotonin receptor ligands
    • WO2002036554 A2 20020510
    • Hong, Y., Kuki, A., Tompkins, E.V., Peng, Z. and Luthin, D.R. (2002) Preparation of amidino-urea serotonin receptor ligands. PCT Int. Appl. WO2002036554 A2 20020510.
    • (2002) PCT Int. Appl.
    • Hong, Y.1    Kuki, A.2    Tompkins, E.V.3    Peng, Z.4    Luthin, D.R.5
  • 36
    • 25444507108 scopus 로고    scopus 로고
    • An efficient synthesis of argifin: A natural product chitinase inhibitor with chemotherapeutic potential
    • Dixon, M.J., Andersen, O.A., van Aalten, D.M.F. and Eggleston, I.M. (2005) An efficient synthesis of argifin: A natural product chitinase inhibitor with chemotherapeutic potential. Bioorg. Med. Chem. Lett. 15, 4717-4721.
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 4717-4721
    • Dixon, M.J.1    Andersen, O.A.2    Van Aalten, D.M.F.3    Eggleston, I.M.4
  • 38
    • 62949225622 scopus 로고    scopus 로고
    • Argifin; efficient solid phase total synthesis and evaluation of analogues of acyclic peptide
    • Sunazuka, T., Sugawara, A., Iguchi, K., Hirose, T., Nagai, K., Noguchi, Y. et al. (2009) Argifin; efficient solid phase total synthesis and evaluation of analogues of acyclic peptide. Bioorg. Med. Chem. 17, 2751-2758.
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 2751-2758
    • Sunazuka, T.1    Sugawara, A.2    Iguchi, K.3    Hirose, T.4    Nagai, K.5    Noguchi, Y.6
  • 39
    • 10044297245 scopus 로고    scopus 로고
    • Banyasin A and banyasides A and B, three novel modified peptides from a water bloom of the cyanobacterium Nostoc sp
    • Pluotno, A. and Carmeli, S. (2005) Banyasin A and banyasides A and B, three novel modified peptides from a water bloom of the cyanobacterium Nostoc sp. Tetrahedron 61, 575-583.
    • (2005) Tetrahedron , vol.61 , pp. 575-583
    • Pluotno, A.1    Carmeli, S.2
  • 40
    • 65349194561 scopus 로고    scopus 로고
    • Computer-aided rational molecular design of argifin-derivatives with more potent inhibitory activity against chitinase B from Serratia marcescens
    • Gouda, H., Sunazuka, T., Iguchi, K., Sugawara, A., Hirose, T., Noguchi, Y. et al. (2009) Computer-aided rational molecular design of argifin-derivatives with more potent inhibitory activity against chitinase B from Serratia marcescens. Bioorg. Med. Chem. Lett. 19, 2630-2633.
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 2630-2633
    • Gouda, H.1    Sunazuka, T.2    Iguchi, K.3    Sugawara, A.4    Hirose, T.5    Noguchi, Y.6
  • 41
    • 0034521981 scopus 로고    scopus 로고
    • Calculating structures and free energies of complex molecules: Combining molecular mechanics and continuum models
    • Kollman, P.A., Massova, I., Reyes, C, Kuhn, B., Huo, S., Chong, L. et al. (2000) Calculating structures and free energies of complex molecules: combining molecular mechanics and continuum models. Acc. Chem. Res. 33, 889-897.
    • (2000) Acc. Chem. Res. , vol.33 , pp. 889-897
    • Kollman, P.A.1    Massova, I.2    Reyes, C.3    Kuhn, B.4    Huo, S.5    Chong, L.6
  • 42
    • 41649117502 scopus 로고    scopus 로고
    • Computational analysis of the binding affinities of the natural-product cyclopentapeptides argifin and argadin to chitinase B from Serratia marcescens
    • Gouda, H., Yanai, Y., Sugawara, A., Sunazuka, T., Ōmura, S. and Hirono, S. (2008) Computational analysis of the binding affinities of the natural-product cyclopentapeptides argifin and argadin to chitinase B from Serratia marcescens. Bioorg. Med. Chem. 16, 3565-3579.
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 3565-3579
    • Gouda, H.1    Yanai, Y.2    Sugawara, A.3    Sunazuka, T.4    Ōmura, S.5    Hirono, S.6
  • 44
    • 0031138076 scopus 로고    scopus 로고
    • Camdas: An automated conformational analysis system using molecular dynamics
    • Tsujishita, H. and Hirono, S. (1997) Camdas: An automated conformational analysis system using molecular dynamics. J. Comput. Aided Mol. Des. 11, 305-315.
    • (1997) J. Comput. Aided Mol. Des. , vol.11 , pp. 305-315
    • Tsujishita, H.1    Hirono, S.2
  • 45
    • 77955099391 scopus 로고    scopus 로고
    • version 4.0; Schrödinger, LLC: New York
    • GLIDE, version 4.0; Schrödinger, LLC: New York, 2007.
    • (2007)
    • Glide1
  • 46
    • 0022469902 scopus 로고
    • Self-assembling cytotoxins
    • Rideout, D. (1986) Self-assembling cytotoxins. Science 233, 561-563.
