메뉴 건너뛰기




Volumn 85, Issue 1, 2011, Pages 582-595

Simian immunodeficiency virus from the sooty mangabey and rhesus macaque is modified with O-linked carbohydrate

Author keywords

[No Author keywords available]

Indexed keywords

JACALIN;

EID: 78650050006     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01871-10     Document Type: Article
Times cited : (24)

References (55)
  • 1
    • 33947627620 scopus 로고    scopus 로고
    • Glycosylation-dependent interaction of jacalin with CD45 induces T lymphocyte activation and Th1/Th2 cytokine secretion
    • Baba, M., B. Yong Ma, M. Nonaka, Y. Matsuishi, M. Hirano, N. Nakamura, N. Kawasaki, and T. Kawasaki. 2007. Glycosylation-dependent interaction of jacalin with CD45 induces T lymphocyte activation and Th1/Th2 cytokine secretion. J. Leukoc. Biol. 81:1002-1011.
    • (2007) J. Leukoc. Biol. , vol.81 , pp. 1002-1011
    • Baba, M.1    Yong Ma, B.2    Nonaka, M.3    Matsuishi, Y.4    Hirano, M.5    Nakamura, N.6    Kawasaki, N.7    Kawasaki, T.8
  • 2
    • 0027402782 scopus 로고
    • Distinguishing features of an infectious molecular clone of the highly divergent and noncytopathic human immunodeficiency virus type 2 UC1 strain
    • Barnett, S. W., M. Quiroga, A. Werner, D. Dina, and J. A. Levy. 1993. Distinguishing features of an infectious molecular clone of the highly divergent and noncytopathic human immunodeficiency virus type 2 UC1 strain. J. Virol. 67:1006-1014.
    • (1993) J. Virol. , vol.67 , pp. 1006-1014
    • Barnett, S.W.1    Quiroga, M.2    Werner, A.3    Dina, D.4    Levy, J.A.5
  • 3
    • 0027957921 scopus 로고
    • Human immunodeficiency virus type 1 envelope glycoprotein is modified by O-linked oligosaccharides
    • Bernstein, H. B., S. P. Tucker, E. Hunter, J. S. Schutzbach, and R. W. Compans. 1994. Human immunodeficiency virus type 1 envelope glycoprotein is modified by O-linked oligosaccharides. J. Virol. 68:463-468.
    • (1994) J. Virol. , vol.68 , pp. 463-468
    • Bernstein, H.B.1    Tucker, S.P.2    Hunter, E.3    Schutzbach, J.S.4    Compans, R.W.5
  • 4
    • 45549094069 scopus 로고    scopus 로고
    • GlycoWorkbench: A tool for the computer-assisted annotation of mass spectra of glycans
    • Ceroni, A., K. Maass, H. Geyer, R. Geyer, A. Dell, and S. M. Haslam. 2008. GlycoWorkbench: a tool for the computer-assisted annotation of mass spectra of glycans. J. Proteome Res. 7:1650-1659.
    • (2008) J. Proteome Res. , vol.7 , pp. 1650-1659
    • Ceroni, A.1    Maass, K.2    Geyer, H.3    Geyer, R.4    Dell, A.5    Haslam, S.M.6
  • 5
    • 0028308517 scopus 로고
    • Persistence of simian immunodeficiency virus Mne variants upon transmission
    • Chackerian, B., W. R. Morton, and J. Overbaugh. 1994. Persistence of simian immunodeficiency virus Mne variants upon transmission. J. Virol. 68:4080-4085.
    • (1994) J. Virol. , vol.68 , pp. 4080-4085
    • Chackerian, B.1    Morton, W.R.2    Overbaugh, J.3
  • 6
    • 0030842609 scopus 로고    scopus 로고
    • Specific N-linked and O-linked glycosylation modifications in the envelope V1 domain of simian immunodeficiency virus variants that evolve in the host alter recognition by neutralizing antibodies
    • Chackerian, B., L. M. Rudensey, and J. Overbaugh. 1997. Specific N-linked and O-linked glycosylation modifications in the envelope V1 domain of simian immunodeficiency virus variants that evolve in the host alter recognition by neutralizing antibodies. J. Virol. 71:7719-7727.
