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Volumn 17, Issue 8, 2010, Pages 1031-1039

Oyster mushroom laccase inhibits hepatitis C virus entry into peripheral blood cells and hepatoma cells

Author keywords

Hepatitis C virus; Intracellular blocking; Laccase; Mushroom; Neutralization; Purification

Indexed keywords

BASIDIOMYCOTA; HEPATITIS C VIRUS; PLEUROTUS OSTREATUS;

EID: 77958075970     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986610791498948     Document Type: Article
Times cited : (77)

References (53)
  • 1
    • 38749106195 scopus 로고    scopus 로고
    • Structure and mechanism of the M2 proton channel of influenza A virus
    • Schnell, J.R.; Chou, J.J. Structure and mechanism of the M2 proton channel of influenza A virus. Nature, 2008, 451, 591-595.
    • (2008) Nature , vol.451 , pp. 591-595
    • Schnell, J.R.1    Chou, J.J.2
  • 2
    • 66149112971 scopus 로고    scopus 로고
    • Mechanism of drug inhibition and drug resistance of influenza A M2 channel
    • Pielak, R.M.; Jason, R.; Schnell, J.R.; Chou, J.J. Mechanism of drug inhibition and drug resistance of influenza A M2 channel. Proc. Natl. Acad. Sci. USA, 2009, 106, 7379-7384.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 7379-7384
    • Pielak, R.M.1    Jason, R.2    Schnell, J.R.3    Chou, J.J.4
  • 3
    • 56349166106 scopus 로고    scopus 로고
    • An in-depth analysis of the biological functional studies based on the NMR M2 channel structure of influenza A virus
    • Huang, R.B.; Du, Q.S.; Wang, C.H.; Chou, K.C. An in-depth analysis of the biological functional studies based on the NMR M2 channel structure of influenza A virus. Biochem. Biophys. Res. Comm., 2008, 377, 1243-1247.
    • (2008) Biochem. Biophys. Res. Comm. , vol.377 , pp. 1243-1247
    • Huang, R.B.1    Du, Q.S.2    Wang, C.H.3    Chou, K.C.4
  • 4
    • 67349139888 scopus 로고    scopus 로고
    • Energetic analysis of the two controversial drug binding sites of the M2 proton channel in influenza A virus
    • Du, Q.S.; Huang, R.B.; Wang, C.H.; Li, X.M.; Chou, K.C. Energetic analysis of the two controversial drug binding sites of the M2 proton channel in influenza A virus. J. Theor. Biol., 2009, 259, 159-164.
    • (2009) J. Theor. Biol. , vol.259 , pp. 159-164
    • Du, Q.S.1    Huang, R.B.2    Wang, C.H.3    Li, X.M.4    Chou, K.C.5
  • 5
    • 67650073942 scopus 로고    scopus 로고
    • Investigation into adamantane-based M2 inhibitors with FB-QSAR
    • Wei, H.; Wang, C.H.; Du, Q.S.; Meng, J.; Chou, K.C. Investigation into adamantane-based M2 inhibitors with FB-QSAR. Med. Chem., 2009, 5, 305-317.
    • (2009) Med. Chem. , vol.5 , pp. 305-317
    • Wei, H.1    Wang, C.H.2    Du, Q.S.3    Meng, J.4    Chou, K.C.5
  • 6
    • 69249222514 scopus 로고    scopus 로고
    • Insights from investigating the interactions of adamantane-based drugs with the M2 proton channel from the H1N1 swine virus
    • Wang, J.F.; Wei, D.Q.; Chou, K.C. Insights from investigating the interactions of adamantane-based drugs with the M2 proton channel from the H1N1 swine virus. Biochem. Biophys. Res. Commun., 2009, 388, 413-417.
    • (2009) Biochem. Biophys. Res. Commun. , vol.388 , pp. 413-417
    • Wang, J.F.1    Wei, D.Q.2    Chou, K.C.3
  • 7
    • 67650069265 scopus 로고    scopus 로고
    • Insights from investigating the interaction of oseltamivir (Tamiflu) with neuraminidase of the 2009 H1N1 swine flu virus
    • Wang, S.Q.; Du, Q.S.; Huang, R.B.; Zhang, D.W.; Chou, K.C. Insights from investigating the interaction of oseltamivir (Tamiflu) with neuraminidase of the 2009 H1N1 swine flu virus. Biochem. Biophys. Res. Commun., 2009, 386, 432-436.