    • (1986) Science , vol.233 , pp. 561-563
    • Rideout, D.1
  • 47
    • 0025117445 scopus 로고
    • Synergism through direct covalent bonding between agents: A strategy for rational design of chemotherapeutic combinations
    • Rideout, D., Calogeropoulu, T., Jaworski, J. and McCarthy, M. (1990) Synergism through direct covalent bonding between agents: A strategy for rational design of chemotherapeutic combinations. Biopolymers 29, 247-262.
    • (1990) Biopolymers , vol.29 , pp. 247-262
    • Rideout, D.1    Calogeropoulu, T.2    Jaworski, J.3    McCarthy, M.4
  • 48
    • 0025974512 scopus 로고
    • Multisubstrate adduct inhibitors of glycinamide ribonucleotide transformylase: Synthetic and enzyme-assembled
    • Inglese, J. and Benkovic, S.J. (1991) Multisubstrate adduct inhibitors of glycinamide ribonucleotide transformylase: Synthetic and enzyme-assembled. Tetrahedron 47, 2351-2364.
    • (1991) Tetrahedron , vol.47 , pp. 2351-2364
    • Inglese, J.1    Benkovic, S.J.2
  • 49
    • 0030852355 scopus 로고    scopus 로고
    • 10-Formyl-5,8,10-trideazafolic acid (10-formyl-TDAF): A potent inhibitor of glycinamide ribonucleotide transformylase
    • Boger, D.L., Haynes, N.-E., Kitos, P.A., Warren, M.S., Ramcharan, J., Marolewski, A.E. et al. (1997) 10-Formyl-5,8,10-trideazafolic acid (10-formyl-TDAF): A potent inhibitor of glycinamide ribonucleotide transformylase. Bioorg. Med. Chem. 5, 1817-1830.
    • (1997) Bioorg. Med. Chem. , vol.5 , pp. 1817-1830
    • Boger, D.L.1    Haynes, N.-E.2    Kitos, P.A.3    Warren, M.S.4    Ramcharan, J.5    Marolewski, A.E.6
  • 50
    • 0034646370 scopus 로고    scopus 로고
    • Combinatorial target-guided ligand assembly: Identification of potent subtype-selective c-Src inhibitors
    • Maly, D.J., Choong, I.C. and Ellman, J.A. (2000) Combinatorial target-guided ligand assembly: identification of potent subtype-selective c-Src inhibitors. Proc. Natl. Acad. Sci. USA 97, 2419-2424.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2419-2424
    • Maly, D.J.1    Choong, I.C.2    Ellman, J.A.3
  • 51
    • 0034602053 scopus 로고    scopus 로고
    • Target-accelerated combinatorial synthesis and discovery of highly potent antibiotics effective against vancomycin-resistant bacteria
    • Nicolaou, K.C., Hughes, R., Cho, S.Y., Winssinger, N., Smethurst, C, Labischinski, H. et al. (2000) Target-accelerated combinatorial synthesis and discovery of highly potent antibiotics effective against vancomycin-resistant bacteria. Angew. Chem. Int. Ed. 39, 3823-3828.
    • (2000) Angew. Chem. Int. Ed. , vol.39 , pp. 3823-3828
    • Nicolaou, K.C.1    Hughes, R.2    Cho, S.Y.3    Winssinger, N.4    Smethurst, C.5    Labischinski, H.6
  • 52
    • 0035856543 scopus 로고    scopus 로고
    • Unexpected formation of an epoxide-derived multisubstrate adduct inhibitor on the active site of GAR transformylase
    • Greasley, S.E., Marsilje, H.T., Cai, H., Baker, S., Benkovic, S.J., Boger, D.L. et al. (2001) Unexpected formation of an epoxide-derived multisubstrate adduct inhibitor on the active site of GAR transformylase. Biochemistry 40, 13538-13547.
    • (2001) Biochemistry , vol.40 , pp. 13538-13547
    • Greasley, S.E.1    Marsilje, H.T.2    Cai, H.3    Baker, S.4    Benkovic, S.J.5    Boger, D.L.6
  • 53
    • 0035805266 scopus 로고    scopus 로고
    • Using an enzyme's active site to template inhibitors
    • Nguyen, R. and Huc, I. (2001) Using an enzyme's active site to template inhibitors. Angew. Chem. Int. Ed. 40, 1774-1776.
    • (2001) Angew. Chem. Int. Ed. , vol.40 , pp. 1774-1776
    • Nguyen, R.1    Huc, I.2
  • 54
    • 0035801386 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of vancomycin dimers with potent activity against vancomycin-resistant bacteria: Target-accelerated combinatorial synthesis
    • Nicolaou, K.C., Hughes, R., Cho, S.Y., Winssinger, N., Labischinski, H. and Endermann, R. (2001) Synthesis and biological evaluation of vancomycin dimers with potent activity against vancomycin-resistant bacteria: Target-accelerated combinatorial synthesis. Chem. Eur. J. 7, 3824-3843.
