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Volumn 21, Issue 8, 2011, Pages 1060-1070

Lectin microarray profiling of metastatic breast cancers

Author keywords

breast cancer; glycome; lectin; metastasis; microarray

Indexed keywords

FETUIN; GLYCAN; JACALIN; LECTIN; N ACETYLGALACTOSAMINE; PEANUT AGGLUTININ; PLANT LECTIN; SOYBEAN AGGLUTININ;

EID: 79960272328     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwr045     Document Type: Article
Times cited : (82)

References (62)
  • 1
    • 77954601866 scopus 로고    scopus 로고
    • Glycomic analysis of sialic acid linkages in glycans derived from blood serum glycoproteins
    • Alley WR, Novotny MV. 2010. Glycomic analysis of sialic acid linkages in glycans derived from blood serum glycoproteins. J Proteome Res. 9:3062-3072.
    • (2010) J Proteome Res. , vol.9 , pp. 3062-3072
    • Alley, W.R.1    Novotny, M.V.2
  • 3
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein gly-cosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler R, Hermjakob H, Sharon N. 1999. On the frequency of protein gly-cosylation, as deduced from analysis of the SWISS-PROT database. Biochim Biophys Acta. 1473:4-8.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 4
    • 35748976558 scopus 로고    scopus 로고
    • Clinical evaluation of the simultaneous determination of CA 15-3, CA 125 and sHER2 in breast cancer
    • DOI 10.1080/13547500701520563, PII 780573426
    • Baskic D, Ristic P, Matic S, Bankovic D, Popovic S, Arsenijevic N. 2007. Clinical evaluation of the simultaneous determination of CA 15-3, CA 125 and sHER2 in breast cancer. Biomarkers. 12:657-667. (Pubitemid 350048080)
    • (2007) Biomarkers , vol.12 , Issue.6 , pp. 657-667
    • Baskic, D.1    Ristic, P.2    Matic, S.3    Bankovic, D.4    Popovic, S.5    Arsenijevic, N.6
  • 5
    • 61449238139 scopus 로고    scopus 로고
    • Development of a nanoLC LTQ orbitrap mass spectrometric method for profiling glycans derived from plasma from healthy, benign tumor control, and epithelial ovarian cancer patients
    • Bereman MS, Williams TI, Muddiman DC. 2009. Development of a nanoLC LTQ orbitrap mass spectrometric method for profiling glycans derived from plasma from healthy, benign tumor control, and epithelial ovarian cancer patients. Anal Chem. 81:1130-1136.
    • (2009) Anal Chem , vol.81 , pp. 1130-1136
    • Bereman, M.S.1    Williams, T.I.2    Muddiman, D.C.3
  • 7
    • 33744799438 scopus 로고    scopus 로고
    • Mucin-type O-glycans in human colon and breast cancer: Glycodynamics and functions
    • DOI 10.1038/sj.embor.7400705, PII 7400705
    • Brockhausen I. 2006. Mucin-type O-glycans in human colon and breast cancer: Glycodynamics and functions. EMBO Rep. 7:599-604. (Pubitemid 43827326)
    • (2006) EMBO Reports , vol.7 , Issue.6 , pp. 599-604
    • Brockhausen, I.1
  • 8
    • 0033977912 scopus 로고    scopus 로고
    • The involvement of Helix pomatia lectin (HPA) binding N- acetylgalactosamine glycans in cancer progression
    • Brooks SA. 2000. The involvement of Helix pomatia lectin (HPA) binding N-acetylgalactosamine glycans in cancer progression. Histol Histopathol. 15:143-158. (Pubitemid 30044299)
    • (2000) Histology and Histopathology , vol.15 , Issue.1 , pp. 143-158
    • Brooks, S.A.1
  • 10
    • 17644378372 scopus 로고    scopus 로고
    • Outcome of patients with ductal carcinoma in situ untreated after diagnostic biopsy: Results from the nurses' health study
    • DOI 10.1002/cncr.20979
    • Collins LC, Tamimi RM, Baer HJ, Connolly JL, Colditz GA, Schnitt SJ. 2005. Outcome of patients with ductal carcinoma in situ untreated after diagnostic biopsy: Results from the Nurses' Health Study. Cancer. 103:1778-1784. (Pubitemid 40563248)
    • (2005) Cancer , vol.103 , Issue.9 , pp. 1778-1784
    • Collins, L.C.1    Tamimi, R.M.2    Baer, H.J.3    Connolly, J.L.4    Colditz, G.A.5    Schnitt, S.J.6
  • 11
    • 0020479688 scopus 로고
    • Characterization of the structural determinants required for the high affinity interaction of asparagine-linked oligosaccharides with immobilized Phaseolus vulgaris leukoagglutinating and erythroagglutinating lectins
    • Cummings RD, Kornfeld S. 1982. Characterization of the structural determinants required for the high affinity interaction of asparagine-linked oligosaccharides with immobilized Phaseolus vulgaris leukoagglutinating and erythroagglutinating lectins. J Biol Chem. 257:11230-11234.