    • (1997) J. Virol. , vol.71 , pp. 7719-7727
    • Chackerian, B.1    Rudensey, L.M.2    Overbaugh, J.3
  • 8
    • 0029123329 scopus 로고
    • + cells against HIV-1, binds to the external envelope glycoprotein gp120
    • + cells against HIV-1, binds to the external envelope glycoprotein gp120. Immunol. Lett. 47:141-143.
    • (1995) Immunol. Lett. , vol.47 , pp. 141-143
    • Corbeau, P.1    Pasquali, J.L.2    Devaux, C.3
  • 9
    • 0016159877 scopus 로고
    • Cryptic A-like receptor sites in human erythrocyte glycoproteins: Proposed nature of Tn-antigen
    • Dahr, W., G. Uhlenbruck, and G. W. Bird. 1974. Cryptic A-like receptor sites in human erythrocyte glycoproteins: proposed nature of Tn-antigen. Vox Sang. 27:29-42.
    • (1974) Vox Sang. , vol.27 , pp. 29-42
    • Dahr, W.1    Uhlenbruck, G.2    Bird, G.W.3
  • 10
    • 0016477731 scopus 로고
    • The synthesis of 3,6-di-O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)- D-galactose, a branched trisaccharide reported as a hydrolysis product of blood-group substances
    • David, S., and A. Veyieres. 1975. The synthesis of 3,6-di-O-(2-acetamido- 2-deoxy-β-D-glucopyranosyl)-D-galactose, a branched trisaccharide reported as a hydrolysis product of blood-group substances. Carbohydr. Res. 40:23-29.
    • (1975) Carbohydr. Res. , vol.40 , pp. 23-29
    • David, S.1    Veyieres, A.2
  • 12
    • 1842531413 scopus 로고    scopus 로고
    • Kinetic modeling confirms the biosynthesis of mucin core 1 (β-Gal(1-3) α-GalNAc-O-Ser/Thr) O-glycan structures are modulated by neighboring glycosylation effects
    • Gerken, T. A. 2004. Kinetic modeling confirms the biosynthesis of mucin core 1 (β-Gal(1-3) α-GalNAc-O-Ser/Thr) O-glycan structures are modulated by neighboring glycosylation effects. Biochemistry 43:4137-4142.
    • (2004) Biochemistry , vol.43 , pp. 4137-4142
    • Gerken, T.A.1
  • 13
    • 0032500663 scopus 로고    scopus 로고
    • Site-specific core 1 O-glycosylation pattern of the porcine submaxillary gland mucin tandem repeat. Evidence for the modulation of glycan length by peptide sequence
    • Gerken, T. A., C. L. Owens, and M. Pasumarthy. 1998. Site-specific core 1 O-glycosylation pattern of the porcine submaxillary gland mucin tandem repeat. Evidence for the modulation of glycan length by peptide sequence. J. Biol. Chem. 273:26580-26588.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26580-26588
    • Gerken, T.A.1    Owens, C.L.2    Pasumarthy, M.3
  • 15
    • 0028107095 scopus 로고
    • Towards characterizing O-glycans: The relative merits of in vivo and in vitro approaches in seeking peptide motifs specifying O-glycosylation sites
    • Gooley, A. A., and K. L. Williams. 1994. Towards characterizing O-glycans: the relative merits of in vivo and in vitro approaches in seeking peptide motifs specifying O-glycosylation sites. Glycobiology 4:413-417.
    • (1994) Glycobiology , vol.4 , pp. 413-417
    • Gooley, A.A.1    Williams, K.L.2
  • 16
    • 0023655430 scopus 로고
    • O-linked N-acetylglucosamine is attached to proteins of the nuclear pore. Evidence for cytoplasmic and nucleoplasmic glycoproteins
    • Hanover, J. A., C. K. Cohen, M. C. Willingham, and M. K. Park. 1987. O-linked N-acetylglucosamine is attached to proteins of the nuclear pore. Evidence for cytoplasmic and nucleoplasmic glycoproteins. J. Biol. Chem. 262:9887-9894.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9887-9894
    • Hanover, J.A.1    Cohen, C.K.2    Willingham, M.C.3    Park, M.K.4
  • 17
    • 0026451818 scopus 로고
    • An O-linked carbohydrate neutralization epitope of HIV-1 gp120 is expressed by HIV-1 env gene recombinant vaccinia virus
    • Hansen, J. E., H. Clausen, S. L. Hu, J. O. Nielsen, and S. Olofsson. 1992. An O-linked carbohydrate neutralization epitope of HIV-1 gp120 is expressed by HIV-1 env gene recombinant vaccinia virus. Arch. Virol. 126:11-20.
