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Volumn 42, Issue 6, 1989, Pages 883-889

Mannostatins A and B : New inhibitors of α-d-mannosidase, produced by stereptoverticillium verticillus var. Quintum ME3-AG3: Taxonomy, production, isolation, physico-chemical properties and biological activities

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA MANNOSIDASE; MANNOSTATIN A; MANNOSTATIN B;

EID: 0024358482     PISSN: 00218820     EISSN: 18811469     Source Type: Journal    
DOI: 10.7164/antibiotics.42.883     Document Type: Article
Times cited : (113)

References (19)
  • 1
    • 0017328787 scopus 로고
    • Cell-specific differences in membrane β-glucosidase from normal and Gaucher cells
    • Bryan, M. T.; N. G. Beratis & K. Hirschhorn: Cell-specific differences in membrane β-glucosidase from normal and Gaucher cells. Biochim. Biophys. Acta 480: 442-449, 1977.
    • (1977) Biochim. Biophys. Acta , vol.480 , pp. 442-449
    • Bryan, M.T.1    Beratis, N.G.2    Hirschhorn, K.3
  • 2
    • 0017735337 scopus 로고
    • Glyeosyltransferases and glycosidases in Morris hepatomas
    • Bauer, C. H.; P. Vescher, H.-J. Grünholz & W. Reutter: Glyeosyltransferases and glycosidases in Morris hepatomas. Cancer Res. 37: 1513-1518, 1977.
    • (1977) Cancer Res. , vol.37 , pp. 1513-1518
    • Bauer, C.H.1    Vescher, P.2    Grünholz, H.-J.3    Reutter, W.4
  • 3
    • 0015745268 scopus 로고
    • Differential effect of neuraminidase on the immunogenicity of viral associated and private antigens of mammary carcinomas
    • Simons, R. L. & A. Rios: Differential effect of neuraminidase on the immunogenicity of viral associated and private antigens of mammary carcinomas. J. Immunol. III: 1820-1825, 1973.
    • (1973) J. Immunol. , vol.3 , pp. 1820-1825
    • Simons, R.L.1    Rios, A.2
  • 4
    • 0015969911 scopus 로고
    • The significance of influenza virus neuraminidase in immunity
    • Rott, R.; H. Becht & M. Orlich: The significance of influenza virus neuraminidase in immunity. J. Gen. Virol. 22: 35-41, 1974.
    • (1974) J. Gen. Virol. , vol.22 , pp. 35-41
    • Rott, R.1    Becht, H.2    Orlich, M.3
  • 5
    • 0015993739 scopus 로고
    • Sialic acid residues exposed on mammalian cell surface: The effect of adsorption of denatured virus particles
    • Aoyagi, T.; J. Suzuki, K. Nerome, R. Nishizawa, T. Takeuchi & H. Umezawa: Sialic acid residues exposed on mammalian cell surface: The effect of adsorption of denatured virus particles. Biochem. Biophys. Res. Commun. 57: 271-278, 1974.
    • (1974) Biochem. Biophys. Res. Commun. , vol.57 , pp. 271-278
    • Aoyagi, T.1    Suzuki, J.2    Nerome, K.3    Nishizawa, R.4    Takeuchi, T.5    Umezawa, H.6
  • 6
    • 0015189453 scopus 로고
    • An enzyme inhibitor, panosialin, produced by Streptomyces
    • Biological activity, isolation and characterization of panosialin
    • Aoyagi, T.; M. Yagisawa, M. Kumagai, M. Hamada, Y. Okami, T. Takeuchi & H. Umezawa: An enzyme inhibitor, panosialin, produced by Streptomyces. I. Biological activity, isolation and characterization of panosialin. J. Antibiotics 24: 860-869, 1971.
    • (1971) J. Antibiotics , vol.24 , Issue.1 , pp. 860-869
    • Aoyagi, T.1    Yagisawa, M.2    Kumagai, M.3    Hamada, M.4    Okami, Y.5    Takeuchi, T.6    Umezawa, H.7
  • 7
    • 0016318699 scopus 로고
    • Purification and characterization of a sialidase inhibitor, siastatin, produced by Streptomyces
    • Umezawa, H.; T. Aoyagi, T. Komiyama, H. Morishima, M. Hamada & T. Takeuchi: Purification and characterization of a sialidase inhibitor, siastatin, produced by Streptomyces. J. Antibiotics 27: 963-969, 1974.
    • (1974) J. Antibiotics , vol.27 , pp. 963-969
    • Umezawa, H.1    Aoyagi, T.2    Komiyama, T.3    Morishima, H.4    Hamada, M.5    Takeuchi, T.6
  • 9
    • 0016589660 scopus 로고
    • Isoflavone rhamunosides, inhibitors of β-galactosidase produced by actinomycetes