    • (2009) Biochem. Biophys. Res. Commun. , vol.386 , pp. 432-436
    • Wang, S.Q.1    Du, Q.S.2    Huang, R.B.3    Zhang, D.W.4    Chou, K.C.5
  • 8
    • 33646160618 scopus 로고    scopus 로고
    • Insights from modeling the 3D structure of H5N1 influenza virus neuraminidase and its binding interactions with ligands
    • Wei, D.Q.; Du, Q.S.; Sun, H.; Chou, K.C. Insights from modeling the 3D structure of H5N1 influenza virus neuraminidase and its binding interactions with ligands. Biochem. Biophys. Res. Comm., 2006, 344, 1048-1055.
    • (2006) Biochem. Biophys. Res. Comm. , vol.344 , pp. 1048-1055
    • Wei, D.Q.1    Du, Q.S.2    Sun, H.3    Chou, K.C.4
  • 9
    • 33846617350 scopus 로고    scopus 로고
    • Study of drug resistance of chicken influenza A virus (H5N1) from homology-modeled 3D structures of neuraminidases
    • Wang, S.Q.; Du, Q.S.; Chou, K.C. Study of drug resistance of chicken influenza A virus (H5N1) from homology-modeled 3D structures of neuraminidases. Biochem. Biophys. Res. Comm., 2007, 354, 634-640.
    • (2007) Biochem. Biophys. Res. Comm. , vol.354 , pp. 634-640
    • Wang, S.Q.1    Du, Q.S.2    Chou, K.C.3
  • 10
    • 67651146680 scopus 로고    scopus 로고
    • Binding mechanism of H5N1 influenza virus neuraminidase with ligands and its implication for drug design
    • Gong, K.; Li, L.; Wang, J.F.; Cheng, F.; Wei, D.Q.; Chou, K.C. Binding mechanism of H5N1 influenza virus neuraminidase with ligands and its implication for drug design. Med. Chem., 2009, 5, 242-249.
    • (2009) Med. Chem. , vol.5 , pp. 242-249
    • Gong, K.1    Li, L.2    Wang, J.F.3    Cheng, F.4    Wei, D.Q.5    Chou, K.C.6
  • 11
    • 33344460430 scopus 로고    scopus 로고
    • A probability cellular automaton model for hepatitis B viral infections
    • Xiao, X.; Shao, S.H.; Chou, K.C. A probability cellular automaton model for hepatitis B viral infections. Biochem. Biophys. Res. Comm., 2006, 342, 605-610.
    • (2006) Biochem. Biophys. Res. Comm. , vol.342 , pp. 605-610
    • Xiao, X.1    Shao, S.H.2    Chou, K.C.3
  • 12
    • 3042732887 scopus 로고    scopus 로고
    • Proteomic profiling of proteins decreased in hepatocellular carcinoma from patients infected with hepatitis C virus
    • Yokoyama, Y.; Kuramitsu, Y.; Takashima, M. Proteomic profiling of proteins decreased in hepatocellular carcinoma from patients infected with hepatitis C virus. Proteomics., 2004, 4, 2111-2116.
    • (2004) Proteomics. , vol.4 , pp. 2111-2116
    • Yokoyama, Y.1    Kuramitsu, Y.2    Takashima, M.3
  • 13
    • 0028218513 scopus 로고
    • Identification of genotypes of hepatitis C virus by sequence comparisons in the core, E1 and NS-5 regions
    • Simmonds, P.; Smith, D.B.; McOmish, F. Identification of genotypes of hepatitis C virus by sequence comparisons in the core, E1 and NS-5 regions. J. Gen. Virol., 1994, 75 (Pt 5), 1053-1061.
    • (1994) J. Gen. Virol. , vol.75 , Issue.PT 5 , pp. 1053-1061
    • Simmonds, P.1    Smith, D.B.2    McOmish, F.3
  • 14
    • 4544248506 scopus 로고    scopus 로고
    • Hepatocellular carcinoma paradigm of preventive oncology
    • O'Brien, T.R.; Kirk, G.; Zhang, M. Hepatocellular carcinoma paradigm of preventive oncology. Cancer J., 2004, 10, 67-73.