    • (1992) Arch. Virol. , vol.126 , pp. 11-20
    • Hansen, J.E.1    Clausen, H.2    Hu, S.L.3    Nielsen, J.O.4    Olofsson, S.5
  • 18
    • 0030019509 scopus 로고    scopus 로고
    • Sensitivity of HIV-1 to neutralization by antibodies against O-linked carbohydrate epitopes despite deletion of O-glycosylation signals in the V3 loop
    • Hansen, J. E., B. Jansson, G. J. Gram, H. Clausen, J. O. Nielsen, and S. Olofsson. 1996. Sensitivity of HIV-1 to neutralization by antibodies against O-linked carbohydrate epitopes despite deletion of O-glycosylation signals in the V3 loop. Arch. Virol. 141:291-300.
    • (1996) Arch. Virol. , vol.141 , pp. 291-300
    • Hansen, J.E.1    Jansson, B.2    Gram, G.J.3    Clausen, H.4    Nielsen, J.O.5    Olofsson, S.6
  • 19
    • 0025789923 scopus 로고
    • Broadly neutralizing antibodies targeted to mucin-type carbohydrate epitopes of human immunodeficiency virus
    • Hansen, J. E., C. Nielsen, M. Arendrup, S. Olofsson, L. Mathiesen, J. O. Nielsen, and H. Clausen. 1991. Broadly neutralizing antibodies targeted to mucin-type carbohydrate epitopes of human immunodeficiency virus. J. Virol. 65:6461-6467.
    • (1991) J. Virol. , vol.65 , pp. 6461-6467
    • Hansen, J.E.1    Nielsen, C.2    Arendrup, M.3    Olofsson, S.4    Mathiesen, L.5    Nielsen, J.O.6    Clausen, H.7
  • 20
    • 0014938580 scopus 로고
    • Biosynthesis of blood group active glycoproteins: A peptidyl: α-N-acetylgalactosaminyltransferase from human submaxillary gland and stomach mucosal tissue
    • Hearn, V. M., S. D. Goodwin, and W. M. Watkins. 1970. Biosynthesis of blood group active glycoproteins: a peptidyl: α-N- acetylgalactosaminyltransferase from human submaxillary gland and stomach mucosal tissue. Biochem. Biophys. Res. Commun. 41:1279-1286.
    • (1970) Biochem. Biophys. Res. Commun. , vol.41 , pp. 1279-1286
    • Hearn, V.M.1    Goodwin, S.D.2    Watkins, W.M.3
  • 23
    • 0025343127 scopus 로고
    • Genetic organization of a chimpanzee lentivirus related to HIV-1
    • Huet, T., R. Cheynier, A. Meyerhans, G. Roelants, and S. Wain-Hobson. 1990. Genetic organization of a chimpanzee lentivirus related to HIV-1. Nature 345:356-359.
    • (1990) Nature , vol.345 , pp. 356-359
    • Huet, T.1    Cheynier, R.2    Meyerhans, A.3    Roelants, G.4    Wain-Hobson, S.5
  • 24
    • 33750997858 scopus 로고    scopus 로고
    • Glycomic Profiling of Cells and Tissues by Mass Spectrometry: Fingerprinting and Sequencing Methodologies
    • DOI 10.1016/S0076-6879(06)15005-3, PII S0076687906150053, Glycobiology
    • Jang-Lee, J., S. J. North, M. Sutton-Smith, D. Goldberg, M. Panico, H. Morris, S. Haslam, and A. Dell. 2006. Glycomic profiling of cells and tissues by mass spectrometry: fingerprinting and sequencing methodologies. Methods Enzymol. 415:59-86. (Pubitemid 44751091)
    • (2006) Methods in Enzymology , vol.415 , pp. 59-86
    • Jang-Lee, J.1    North, S.J.2    Sutton-Smith, M.3    Goldberg, D.4    Panico, M.5    Morris, H.6    Haslam, S.7    Dell, A.8
  • 25
    • 73649139554 scopus 로고    scopus 로고
    • Mucin-type O-glycosylation-putting the pieces together
    • Jensen, P. H., D. Kolarich, and N. H. Packer. 2010. Mucin-type O-glycosylation-putting the pieces together. FEBS J. 277:81-94.
