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Volumn 26, Issue 5, 2003, Pages 367-374

Neuraminidase inhibitors from Reynoutria elliptica

Author keywords

Emodin; Emodin 3 methyl ether; Influenza; Neuraminidase inhibitor; Physcion; Reynoutria elliptica; trans Resveratrol; Hydroxy emodin

Indexed keywords


EID: 0242686235     PISSN: 02536269     EISSN: 02536269     Source Type: Journal    
DOI: 10.1007/BF02976693     Document Type: Article
Times cited : (25)

References (18)
  • 1
    • 0026508847 scopus 로고
    • The 2.2 resolution crystal structure of influenza B neuraminidase and its complex with sialic acid
    • Burmeister, W. P., Ruigrok, R. W., and Cusack, S., The 2.2 resolution crystal structure of influenza B neuraminidase and its complex with sialic acid. EMBO J., 11, 49-56 (1992).
    • (1992) EMBO J. , vol.11 , pp. 49-56
    • Burmeister, W.P.1    Ruigrok, R.W.2    Cusack, S.3
  • 2
    • 0035847150 scopus 로고    scopus 로고
    • High-speed counter-current chromatography separation and purification resvertrol and piceid Polygonum cuspidatum
    • Chen, L., Han, Y., Yang, F., and Zhang, T., High-speed counter-current chromatography separation and purification resvertrol and piceid Polygonum cuspidatum. J. Chromatogr. A., 907, 343-346 (2001).
    • (2001) J. Chromatogr. A , vol.907 , pp. 343-346
    • Chen, L.1    Han, Y.2    Yang, F.3    Zhang, T.4
  • 3
    • 0028113435 scopus 로고
    • Influenza virus neuraminidase: Structure, antibiotics and inhibitors
    • Colman, P. M., Influenza virus neuraminidase: structure, antibiotics and inhibitors. Protein Sci., 3, 1687-1696 (1994).
    • (1994) Protein Sci. , vol.3 , pp. 1687-1696
    • Colman, P.M.1
  • 4
    • 0043289633 scopus 로고
    • Design and antiviral properties of influenza virus neuraminidase inhibitors
    • Colman, P. M., Design and antiviral properties of influenza virus neuraminidase inhibitors. Pure Appl. Chem., 67, 1683-1688 (1995).
    • (1995) Pure Appl. Chem. , vol.67 , pp. 1683-1688
    • Colman, P.M.1
  • 5
    • 0032758673 scopus 로고    scopus 로고
    • A novel approach to antiviral to therapy for influenza
    • Colman, P. M., A novel approach to antiviral to therapy for influenza. J. Antimicrob. Chemother., 44, 17-22 (1999).
    • (1999) J. Antimicrob. Chemother. , vol.44 , pp. 17-22
    • Colman, P.M.1
  • 6
    • 0032328062 scopus 로고    scopus 로고
    • 13C NMR spectra of anthraquinone glycoside from Rhamnus frangula
    • 13C NMR spectra of anthraquinone glycoside from Rhamnus frangula. Mag. Res. Chem., 36, 769-772 (1998).
    • (1998) Mag. Res. Chem. , vol.36 , pp. 769-772
    • Francis, G.W.1    Aksnes, D.W.2    Holt, Q.3
  • 7
    • 0342745990 scopus 로고
    • The specific enzyme of influenza virus and Vibrio cholerae
    • Gottschalk, A., The specific enzyme of influenza virus and Vibrio cholerae. Biochem. Biophys. Acta., 23, 645-646 (1957).
    • (1957) Biochem. Biophys. Acta. , vol.23 , pp. 645-646
    • Gottschalk, A.1
  • 8
    • 0023803844 scopus 로고
    • The molecular biology of influenza virus pathogenicity
    • Klenk, H. O. and Rott, R., The molecular biology of influenza virus pathogenicity. Adv. Virus Res., 34, 247-280 (1988).
    • (1988) Adv. Virus Res. , vol.34 , pp. 247-280
    • Klenk, H.O.1    Rott, R.2
  • 9
    • 0028862190 scopus 로고
    • Anthraquinone and stilbene derivatives from the cultivated Korean Rhubarb Rhizomes
    • Ko, S. K., Whang, W. K., and Kim, I. H., Anthraquinone and stilbene derivatives from the cultivated Korean Rhubarb Rhizomes. Arch. Pharm. Res., 18, 282-288 (1995).