    • (2004) Cancer J. , vol.10 , pp. 67-73
    • O'Brien, T.R.1    Kirk, G.2    Zhang, M.3
  • 15
    • 3042586666 scopus 로고    scopus 로고
    • A national project for the management of viral hepatitis toward prevention of hepatocellular carcinoma in Japan
    • Tanaka, J.; Yoshizawa, H. A national project for the management of viral hepatitis toward prevention of hepatocellular carcinoma in Japan. Gan To Kagaku Ryoho., 2004, 31, 864-870.
    • (2004) Gan To Kagaku Ryoho. , vol.31 , pp. 864-870
    • Tanaka, J.1    Yoshizawa, H.2
  • 16
    • 0031627537 scopus 로고    scopus 로고
    • Genomic subtypes of hepatitis C virus: Epidemiology, diagnosis and clinical consequences
    • Nousbam, J. Genomic subtypes of hepatitis C virus: epidemiology, diagnosis and clinical consequences. Bull. Soc. Pathol. Exot., 1998, 91(1), 29-33.
    • (1998) Bull. Soc. Pathol. Exot. , vol.91 , Issue.1 , pp. 29-33
    • Nousbam, J.1
  • 18
    • 0032879845 scopus 로고    scopus 로고
    • Combination treatment of interferon alpha-2b and ribavirin in comparison to interferon monotherapy in treatment of chronic hepatitis C genotype 4 patients
    • EL-Zayada, A.; Selim, O.; Haddad, S. Combination treatment of interferon alpha-2b and ribavirin in comparison to interferon monotherapy in treatment of chronic hepatitis C genotype 4 patients. Ital. J. Gastrroenterol. Hepato., 1999, 31(6), 472-5.
    • (1999) Ital. J. Gastrroenterol. Hepato. , vol.31 , Issue.6 , pp. 472-475
    • EL-Zayada, A.1    Selim, O.2    Haddad, S.3
  • 19
    • 77958050497 scopus 로고    scopus 로고
    • World Health Organization, In: 2002-2005: Available at, Accessed on June 18/04
    • World Health Organization: WHO Tradional Medicine Strategy 2002-2005. In: 2002-2005: Available at: http://www.who.int/medicines/library/trm/trm_strat_eng.pdf. Accessed on June 18/04.
    • WHO Tradional Medicine Strategy 2002-2005
  • 20
    • 0034710837 scopus 로고    scopus 로고
    • Isolation of a novel ubiquitin-like protein from Pleurotus ostreatus mushroom with anti-human immunodeficiency virus, translation-inhibitory, and ribonuclease activities
    • Wang, H.X.; Ng, T.B. Isolation of a novel ubiquitin-like protein from Pleurotus ostreatus mushroom with anti-human immunodeficiency virus, translation-inhibitory, and ribonuclease activities. Biochem. Biophys. Res. Commun., 2000, 276, 587-93.
    • (2000) Biochem. Biophys. Res. Commun. , vol.276 , pp. 587-593
    • Wang, H.X.1    Ng, T.B.2
  • 21
    • 2542418906 scopus 로고    scopus 로고
    • A new ribonuclease from the black oyster mushroom Pleurotus ostreatus
    • Wang, H.X.; Ng, T.B. A new ribonuclease from the black oyster mushroom Pleurotus ostreatus. Peptides, 2004, 25, 685-7.
    • (2004) Peptides , vol.25 , pp. 685-687
    • Wang, H.X.1    Ng, T.B.2
  • 22
    • 0347481321 scopus 로고    scopus 로고
    • A homodimeric laccase with unqiue characteristics from the yellow mushroom Cantharellus cibarius
    • Ng, T.B.; Wang, H.X. A homodimeric laccase with unqiue characteristics from the yellow mushroom Cantharellus cibarius. Biochem. Biophys. Res. Commun., 2004, 313, 37-41.