    • (2010) FEBS J. , vol.277 , pp. 81-94
    • Jensen, P.H.1    Kolarich, D.2    Packer, N.H.3
  • 27
    • 13644257223 scopus 로고    scopus 로고
    • Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites
    • DOI 10.1093/glycob/cwh151
    • Julenius, K., A. Molgaard, R. Gupta, and S. Brunak. 2005. Prediction, conservation analysis, and structural characterization of mammalian mucintype O-glycosylation sites. Glycobiology 15:153-164. (Pubitemid 40227920)
    • (2005) Glycobiology , vol.15 , Issue.2 , pp. 153-164
    • Julenius, K.1    Molgaard, A.2    Gupta, R.3    Brunak, S.4
  • 31
    • 0016702060 scopus 로고
    • The purification, composition, and specificity of the anti-T lectin from peanut (Arachis hypogaea)
    • Lotan, R., E. Skutelsky, D. Danon, and N. Sharon. 1975. The purification, composition, and specificity of the anti-T lectin from peanut (Arachis hypogaea). J. Biol. Chem. 250:8518-8523.
    • (1975) J. Biol. Chem. , vol.250 , pp. 8518-8523
    • Lotan, R.1    Skutelsky, E.2    Danon, D.3    Sharon, N.4
  • 32
    • 0030775635 scopus 로고    scopus 로고
    • Neutralization sensitivity of cell culture-passaged simian immunodeficiency virus
    • Means, R. E., T. Greenough, and R. C. Desrosiers. 1997. Neutralization sensitivity of cell culture-passaged simian immunodeficiency virus. J. Virol. 71:7895-7902.
    • (1997) J. Virol. , vol.71 , pp. 7895-7902
    • Means, R.E.1    Greenough, T.2    Desrosiers, R.C.3
  • 33
    • 0031442648 scopus 로고    scopus 로고
    • Charge distribution of flanking amino acids inhibits O-glycosylation of several singlesite acceptors in vivo
    • Nehrke, K., K. G. Ten Hagen, F. K. Hagen, and L. A. Tabak. 1997. Charge distribution of flanking amino acids inhibits O-glycosylation of several singlesite acceptors in vivo. Glycobiology 7:1053-1060.
    • (1997) Glycobiology , vol.7 , pp. 1053-1060
    • Nehrke, K.1    Ten Hagen, K.G.2    Hagen, F.K.3    Tabak, L.A.4
  • 34
    • 0026671622 scopus 로고
    • Alterations in potential sites for glycosylation predominate during evolution of the simian immunodeficiency virus envelope gene in macaques
    • Overbaugh, J., and L. M. Rudensey. 1992. Alterations in potential sites for glycosylation predominate during evolution of the simian immunodeficiency virus envelope gene in macaques. J. Virol. 66:5937-5948.
    • (1992) J. Virol. , vol.66 , pp. 5937-5948
    • Overbaugh, J.1    Rudensey, L.M.2
  • 35
    • 0017008364 scopus 로고
    • Immunochemical studies on the specificity of the peanut (Arachis hypogaea) agglutinin
    • Pereira, M. E., E. A. Kabat, R. Lotan, and N. Sharon. 1976. Immunochemical studies on the specificity of the peanut (Arachis hypogaea) agglutinin. Carbohydr. Res. 51:107-118.
    • (1976) Carbohydr. Res. , vol.51 , pp. 107-118
    • Pereira, M.E.1    Kabat, E.A.2    Lotan, R.3    Sharon, N.4
  • 38
    • 3343023761 scopus 로고    scopus 로고
    • Deconvoluting the functions of polypeptide N-α- acetylgalactosaminyltransferase family members by glycopeptide substrate profiling
    • Pratt, M. R., H. C. Hang, K. G. Ten Hagen, J. Rarick, T. A. Gerken, L. A. Tabak, and C. R. Bertozzi. 2004. Deconvoluting the functions of polypeptide N-α-acetylgalactosaminyltransferase family members by glycopeptide substrate profiling. Chem. Biol. 11:1009-1016.