    • (1982) J Biol Chem , vol.257 , pp. 11230-11234
    • Cummings, R.D.1    Kornfeld, S.2
  • 13
    • 0023255440 scopus 로고
    • β1-6 branching of Asn-linked oligosaccharides is directly associated with metastasis
    • Dennis JW, Laferte S, Waghorne C, Breitman ML, Kerbel RS. 1987. Beta 1-6 branching of Asn-linked oligosaccharides is directly associated with metastasis. Science. 236:582-585. (Pubitemid 17069927)
    • (1987) Science , vol.236 , Issue.4801 , pp. 582-585
    • Dennis, J.W.1    Laferte, S.2    Waghorne, C.3
  • 14
    • 20844437106 scopus 로고    scopus 로고
    • Glycans in cancer and inflammation - Potential for therapeutics and diagnostics
    • DOI 10.1038/nrd1751
    • Dube DH, Bertozzi CR. 2005. Glycans in cancer and inflammation-potential for therapeutics and diagnostics. Nat Rev Drug Discov. 4:477-488. (Pubitemid 40861990)
    • (2005) Nature Reviews Drug Discovery , vol.4 , Issue.6 , pp. 477-488
    • Dube, D.H.1    Bertozzi, C.R.2
  • 15
    • 0035380645 scopus 로고    scopus 로고
    • Proteome and glycosylation mapping identifies post-translational modifications associated with aggressive breast cancer
    • Dwek MV, Ross HA, Leathem AJ. 2001. Proteome and glycosylation mapping identifies post-translational modifications associated with aggressive breast cancer. Proteomics. 1:756-762. (Pubitemid 33696518)
    • (2001) Proteomics , vol.1 , Issue.6 , pp. 756-762
    • Dwek, M.V.1    Ross, H.A.2    Leathem, A.J.C.3
  • 16
    • 0021999503 scopus 로고
    • Demonstration by monoclonal antibodies that carbohydrate structures of glycoproteins and glycolipids are onco-developmental antigens
    • DOI 10.1038/314053a0
    • Feizi T. 1985. Demonstration by monoclonal antibodies that carbohydrate structures of glycoproteins and glycolipids are onco-developmental antigens. Nature. 314:53-57. (Pubitemid 15142022)
    • (1985) Nature , vol.314 , Issue.6006 , pp. 53-57
    • Feizi, T.1
  • 17
    • 33745381312 scopus 로고    scopus 로고
    • Genetic defects in the human glycome
    • DOI 10.1038/nrg1894, PII N1894
    • Freeze HH. 2006. Genetic defects in the human glycome. Nat Rev Genet. 7:537-551. (Pubitemid 43943571)
    • (2006) Nature Reviews Genetics , vol.7 , Issue.7 , pp. 537-551
    • Freeze, H.H.1
  • 18
    • 21744431575 scopus 로고    scopus 로고
    • The sweet and sour of cancer: Glycans as novel therapeutic targets
    • DOI 10.1038/nrc1649
    • Fuster MM, Esko JD. 2005. The sweet and sour of cancer: Glycans as novel therapeutic targets. Nat Rev Cancer. 5:526-542. (Pubitemid 40942829)
    • (2005) Nature Reviews Cancer , vol.5 , Issue.7 , pp. 526-542
    • Fuster, M.M.1    Esko, J.D.2
  • 19
    • 60449111627 scopus 로고    scopus 로고
    • Glycomic profiling of invasive and non-invasive breast cancer cells
    • Goetz JA, Mechref Y, Kang P, Jeng MH, Novotny MV 2009. Glycomic profiling of invasive and non-invasive breast cancer cells. Glycoconj J. 26:117-131.