    • (2004) Biochem. Biophys. Res. Commun. , vol.313 , pp. 37-41
    • Ng, T.B.1    Wang, H.X.2
  • 23
    • 33846837387 scopus 로고    scopus 로고
    • A peptide with HIV-1 reverse transcriptase inhibitory activity from the medicinal mushroom Russula paludosa
    • Wang, J.; Wang, H.X.; Ng, T.B. A peptide with HIV-1 reverse transcriptase inhibitory activity from the medicinal mushroom Russula paludosa. Peptides. 2007, 28, 560-565.
    • (2007) Peptides , vol.28 , pp. 560-565
    • Wang, J.1    Wang, H.X.2    Ng, T.B.3
  • 24
    • 0025862365 scopus 로고
    • Induction of immunopotentiation activity by a protein-bound polysaccharide, PSK
    • Sagakami, H.; Aohi, T.; Simpson, A.; Tanuma, S. Induction of immunopotentiation activity by a protein-bound polysaccharide, PSK. J. Anticancer Res., 1991, 11, 993-1000.
    • (1991) J. Anticancer Res. , vol.11 , pp. 993-1000
    • Sagakami, H.1    Aohi, T.2    Simpson, A.3    Tanuma, S.4
  • 25
    • 0032917302 scopus 로고    scopus 로고
    • Therapeutic effects of substances occurring in higher Basidiomycetes mushrooms: A modern perspective
    • Wasser, S.P.; Weis, A.L. Therapeutic effects of substances occurring in higher Basidiomycetes mushrooms: a modern perspective. Crit. Rev. Immunol., 1999, 19, 65-96.
    • (1999) Crit. Rev. Immunol. , vol.19 , pp. 65-96
    • Wasser, S.P.1    Weis, A.L.2
  • 26
    • 0002876898 scopus 로고    scopus 로고
    • Medicinal value of the genus Pleurotus (Fr.) P.Karst. (Agaricales s.l. Basidiomycetes)
    • Gunde-Cimerman, N. Medicinal value of the genus Pleurotus (Fr.) P. Karst. (Agaricales s.l. Basidiomycetes). Int. J. Med. Mushroom., 1999, 1, 69-80.
    • (1999) Int. J. Med. Mushroom. , vol.1 , pp. 69-80
    • Gunde-Cimerman, N.1
  • 27
    • 0033839705 scopus 로고    scopus 로고
    • Fruiting body production in Basidiomycetes
    • Kües, U.; Liu, Y. Fruiting body production in Basidiomycetes. Appl. Microbiol. Biotechnol., 2000, 54, 141-152.
    • (2000) Appl. Microbiol. Biotechnol. , vol.54 , pp. 141-152
    • Kües, U.1    Liu, Y.2
  • 28
    • 0028351015 scopus 로고
    • Enzymes and small molecular mass agents involved with lignocellulose degradation
    • Evans, C.S.; Dutton, M.V.; Guillen, F.; Veness, R.G. Enzymes and small molecular mass agents involved with lignocellulose degradation. FEMS Microbiol Rev., 1994, 13, 235-240.
    • (1994) FEMS Microbiol Rev. , vol.13 , pp. 235-240
    • Evans, C.S.1    Dutton, M.V.2    Guillen, F.3    Veness, R.G.4
  • 29
    • 0030217935 scopus 로고    scopus 로고
    • Reduction of phenol content and toxicity in olive oil mill waste waters with the ligninolytic fungus Pleurotus ostreatus
    • Martirani, L.; Giardina, P.; Marzullo, L.; Sannia, G. Reduction of phenol content and toxicity in olive oil mill waste waters with the ligninolytic fungus Pleurotus ostreatus. Water Res., 1996, 30, 1914-1918.
    • (1996) Water Res. , vol.30 , pp. 1914-1918
    • Martirani, L.1    Giardina, P.2    Marzullo, L.3    Sannia, G.4
  • 30
    • 85133711702 scopus 로고    scopus 로고
    • Potential activity of camel milk-amylase and lactoferrin against hepatitis C virus infectivity in HepG2 and Lymphocytes
    • El-FFakharany, E. M.; Tabll, A.; Abd El-WWahab, A.; Haroun M.B.; Redwan, E. M. Potential activity of camel milk-amylase and lactoferrin against hepatitis C virus infectivity in HepG2 and Lymphocytes. J. Hep. Monthly., 2008, 8(2), 57-64.