    • Aoyagi, T.; T. Hazato, M. Kumagai, M. Hamada, T. Takeuchi & H. Umezawa: Isoflavone rhamunosides, inhibitors of β-galactosidase produced by actinomycetes. J. Antibiotics 28: 1006-1008, 1975.
    • (1975) J. Antibiotics , vol.28 , pp. 1006-1008
    • Aoyagi, T.1    Hazato, T.2    Kumagai, M.3    Hamada, M.4    Takeuchi, T.5    Umezawa, H.6
  • 10
    • 0018381892 scopus 로고
    • β-Galactosidase-mhibiting new isoflavonoids produced by actinomycetes
    • Hazato, T.; H. Naganawa, M. Kumagai, T. Aoyagi & H. Umezawa: β-Galactosidase-mhibiting new isoflavonoids produced by actinomycetes. J. Antibiotics 32: 217-222, 1979.
    • (1979) J. Antibiotics , vol.32 , pp. 217-222
    • Hazato, T.1    Naganawa, H.2    Kumagai, M.3    Aoyagi, T.4    Umezawa, H.5
  • 11
    • 0018394707 scopus 로고
    • p-Hydroxyphenylacetaldoxime, an inhibitor of β-galactosidase, produced by actinomycetes
    • Hazato, T.; M. Kumagai, H. Naganawa, T. Aoyagi & H. Umezawa: p-Hydroxyphenylacetaldoxime, an inhibitor of β-galactosidase, produced by actinomycetes. J. Antibiotics 32: 91 - 93, 1979.
    • (1979) J. Antibiotics , vol.32 , pp. 91-93
    • Hazato, T.1    Kumagai, M.2    Naganawa, H.3    Aoyagi, T.4    Umezawa, H.5
  • 12
    • 0013770017 scopus 로고
    • Inhibition of glycosidases by aldonolactones of corresponding configuration
    • Inhibitors of mannosidase and glucosidase
    • Levvy, G. A.; A. J. Hay & J. Conchie: Inhibition of glycosidases by aldonolactones of corresponding configuration. 4. Inhibitors of mannosidase and glucosidase. Biochem. J. 91: 378 - 384, 1964.
    • (1964) Biochem. J. , vol.91 , Issue.4 , pp. 378-384
    • Levvy, G.A.1    Hay, A.J.2    Conchie, J.3
  • 13
    • 85004532727 scopus 로고
    • Methods for characterization of Streptomyces species
    • Skirling, E. B. & D. Gottlieb: Methods for characterization of Streptomyces species. Int. J. Syst. Bacteriol. 16: 313-340, 1966.
    • (1966) Int. J. Syst. Bacteriol. , vol.16 , pp. 313-340
    • Skirling, E.B.1    Gottlieb, D.2
  • 15
    • 0013969908 scopus 로고
    • The structure of nojirimycin, a piperidinose sugar antibiotic
    • Ser. A
    • Inouye, S.; T. Tsuruoka & T. Niida: The structure of nojirimycin, a piperidinose sugar antibiotic. J. Antibiotics, Ser. A 19: 288-292, 1966.
    • (1966) J. Antibiotics , vol.19 , pp. 288-292
    • Inouye, S.1    Tsuruoka, T.2    Niida, T.3
  • 16
    • 0021738039 scopus 로고
    • Novel glycosidase inhibitors, nojirimycin B and D-mannonic-δ-lactam
    • Isolation, structure determination and biological property
    • Niwa, T.; T. Tsuruoka, H. Goi, Y. Kodama, J. Itoh, S. Inouye, Y. Yamada, T. Niida, M. Nobe & Y. Ogawa: Novel glycosidase inhibitors, nojirimycin B and D-mannonic-δ-lactam. Isolation, structure determination and biological property. J. Antibiotics 37: 1579-1586, 1984.
    • (1984) J. Antibiotics , vol.37 , pp. 1579-1586
    • Niwa, T.1    Tsuruoka, T.2    Goi, H.3    Kodama, Y.4    Itoh, J.5    Inouye, S.6    Yamada, Y.7    Niida, T.8    Nobe, M.9    Ogawa, Y.10
  • 17
    • 0001423353 scopus 로고
    • A spectroscopic investigation of swainsonine: An a-mannosidase inhibitor isolated from Swainsona canescens
    • Colegate, S. M.; P. R. Dorling & C. R. Huxtable: A spectroscopic investigation of swainsonine: An a-mannosidase inhibitor isolated from Swainsona canescens. Aust. J. Chem. 32: 2257-2264, 1979.
    • (1979) Aust. J. Chem. , vol.32 , pp. 2257-2264
    • Colegate, S.M.1    Dorling, P.R.2    Huxtable, C.R.3
  • 19
    • 85004362213 scopus 로고
    • Possible participation of rice leaf lectin in the reception of blast fungus proteoglucomannan onto the host cells
    • Kyoto, Aug. 25
    • Kang, H.; M. Haga, T. Aoyagi & Y. Sekizawa: Possible participation of rice leaf lectin in the reception of blast fungus proteoglucomannan onto the host cells. 5th International Congress of Plant Pathology, p. 251, Kyoto, Aug. 25, 1988.
    • (1988) 5th International Congress of Plant Pathology , pp. 251
    • Kang, H.1    Haga, M.2    Aoyagi, T.3    Sekizawa, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.