    • (2009) Glycoconj J , vol.26 , pp. 117-131
    • Goetz, J.A.1    Mechref, Y.2    Kang, P.3    Jeng, M.H.4    Novotny, M.V.5
  • 20
    • 0030480250 scopus 로고    scopus 로고
    • Tumor malignancy defined by aberrant glycosylation and sphingo(glyco)lipid metabolism
    • Hakomori S. 1996. Tumor malignancy defined by aberrant glycosylation and sphingo(glyco)lipid metabolism. Cancer Res. 56:5309-5318. (Pubitemid 27011703)
    • (1996) Cancer Research , vol.56 , Issue.23 , pp. 5309-5318
    • Hakomori, S.-I.1
  • 21
    • 48749083261 scopus 로고    scopus 로고
    • Concept, strategy and realization of lectin-based glycan profiling
    • Hirabayashi J. 2008. Concept, strategy and realization of lectin-based glycan profiling. JBiochem. 144:139-147.
    • (2008) JBiochem , vol.144 , pp. 139-147
    • Hirabayashi, J.1
  • 22
    • 33646452547 scopus 로고    scopus 로고
    • Analyzing the dynamic bacterial glycome with a lectin microarray approach
    • DOI 10.1038/nchembio767, PII NCHEMBIO767
    • Hsu KL, Pilobello KT, Mahal LK. 2006. Analyzing the dynamic bacterial glycome with a lectin microarray approach. Nat Chem Biol. 2:153-157. (Pubitemid 44323867)
    • (2006) Nature Chemical Biology , vol.2 , Issue.3 , pp. 153-157
    • Hsu, K.-L.1    Pilobello, K.T.2    Mahal, L.K.3
  • 24
    • 59749086716 scopus 로고    scopus 로고
    • Specificity analysis of lectins and antibodies using remodeled glycoproteins
    • Iskratsch T, Braun A, Paschinger K, Wilson IB. 2009. Specificity analysis of lectins and antibodies using remodeled glycoproteins. Anal Biochem. 386:133-146.
    • (2009) Anal Biochem , vol.386 , pp. 133-146
    • Iskratsch, T.1    Braun, A.2    Paschinger, K.3    Wilson, I.B.4
  • 26
    • 36849033327 scopus 로고    scopus 로고
    • Elderberry bark lectins evolved to recognize Neu5Acα2,6Gal/GalNAc sequence from a Gal/GalNAc binding lectin through the substitution of amino-acid residues critical for the binding to sialic acid
    • DOI 10.1093/jb/mvm146
    • Kaku H, Kaneko H, Minamihara N, Iwata K, Jordan ET, Rojo MA, Minami-Ishii N, Minami E, Hisajima S, Shibuya N. 2007. Elderberry bark lectins evolved to recognize Neu5Acoc2,6Gal/GalNAc sequence from a Gal/GalNAc binding lectin through the substitution of amino-acid residues critical for the binding to sialic acid. J Biochem. 142:393-401. (Pubitemid 350221843)
    • (2007) Journal of Biochemistry , vol.142 , Issue.3 , pp. 393-401
    • Kaku, H.1    Kaneko, H.2    Minamihara, N.3    Iwata, K.4    Jordan, E.T.5    Rojo, M.A.6    Minami-Ishii, N.7    Minami, E.8    Hisajima, S.9    Shibuya, N.10
  • 27
    • 0030070330 scopus 로고    scopus 로고
    • Sialylated oligosaccharide-specific plant lectin from Japanese elderberry (Sambucus sieboldiana) bark tissue has a homologous structure to type II ribosome-inactivating proteins, ricin and abrin. cDNA cloning and molecular modeling study
    • Kaku H, Tanaka Y, Tazaki K, Minami E, Mizuno H, Shibuya N. 1996. Sialylated oligosaccharide-specific plant lectin from Japanese elderberry (Sambucus sieboldiana) bark tissue has a homologous structure to type II ribosome-inactivating proteins, ricin and abrin. cDNA cloning and molecular modeling study. J Biol Chem. 271:1480-1485.
    • (1996) J Biol Chem , vol.271 , pp. 1480-1485
    • Kaku, H.1    Tanaka, Y.2    Tazaki, K.3    Minami, E.4    Mizuno, H.5    Shibuya, N.6
  • 28
    • 33745886837 scopus 로고    scopus 로고
    • Expression of Vicia villosa agglutinin (VVA)-binding glycoprotein in primary breast cancer cells in relation to lymphatic metastasis: Is atypical MUC1 bearing Tn antigen a receptor of VVA?