    • (2008) J. Hep. Monthly. , vol.8 , Issue.2 , pp. 57-64
    • El-FFakharany, E.M.1    Tabll, A.2    Abd El-WWahab, A.3    Haroun, M.B.4    Redwan, E.M.5
  • 32
    • 0002891534 scopus 로고    scopus 로고
    • Purification and characterization of extracellular laccase from Pleurotus ostreatus
    • Okamoto, K.; Yanagi, S.O.; Skai, T. Purification and characterization of extracellular laccase from Pleurotus ostreatus. Micoscience. 2000, 41, 7-13.
    • (2000) Micoscience , vol.41 , pp. 7-13
    • Okamoto, K.1    Yanagi, S.O.2    Skai, T.3
  • 33
    • 0017184389 scopus 로고
    • A rapid sensitive method for the quantitation of microgram quantities of protein utilizing the principle of proteindye binding
    • Bradford, M.M. A rapid sensitive method for the quantitation of microgram quantities of protein utilizing the principle of proteindye binding. Anal. Biochem., 1976, 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 34
    • 0034541154 scopus 로고    scopus 로고
    • Purification and characterization of a new member of the laccase family from the white-rot basidiomycete Coriolus hirsutus
    • Shin, K.S.; Lee, Y.J. Purification and characterization of a new member of the laccase family from the white-rot basidiomycete Coriolus hirsutus. J. Arch. Biochem. Biophys., 2000, 384, 109-115.
    • (2000) J. Arch. Biochem. Biophys. , vol.384 , pp. 109-115
    • Shin, K.S.1    Lee, Y.J.2
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0004136246 scopus 로고    scopus 로고
    • 3rd Ed. Cold Spring Harbor, New York, U.S.A., Cold Spring Harbor Laboratory Press
    • Sambrook, J.; Russell, D.W. Molecular cloning: A laboratory manual, 3rd Ed. Cold Spring Harbor, New York, U.S.A., Cold Spring Harbor Laboratory Press, 2001.
    • (2001) Molecular cloning: A laboratory manual
    • Sambrook, J.1    Russell, D.W.2
  • 37
    • 34347394504 scopus 로고    scopus 로고
    • Camel lactoferrin markedly inhibits hepatitis C virus genotype 4 infection of human peripheral blood leukocytes
    • Redwan, El-R.M.; Tabll, A. Camel lactoferrin markedly inhibits hepatitis C virus genotype 4 infection of human peripheral blood leukocytes. J. Immunoassay Immunochem., 2007, 28, 267-277.
    • (2007) J. Immunoassay Immunochem. , vol.28 , pp. 267-277
    • Redwan, E.-R.M.1    Tabll, A.2
  • 38
    • 46649119727 scopus 로고    scopus 로고
    • Potential activity of camel milk-amylase and lactoferrin against hepatitis C virus infectivity in HepG2 and lymphocytes
    • El-Fakharany, E.M.; Tabll, A.; El-Wahab, A.A.; Haroun, B.M.; EL-Rashdy, M.; Redwan. Potential activity of camel milk-amylase and lactoferrin against hepatitis C virus infectivity in HepG2 and lymphocytes. Hepatitis Monthly., 2008, 8(2), 101-109.
    • (2008) Hepatitis Monthly. , vol.8 , Issue.2 , pp. 101-109
    • El-Fakharany, E.M.1    Tabll, A.2    El-Wahab, A.A.3    Haroun, B.M.4    EL-Rashdy, M.5    Redwan6
  • 39
    • 0032540093 scopus 로고    scopus 로고
    • Lactoferrin markedly inhibits hepatitis C virus infection in cultured human hepatocytes
    • Ikeda, M.; Nozaki, A.; Sugiyama, K. Lactoferrin markedly inhibits hepatitis C virus infection in cultured human hepatocytes. Biochem. Biophys. Res. Commun., 1998, 245, 549-553.
