메뉴 건너뛰기




Volumn 70, Issue 10, 2006, Pages 2583-2587

Tumor antigen occurs in N-glycan of royal jelly glycoproteins: Honeybee cells synthesize T-antigen unit in N-glycan moiety

Author keywords

Apis mellifera; Insect N glycan; Royal jelly; T antigen; Tumor marker

Indexed keywords

BIOCHEMISTRY; CELLS; POLYSACCHARIDES; PROTEINS; SYNTHESIS (CHEMICAL); TUMORS;

EID: 33750475586     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.60331     Document Type: Article
Times cited : (12)

References (13)
  • 1
    • 0007807105 scopus 로고    scopus 로고
    • Characterization and physiological function of royal jelly proteins
    • Yonekura, M., Characterization and physiological function of royal jelly proteins. Honeybee Sci. (in Japanese), 19, 15-22 (1998).
    • (1998) Honeybee Sci. (in Japanese) , vol.19 , pp. 15-22
    • Yonekura, M.1
  • 2
    • 0036952482 scopus 로고    scopus 로고
    • Signal transduction mechanism leading to enhanced proliferation of primary cultured adult rat hepatocytes treated with royal jelly 57-kDa protein
    • Kamakura, M., Signal transduction mechanism leading to enhanced proliferation of primary cultured adult rat hepatocytes treated with royal jelly 57-kDa protein. J. Biochem., 132, 911-919 (2002).
    • (2002) J. Biochem. , vol.132 , pp. 911-919
    • Kamakura, M.1
  • 3
    • 2442440211 scopus 로고    scopus 로고
    • First evidence for occurrence of Galβ1-3GlcNAcβ1-4Man unit in N-glycans of insect glycoprotein: β1-3Gal and β1-4GlcNAc transferases are involved in N-glycan processing of royal jelly glycoproteins
    • Kimura, Y., Tsumura, K., Kimura, M., Okihara, K., Sugimoto, H., and Yamada, H., First evidence for occurrence of Galβ1-3GlcNAcβ1-4Man unit in N-glycans of insect glycoprotein: β1-3Gal and β1-4GlcNAc transferases are involved in N-glycan processing of royal jelly glycoproteins. Biosci. Biotechnol. Biochem., 67, 1852-1856 (2003).
    • (2003) Biosci. Biotechnol. Biochem. , vol.67 , pp. 1852-1856
    • Kimura, Y.1    Tsumura, K.2    Kimura, M.3    Okihara, K.4    Sugimoto, H.5    Yamada, H.6
  • 4
    • 2842588207 scopus 로고    scopus 로고
    • 350 kDa Royal jelly glycoprotein which stimulates proliferation of human monocyte bears the β1-3galactosylated N-glycan: Analysis of the N-glycosylation site
    • Kimura, M., Kimura, Y., Tsumura, K., Okihara, K., Sugimoto, H., Yamada, H., and Yonekura, M., 350 kDa Royal jelly glycoprotein which stimulates proliferation of human monocyte bears the β1-3galactosylated N-glycan: analysis of the N-glycosylation site. Biosci. Biotechnol. Biochem., 67, 2055-2058 (2003).
    • (2003) Biosci. Biotechnol. Biochem. , vol.67 , pp. 2055-2058
    • Kimura, M.1    Kimura, Y.2    Tsumura, K.3    Okihara, K.4    Sugimoto, H.5    Yamada, H.6    Yonekura, M.7
  • 5
    • 0029269727 scopus 로고
    • N-Linked oligosaccharides of 350 kDa royal jelly glycoprotein
    • Kimura, Y., Washino., N., and Yonekura, M., N-Linked oligosaccharides of 350 kDa royal jelly glycoprotein. Biosci. Biotechnol. Biochem., 59, 507-509 (1995).
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 507-509
    • Kimura, Y.1    Washino, N.2    Yonekura, M.3
  • 9
    • 0030869461 scopus 로고    scopus 로고
    • Purification and characterization of β-N-acetylgalactosaminidase from Bacillus sp. AT173-1
    • Tanaka, A., and Ozaki, S., Purification and characterization of β-N-acetylgalactosaminidase from Bacillus sp. AT173-1. J. Biochem., 122, 330-336 (1997).
    • (1997) J. Biochem. , vol.122 , pp. 330-336
    • Tanaka, A.1    Ozaki, S.2
  • 10
    • 0026657767 scopus 로고
    • An enzyme releasing lacto-N-biose from oligosaccharides
    • Sano, M., Hayakawa, K., and Kato, I., An enzyme releasing lacto-N-biose from oligosaccharides. Proc. Natl. Acad. Sci. USA, 89, 8512-8516 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8512-8516
    • Sano, M.1    Hayakawa, K.2    Kato, I.3
  • 11
    • 0031267027 scopus 로고    scopus 로고
    • Structural analysis of N-glycans of storage glycoproteins in soybean seeds
    • Kimura, Y., Ohno, A., and Takagi, S., Structural analysis of N-glycans of storage glycoproteins in soybean seeds. Biosci. Biotechnol. Biochem., 61, 1866-1871 (1997).
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 1866-1871
    • Kimura, Y.1    Ohno, A.2    Takagi, S.3
  • 12
    • 0024260839 scopus 로고
    • The asparagine-linked oligosaccharides on bovine fetuin
    • Green, E. D., Adelt, G., and Baenzinger, J. U., The asparagine-linked oligosaccharides on bovine fetuin. J. Biol. Chem., 263, 18253-18268 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 18253-18268
    • Green, E.D.1    Adelt, G.2    Baenzinger, J.U.3
  • 13
    • 0001228662 scopus 로고    scopus 로고
    • O-Glycans
    • eds. Varki, A., Cummings, R., Esko, J., Freeze, H., Hart, G., and Marth, J., Cold Spring Harbor Laboratory Press, New York
    • Marth, J., O-Glycans. In "Glycobiology," eds. Varki, A., Cummings, R., Esko, J., Freeze, H., Hart, G., and Marth, J., Cold Spring Harbor Laboratory Press, New York, pp. 101-113 (1999).
    • (1999) Glycobiology , pp. 101-113
    • Marth, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.