    • DOI 10.1007/s10549-005-9115-6
    • Kawaguchi T, Takazawa H, Imai S, Morimoto J, Watanabe T, Kanno M, Igarashi S. 2006. Expression of Vicia villosa agglutinin (VVA)-binding glycoprotein in primary breast cancer cells in relation to lymphatic metastasis: Is atypical MUC1 bearing Tn antigen a receptor of VVA? Breast Cancer Res Treat. 98:31-43. (Pubitemid 44050778)
    • (2006) Breast Cancer Research and Treatment , vol.98 , Issue.1 , pp. 31-43
    • Kawaguchi, T.1    Takazawa, H.2    Imai, S.3    Morimoto, J.4    Watanabe, T.5    Kanno, M.6    Igarashi, S.7
  • 30
    • 18844370547 scopus 로고    scopus 로고
    • Capillary electrophoresis-mass spectrometry as a powerful tool in clinical diagnosis and biomarker discovery
    • DOI 10.1002/mas.20051
    • Kolch W, Neususs C, Pelzing M, Mischak H. 2005. Capillary electrophoresis-mass spectrometry as a powerful tool in clinical diagnosis and biomarker discovery. Mass Spectrom Rev. 24:959-977. (Pubitemid 41641706)
    • (2005) Mass Spectrometry Reviews , vol.24 , Issue.6 , pp. 959-977
    • Kolch, W.1    Neususs, C.2    Pelzing, M.3    Mischak, H.4
  • 31
    • 33744504505 scopus 로고    scopus 로고
    • Study of the expression of Tn antigen in different types of human breast cancer cells using VVA-B4 lectin
    • Konska G, Guerry M, Caldefie-Chezet F, De Latour M, Guillot J. 2006. Study of the expression of Tn antigen in different types of human breast cancer cells using VVA-B4 lectin. Oncol Rep. 15:305-310.
    • (2006) Oncol Rep , vol.15 , pp. 305-310
    • Konska, G.1    Guerry, M.2    Caldefie-Chezet, F.3    De Latour, M.4    Guillot, J.5
  • 33
    • 28844480949 scopus 로고    scopus 로고
    • Structural basis for the specificity of basic winged bean lectin for the Tn-antigen: A crystallographic, thermodynamic and modelling study
    • DOI 10.1016/j.febslet.2005.11.011, PII S001457930501358X
    • Kulkarni KA, Sinha S, Katiyar S, Surolia A, Vijayan M, Suguna K. 2005. Structural basis for the specificity of basic winged bean lectin for the Tn-antigen: A crystallographic, thermodynamic and modelling study. FEBS Lett. 579:6775-6780. (Pubitemid 41773685)
    • (2005) FEBS Letters , vol.579 , Issue.30 , pp. 6775-6780
    • Kulkarni, K.A.1    Sinha, S.2    Katiyar, S.3    Surolia, A.4    Vijayan, M.5    Suguna, K.6
  • 34
    • 28544452519 scopus 로고    scopus 로고
    • Evanescent-field fluorescence-assisted lectin microarray: A new strategy for glycan profiling
    • DOI 10.1038/nmeth803, PII N803
    • Kuno A, Uchiyama N, Koseki-Kuno S, Ebe Y, Takashima S, Yamada M, Hirabayashi J. 2005. Evanescent-field fluorescence-assisted lectin microar-ray: A new strategy for glycan profiling. Nat Methods. 2:851-856. (Pubitemid 41741536)
    • (2005) Nature Methods , vol.2 , Issue.11 , pp. 851-856
    • Kuno, A.1    Uchiyama, N.2    Koseki-Kuno, S.3    Ebe, Y.4    Takashima, S.5    Yamada, M.6    Hirabayashi, J.7
  • 38
    • 0042266719 scopus 로고    scopus 로고
    • A genetic approach to mammalian glycan function
    • DOI 10.1146/annurev.biochem.72.121801.161809
    • Lowe JB, Marth JD. 2003. A genetic approach to Mammalian glycan function. Annu Rev Biochem. 72:643-691. (Pubitemid 36930456)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 643-691
    • Lowe, J.B.1    Marth, J.D.2
  • 39
    • 42249114497 scopus 로고    scopus 로고
    • Development of an all-in-one technology for glycan profiling targeting formalin-embedded tissue sections
    • Matsuda A, Kuno A, Ishida H, Kawamoto T, Shoda J, Hirabayashi J. 2008. Development of an all-in-one technology for glycan profiling targeting formalin-embedded tissue sections. Biochem Biophys Res Commun. 370:259-263.