    • (1995) Arch. Pharm. Res. , vol.18 , pp. 282-288
    • Ko, S.K.1    Whang, W.K.2    Kim, I.H.3
  • 10
    • 0028813628 scopus 로고
    • Influenza type a virus neuraminidase does not play a role in viral entry, replication, assembly or budding
    • Lin, C., Eichelberger, M. C., Compans, R. W., and Air, G. M., Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly or budding. J. Virol., 69, 1099-1106 (1995).
    • (1995) J. Virol. , vol.69 , pp. 1099-1106
    • Lin, C.1    Eichelberger, M.C.2    Compans, R.W.3    Air, G.M.4
  • 12
    • 0023612483 scopus 로고
    • ω-Hydroxyemodin, a major hepatic metabolite of emodin in various animals and its mutagenic activity
    • Murakami, H., Kobayashi, J., Musuda, T., Morooka, N., and Ueno, Y., ω-Hydroxyemodin, a major hepatic metabolite of emodin in various animals and its mutagenic activity. Mutation Res., 180, 147-153 (1987).
    • (1987) Mutation Res. , vol.180 , pp. 147-153
    • Murakami, H.1    Kobayashi, J.2    Musuda, T.3    Morooka, N.4    Ueno, Y.5
  • 13
    • 0018844023 scopus 로고
    • The synthesis of 4-methylumberiferyl α-ketoside of N-acetylneuraminic acid and its use in a fluorometric assay for neuraminidase
    • Myers, R. W., Lee, R. T., Lee, Y. C., and Thomas, G. H., The synthesis of 4-methylumberiferyl α-ketoside of N-acetylneuraminic acid and its use in a fluorometric assay for neuraminidase. Anal. Biochem., 101, 166-174 (1980).
    • (1980) Anal. Biochem. , vol.101 , pp. 166-174
    • Myers, R.W.1    Lee, R.T.2    Lee, Y.C.3    Thomas, G.H.4
  • 14
    • 0017151109 scopus 로고
    • Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro- Ntrifluoroacetyl neuraminic acid (FANA): Mechanism of action
    • Palese, P. and Compans, R. W., Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro- Ntrifluoroacetyl neuraminic acid (FANA): mechanism of action. J. General Virol., 33, 159-163 (1976).
    • (1976) J. General Virol. , vol.33 , pp. 159-163
    • Palese, P.1    Compans, R.W.2
  • 15
    • 0016272701 scopus 로고
    • Characterization of temperature sensitive influenza virus mutants
    • Palese, P., Tabita, U., Ueda, M., and Compans, R. W., Characterization of temperature sensitive influenza virus mutants. Virology, 61, 397-410 (1974).
    • (1974) Virology , vol.61 , pp. 397-410
    • Palese, P.1    Tabita, U.2    Ueda, M.3    Compans, R.W.4
  • 16
    • 0026665418 scopus 로고
    • The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor
    • Varghee, J. N., Mckimm-Breschkin, J. L., Caldwell, J. B., Kortt, A. A., and Colman, P. M., The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor. Protein, 14, 327-332 (1992).
    • (1992) Protein , vol.14 , pp. 327-332
    • Varghee, J.N.1    Mckimm-Breschkin, J.L.2    Caldwell, J.B.3    Kortt, A.A.4    Colman, P.M.5
  • 17
    • 0027287506 scopus 로고
    • Rational design of potent sialidase-based inhibitors of influenza virus replication
    • von Itzstein, N., Kok, G. B., and Pegg, M. S., Rational design of potent sialidase-based inhibitors of influenza virus replication. Nature, 363, 418-423 (1993).
    • (1993) Nature , vol.363 , pp. 418-423
    • Von Itzstein, N.1    Kok, G.B.2    Pegg, M.S.3
  • 18
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Willey, D. C. and Skehel, J. J., The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu. Rev. Biochem., 56, 365-394 (1987).
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 365-394
    • Willey, D.C.1    Skehel, J.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.