    • (2001) Chem. Eur. J. , vol.7 , pp. 3824-3843
    • Nicolaou, K.C.1    Hughes, R.2    Cho, S.Y.3    Winssinger, N.4    Labischinski, H.5    Endermann, R.6
  • 55
  • 56
    • 0346994922 scopus 로고    scopus 로고
    • DNA-templated dimerization of hairpin polyamides
    • Poulin-Kerstien, A.T. and Dervan, P.B. (2003) DNA-templated dimerization of hairpin polyamides. J. Am. Chem. Soc. 125, 15811-15821.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 15811-15821
    • Poulin-Kerstien, A.T.1    Dervan, P.B.2
  • 57
    • 54249167081 scopus 로고    scopus 로고
    • L-templated assembly of its own protein-protein interaction modulator from fragments decorated with thio acids and sulfonyl azides
    • L-templated assembly of its own protein-protein interaction modulator from fragments decorated with thio acids and sulfonyl azides. J. Am. Chem. Soc. 130, 13820-13821.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 13820-13821
    • Hu, X.1    Sun, J.2    Wang, H.-G.3    Manetsch, R.4
  • 59
    • 34447562439 scopus 로고    scopus 로고
    • In situ click chemistry: A powerful means for lead discovery
    • Sharpless, K.B. and Manetsch, R. (2006) In situ click chemistry: A powerful means for lead discovery. Expert Opin. Drug Discov. 1, 525-538.
    • (2006) Expert Opin. Drug Discov. , vol.1 , pp. 525-538
    • Sharpless, K.B.1    Manetsch, R.2
  • 60
    • 0037087516 scopus 로고    scopus 로고
    • Click chemistry in situ: Acetylcholinesterase as a reaction vessel for the selective assembly of a femtomolar inhibitor from an array of building blocks
    • Lewis, W.G., Green, L.G., Grynszpan, F., Radió, Z., Carlier, P.R., Taylor, P. et al. (2002) Click chemistry in situ: Acetylcholinesterase as a reaction vessel for the selective assembly of a femtomolar inhibitor from an array of building blocks. Angew. Chem. Int. Ed. 41, 1053-1057.
    • (2002) Angew. Chem. Int. Ed. , vol.41 , pp. 1053-1057
    • Lewis, W.G.1    Green, L.G.2    Grynszpan, F.3    Radió, Z.4    Carlier, P.R.5    Taylor, P.6
  • 63
    • 18644384979 scopus 로고    scopus 로고
    • In situ selection of lead compounds by click chemistry: Target-guided optimization of acetylcholinesterase inhibitors
    • Krasiéski, A., Radić, Z., Manetsch, R., Raushel, J., Taylor, P., Sharpless, K.B. et al. (2005) In situ selection of lead compounds by click chemistry: Target-guided optimization of acetylcholinesterase inhibitors. J. Am. Chem. Soc. 127, 6686-6692.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 6686-6692
    • Krasiéski, A.1    Radić, Z.2    Manetsch, R.3    Raushel, J.4    Taylor, P.5    Sharpless, K.B.6
  • 66
    • 0037099395 scopus 로고    scopus 로고
    • A stepwise Huisgen cycloaddition process: Copper(I)-catalyzed regioselective ligation of azides and terminal alkynes
    • Rostovtsev, V.V., Green, L.G., Fokin, V.V. and Sharpless, K.B. (2002) A stepwise Huisgen cycloaddition process: Copper(I)-catalyzed regioselective ligation of azides and terminal alkynes. Angew. Chem. Int. Ed. 41, 2596-2599.
    • (2002) Angew. Chem. Int. Ed. , vol.41 , pp. 2596-2599
    • Rostovtsev, V.V.1    Green, L.G.2    Fokin, V.V.3    Sharpless, K.B.4
  • 67
    • 0037012920 scopus 로고    scopus 로고
    • Peptidotriazoles on solid phase: [1,2,3]-triazoles by regiospecific copper(I)-catalyzed 1,3-dipolar cyclo-additions of terminal alkynes to azides
    • Tornøe, C.W., Christensen, C. and Meldal, M. (2002) Peptidotriazoles on solid phase: [1,2,3]-triazoles by regiospecific copper(I)-catalyzed 1,3-dipolar cyclo-additions of terminal alkynes to azides. J. Org. Chem. 67, 3057-3064.
    • (2002) J. Org. Chem. , vol.67 , pp. 3057-3064
    • Tornøe, C.W.1    Christensen, C.2    Meldal, M.3
  • 68
    • 4444324951 scopus 로고    scopus 로고
    • Polytriazoles as copper(I)-stabilizing ligands in catalysis
    • Chan, T.R., Hilgraf, R., Sharpless, K.B. and Fokin, V.V. (2004) Polytriazoles as copper(I)-stabilizing ligands in catalysis. Org. Lett. 6, 2853-2885.
    • (2004) Org. Lett. , vol.6 , pp. 2853-2885
    • Chan, T.R.1    Hilgraf, R.2    Sharpless, K.B.3    Fokin, V.V.4


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