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 549-553
    • Ikeda, M.1    Nozaki, A.2    Sugiyama, K.3
  • 40
    • 0033956354 scopus 로고    scopus 로고
    • Characterization of antiviral activity of lactoferrin against hepatitis C virus infection in human cultured cells
    • Ikeda, M.; Nozaki, A.; Sugiyama, K. Characterization of antiviral activity of lactoferrin against hepatitis C virus infection in human cultured cells. J. Virus Res., 2000, 66, 51-63.
    • (2000) J. Virus Res. , vol.66 , pp. 51-63
    • Ikeda, M.1    Nozaki, A.2    Sugiyama, K.3
  • 41
    • 34247098497 scopus 로고    scopus 로고
    • A focus reduction neutralization assay for hepatitis C virus neutralizing antibodies
    • Fournier, C.; Duverlie, G.; Francois, C. A focus reduction neutralization assay for hepatitis C virus neutralizing antibodies. Virol., 2007, 4, 35.
    • (2007) Virol. , vol.4 , pp. 35
    • Fournier, C.1    Duverlie, G.2    Francois, C.3
  • 42
    • 0142157529 scopus 로고    scopus 로고
    • Lentin, a novel and potent antifungal protein from shitake mushroom with inhibitory effects on activity of human immunodeficiency virus-1 reverse transcriptase and proliferation of leukemic cells
    • Ngai, P.H.; Ng, T.B. Lentin, a novel and potent antifungal protein from shitake mushroom with inhibitory effects on activity of human immunodeficiency virus-1 reverse transcriptase and proliferation of leukemic cells. J. Life Sci., 2003, 73, 3363-74.
    • (2003) J. Life Sci. , vol.73 , pp. 3363-3374
    • Ngai, P.H.1    Ng, T.B.2
  • 43
    • 0842267410 scopus 로고    scopus 로고
    • Purification of a novel low molecular-mass laccase with HIV-1 reverse transcriptase inhibitory activity from the mushroom Tricholoma giganteum
    • Wang, H.X.; Ng, T.B. Purification of a novel low molecular-mass laccase with HIV-1 reverse transcriptase inhibitory activity from the mushroom Tricholoma giganteum. Biochem. Biophys. Res. Commun., 2004, 315, 450-4.
    • (2004) Biochem. Biophys. Res. Commun. , vol.315 , pp. 450-454
    • Wang, H.X.1    Ng, T.B.2
  • 44
    • 0027016612 scopus 로고
    • Primary structure of the nonspecific and adenylic acid preferential ribonuclease from the fruit bodies of Lentinus edodes
    • Kobayashi, H.; Inokuchi, N.; Koyama, T.; Watenabe H.; Iwami, M.; Ohgi, K.; Irie, M. Primary structure of the nonspecific and adenylic acid preferential ribonuclease from the fruit bodies of Lentinus edodes. J. Biosci. Biotechnol. Biochem., 1992, 55, 2003-2010.
    • (1992) J. Biosci. Biotechnol. Biochem. , vol.55 , pp. 2003-2010
    • Kobayashi, H.1    Inokuchi, N.2    Koyama, T.3    Watenabe, H.4    Iwami, M.5    Ohgi, K.6    Irie, M.7
  • 45
    • 0035884010 scopus 로고    scopus 로고
    • First simultaneous isolation of a ribosome inactivating protein and an antifungal protein from a mushroom (Lyophyllum shimeiji) together with evidence for synergism of their antifungal effects
    • Lam, S.K.; Ng, T. B. First simultaneous isolation of a ribosome inactivating protein and an antifungal protein from a mushroom (Lyophyllum shimeiji) together with evidence for synergism of their antifungal effects. Arch. Biochem. Biophys., 2001, 39, 271-280.
    • (2001) Arch. Biochem. Biophys. , vol.39 , pp. 271-280
    • Lam, S.K.1    Ng, T.B.2
  • 46
    • 0034805329 scopus 로고    scopus 로고
    • Examination of lectins, polysaccharopeptide, polysaccharide, alkaloid, coumarin and trypsin inhibitors for inhibitory activity against human immunodeficiency virus transcriptase and glycohydrolase
    • Wang, H.X.; Ng, T.B. Examination of lectins, polysaccharopeptide, polysaccharide, alkaloid, coumarin and trypsin inhibitors for inhibitory activity against human immunodeficiency virus transcriptase and glycohydrolase. J. Planta Med., 2001, 67, 669-672.