    • (2004) Chem. Biol. , vol.11 , pp. 1009-1016
    • Pratt, M.R.1    Hang, H.C.2    Ten Hagen, K.G.3    Rarick, J.4    Gerken, T.A.5    Tabak, L.A.6    Bertozzi, C.R.7
  • 39
    • 0025222481 scopus 로고
    • The complete nucleotide sequence of a pathogenic molecular clone of simian immunodeficiency virus
    • Regier, D. A., and R. C. Desrosiers. 1990. The complete nucleotide sequence of a pathogenic molecular clone of simian immunodeficiency virus. AIDS Res. Hum. Retroviruses 6:1221-1231.
    • (1990) AIDS Res. Hum. Retroviruses , vol.6 , pp. 1221-1231
    • Regier, D.A.1    Desrosiers, R.C.2
  • 41
    • 25144446304 scopus 로고    scopus 로고
    • Simian immunodeficiency virus infection in free-ranging sooty mangabeys (Cercocebus atys atys) from the Tai Forest, Cote d'Ivoire: Implications for the origin of epidemic human immunodeficiency virus type 2
    • Santiago, M. L., F. Range, B. F. Keele, Y. Li, E. Bailes, F. Bibollet-Ruche, C. Fruteau, R. Noe, M. Peeters, J. F. Brookfield, G. M. Shaw, P. M. Sharp, and B. H. Hahn. 2005. Simian immunodeficiency virus infection in free-ranging sooty mangabeys (Cercocebus atys atys) from the Tai Forest, Cote d'Ivoire: implications for the origin of epidemic human immunodeficiency virus type 2. J. Virol. 79:12515-12527.
    • (2005) J. Virol. , vol.79 , pp. 12515-12527
    • Santiago, M.L.1    Range, F.2    Keele, B.F.3    Li, Y.4    Bailes, E.5    Bibollet-Ruche, F.6    Fruteau, C.7    Noe, R.8    Peeters, M.9    Brookfield, J.F.10    Shaw, G.M.11    Sharp, P.M.12    Hahn, B.H.13
  • 42
    • 0023002029 scopus 로고
    • Analysis of saccharide binding to Artocarpus integrifolia lectin reveals specific recognition of T-antigen (β-D-Gal(1-3)D-GalNAc)
    • Sastry, M. V., P. Banarjee, S. R. Patanjali, M. J. Swamy, G. V. Swarnalatha, and A. Surolia. 1986. Analysis of saccharide binding to Artocarpus integrifolia lectin reveals specific recognition of T-antigen (β-D-Gal(1-3)D-GalNAc). J. Biol. Chem. 261:11726-11733.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11726-11733
    • Sastry, M.V.1    Banarjee, P.2    Patanjali, S.R.3    Swamy, M.J.4    Swarnalatha, G.V.5    Surolia, A.6
  • 44
    • 77956047416 scopus 로고    scopus 로고
    • Fundamental difference in the content of high-mannose carbohydrate in the HIV-1 and HIV-2 lineages
    • Stansell, E., and R. C. Desrosiers. 2010. Fundamental difference in the content of high-mannose carbohydrate in the HIV-1 and HIV-2 lineages. J. Virol. 84:8998-9009.
    • (2010) J. Virol. , vol.84 , pp. 8998-9009
    • Stansell, E.1    Desrosiers, R.C.2
  • 45
    • 0025266354 scopus 로고
    • Intracellular processing of the gp160 HIV-1 envelope precursor. Endoproteolytic cleavage occurs in a cis or medial compartment of the Golgi complex
    • Stein, B. S., and E. G. Engleman. 1990. Intracellular processing of the gp160 HIV-1 envelope precursor. Endoproteolytic cleavage occurs in a cis or medial compartment of the Golgi complex. J. Biol. Chem. 265:2640-2649.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2640-2649
    • Stein, B.S.1    Engleman, E.G.2
  • 46
    • 0018758637 scopus 로고
    • Initial glycosylation of proteins with acetylgalactosaminylserine linkages
    • Strous, G. J. 1979. Initial glycosylation of proteins with acetylgalactosaminylserine linkages. Proc. Natl. Acad. Sci. U. S. A. 76:2694-2698.