    • (2001) J. Planta Med. , vol.67 , pp. 669-672
    • Wang, H.X.1    Ng, T.B.2
  • 47
    • 0032499619 scopus 로고    scopus 로고
    • A novel lectin with potent immunomodulatory activity isolated from both fruiting bodies and cultured mycelia of the edible mushroom Volvariella volvacea
    • She, Q.B.; Ng, T.B.; Liu, W.K. A novel lectin with potent immunomodulatory activity isolated from both fruiting bodies and cultured mycelia of the edible mushroom Volvariella volvacea. Biochem. Biophys. Res. Commun., 1998, 247, 106-111.
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 106-111
    • She, Q.B.1    Ng, T.B.2    Liu, W.K.3
  • 48
    • 0033179031 scopus 로고    scopus 로고
    • Protein and gene structure of a blue laccase from Pleurotus ostreatus
    • Giardina, P.; Palmieri, G.; Scaloni, A. Protein and gene structure of a blue laccase from Pleurotus ostreatus. J. Biochem., 1999, 341, 655-663.
    • (1999) J. Biochem. , vol.341 , pp. 655-663
    • Giardina, P.1    Palmieri, G.2    Scaloni, A.3
  • 49
    • 52549090474 scopus 로고    scopus 로고
    • Structural and kinetic characterization of native laccases from Pleurotus ostreatus, Rigidoporus lignosus and Trametes trogii
    • Garzillo, A.M.; Colao, M.C.; Buonocore, V. Structural and kinetic characterization of native laccases from Pleurotus ostreatus, Rigidoporus lignosus and Trametes trogii. J. Protein Chem., 2001, 20, 191-201.
    • (2001) J. Protein Chem. , vol.20 , pp. 191-201
    • Garzillo, A.M.1    Colao, M.C.2    Buonocore, V.3
  • 50
    • 0034814968 scopus 로고    scopus 로고
    • Degradation of bisphenol A by purified laccase from Trametes villosa
    • Fukuda, T.; Uchida, H.; Takashima, Y. Degradation of bisphenol A by purified laccase from Trametes villosa. Biochem. Biophys. Res. Commun., 2001, 284, 704-706.
    • (2001) Biochem. Biophys. Res. Commun. , vol.284 , pp. 704-706
    • Fukuda, T.1    Uchida, H.2    Takashima, Y.3
  • 51
    • 0035041411 scopus 로고    scopus 로고
    • Kinetic differences of purified laccases from six Pleurotus ostreatus strains
    • Tinoco, R.; Pickard, M.A.; Vazquez-Duhalt, R. Kinetic differences of purified laccases from six Pleurotus ostreatus strains. J. Lett. Appl. Microbiol., 2001, 32, 331-35.
    • (2001) J. Lett. Appl. Microbiol. , vol.32 , pp. 331-335
    • Tinoco, R.1    Pickard, M.A.2    Vazquez-Duhalt, R.3
  • 52
    • 35349026766 scopus 로고    scopus 로고
    • Cultivation techniques and medicinal properties of Pleurotus spp
    • Gregori, A.; Svagelj, M.; Pohleven, J. Cultivation techniques and medicinal properties of Pleurotus spp. J. Food Tech. Biotech., 2007, 45, 238-249.
    • (2007) J. Food Tech. Biotech. , vol.45 , pp. 238-249
    • Gregori, A.1    Svagelj, M.2    Pohleven, J.3
  • 53
    • 0343488648 scopus 로고    scopus 로고
    • A comparison of human immunodeficiency virus type 1 inhibition by partially purified aqueous extracts of Chinese medicinal herbs
    • Collins, R.A.; Ng, T.B.; Fong, W.P.; Wan, C.C.; Yeung, H.W. A comparison of human immunodeficiency virus type 1 inhibition by partially purified aqueous extracts of Chinese medicinal herbs. J. Life Sci., 1997, 60, 345-351.
    • (1997) J. Life Sci. , vol.60 , pp. 345-351
    • Collins, R.A.1    Ng, T.B.2    Fong, W.P.3    Wan, C.C.4    Yeung, H.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.