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 2694-2698
    • Strous, G.J.1
  • 47
    • 0026171998 scopus 로고
    • Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin
    • Swamy, M. J., D. Gupta, S. K. Mahanta, and A. Surolia. 1991. Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin. Carbohydr. Res. 213:59-67.
    • (1991) Carbohydr. Res. , vol.213 , pp. 59-67
    • Swamy, M.J.1    Gupta, D.2    Mahanta, S.K.3    Surolia, A.4
  • 48
    • 29444435597 scopus 로고    scopus 로고
    • Elucidation of binding specificity of Jacalin toward O-glycosylated peptides: Quantitative analysis by frontal affinity chromatography
    • DOI 10.1093/glycob/cwj038
    • Tachibana, K., S. Nakamura, H. Wang, H. Iwasaki, K. Maebara, L. Cheng, J. Hirabayashi, and H. Narimatsu. 2006. Elucidation of binding specificity of jacalin toward O-glycosylated peptides: quantitative analysis by frontal affinity chromatography. Glycobiology 16:46-53. (Pubitemid 43009807)
    • (2006) Glycobiology , vol.16 , Issue.1 , pp. 46-53
    • Tachibana, K.1    Nakamura, S.2    Wang, H.3    Iwasaki, H.4    Tachibana, K.5    Maebara, K.6    Cheng, L.7    Hirabayashi, J.8    Narimatsu, H.9
  • 49
    • 62449106207 scopus 로고    scopus 로고
    • Recent insights into the biological roles of mucin-type O-glycosylation
    • Tian, E., and K. G. Ten Hagen. 2009. Recent insights into the biological roles of mucin-type O-glycosylation. Glycoconj. J. 26:325-334.
    • (2009) Glycoconj. J. , vol.26 , pp. 325-334
    • Tian, E.1    Ten Hagen, K.G.2
  • 50
    • 0028196640 scopus 로고
    • Variability of the env gene in cynomolgus macaques persistently infected with human immunodeficiency virus type 2 strain ben
    • Tolle, T., H. Petry, B. Bachmann, G. Hunsmann, and W. Luke. 1994. Variability of the env gene in cynomolgus macaques persistently infected with human immunodeficiency virus type 2 strain ben. J. Virol. 68:2765-2771. (Pubitemid 24091960)
    • (1994) Journal of Virology , vol.68 , Issue.4 , pp. 2765-2771
    • Tolle, T.1    Petry, H.2    Bachmann, B.3    Hunsmann, G.4    Luke, W.5
  • 51
    • 0021280147 scopus 로고
    • Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc
    • Torres, C. R., and G. W. Hart. 1984. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc. J. Biol. Chem. 259:3308-3317.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3308-3317
    • Torres, C.R.1    Hart, G.W.2
  • 53
    • 0037418604 scopus 로고    scopus 로고
    • Binding profile of Artocarpus integrifolia agglutinin (jacalin)
    • Wu, A. M., J. H. Wu, L. H. Lin, S. H. Lin, and J. H. Liu. 2003. Binding profile of Artocarpus integrifolia agglutinin (jacalin). Life Sci. 72:2285-2302.
    • (2003) Life Sci. , vol.72 , pp. 2285-2302
    • Wu, A.M.1    Wu, J.H.2    Lin, L.H.3    Lin, S.H.4    Liu, J.H.5
  • 54
    • 0026020337 scopus 로고
    • The amino acid sequence of peanut agglutinin
    • Young, N. M., R. A. Johnston, and D. C. Watson. 1991. The amino acid sequence of peanut agglutinin. Eur. J. Biochem. 196:631-637.
    • (1991) Eur. J. Biochem. , vol.196 , pp. 631-637
    • Young, N.M.1    Johnston, R.A.2    Watson, D.C.3
  • 55
    • 0038157153 scopus 로고    scopus 로고
    • Expression of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase isoforms in murine tissues determined by real-time PCR: A new view of a large family
    • Young, W. W., Jr., D. R. Holcomb, K. G. Ten Hagen, and L. A. Tabak. 2003. Expression of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase isoforms in murine tissues determined by real-time PCR: a new view of a large family. Glycobiology 13:549-557.
    • (2003) Glycobiology , vol.13 , pp. 549-557
    • Young Jr., W.W.1    Holcomb, D.R.2    Ten Hagen, K.G.3    Tabak, L.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.