    • (2008) Biochem Biophys Res Commun , vol.370 , pp. 259-263
    • Matsuda, A.1    Kuno, A.2    Ishida, H.3    Kawamoto, T.4    Shoda, J.5    Hirabayashi, J.6
  • 40
    • 0033045573 scopus 로고    scopus 로고
    • The use of the lectin Helix pomatia agglutinin (HPA) as a prognostic indicator and as a tool in cancer research
    • Mitchell BS, Schumacher U. 1999. The use of the lectin Helix pomatia agglu-tinin (HPA) as a prognostic indicator and as a tool in cancer research. Histol Histopathol. 14:217-226. (Pubitemid 29049369)
    • (1999) Histology and Histopathology , vol.14 , Issue.1 , pp. 217-226
    • Schumacher, U.1
  • 41
    • 24644490868 scopus 로고    scopus 로고
    • Characterization of wheat germ agglutinin ligand on soluble glycoproteins in Caenorhabditis elegans
    • DOI 10.1093/jb/mvi117
    • Natsuka S, Kawaguchi M, Wada Y, Ichikawa A, Ikura K, Hase S. 2005. Characterization of wheat germ agglutinin ligand on soluble glycoproteins in Caenorhabditis elegans. J Biochem. 138:209-213. (Pubitemid 41265372)
    • (2005) Journal of Biochemistry , vol.138 , Issue.2 , pp. 209-213
    • Natsuka, S.1    Kawaguchi, M.2    Wada, Y.3    Ichikawa, A.4    Ikura, K.5    Hase, S.6
  • 43
    • 0025367755 scopus 로고
    • Comparison of the carbohydrate-binding specificities of seven N-acetyl-D-galactosamine-recognizing lectins
    • DOI 10.1111/j.1432-1033.1990.tb19144.x
    • Piller V, Piller F, Cartron JP. 1990. Comparison of the carbohydrate-binding specificities of seven N-acetyl-D-galactosamine-recognizing lectins. Eur J Biochem. 191:461-466. (Pubitemid 20233763)
    • (1990) European Journal of Biochemistry , vol.191 , Issue.2 , pp. 461-466
    • Piller, V.1    Piller, F.2    Cartron, J.-P.3
  • 44
    • 20444501805 scopus 로고    scopus 로고
    • Development of a lectin microarray for the rapid analysis of protein glycopatterns
    • DOI 10.1002/cbic.200400403
    • Pilobello KT, Krishnamoorthy L, Slawek D, Mahal LK. 2005. Development of a lectin microarray for the rapid analysis of protein glycopatterns. Chembiochem. 6:985-989. (Pubitemid 40825336)
    • (2005) ChemBioChem , vol.6 , Issue.6 , pp. 985-989
    • Pilobello, K.T.1    Krishnamoorthy, L.2    Slawek, D.3    Mahal, L.K.4
  • 47
    • 77953420571 scopus 로고    scopus 로고
    • Fabrication of an oriented lectin microarray
    • Propheter DC, Hsu KL, Mahal LK. 2010. Fabrication of an oriented lectin microarray. Chembiochem. 11:1203-1207.
    • (2010) Chembiochem , vol.11 , pp. 1203-1207
    • Propheter, D.C.1    Hsu, K.L.2    Mahal, L.K.3
  • 50
    • 0030664540 scopus 로고    scopus 로고
    • Lectin histochemical HPA-binding pattern of human breast and colon cancers is associated with metastases formation in severe combined immunodeficient mice
    • DOI 10.1023/A:1026404832394
    • Schumacher U, Adam E. 1997. Lectin histochemical HPA-binding pattern of human breast and colon cancers is associated with metastases formation in severe combined immunodeficient mice. Histochem J. 29:677-684. (Pubitemid 27489870)
    • (1997) Histochemical Journal , vol.29 , Issue.9 , pp. 677-684
    • Schumacher, U.1    Adam, E.2
  • 51
    • 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, Nakamura S, Wang H, Iwasaki H, Maebara K, Cheng L, Hirabayashi J, Narimatsu H. 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
  • 52
    • 64549138417 scopus 로고    scopus 로고
    • Comparative analysis of core-fucose-binding lectins from Lens culinaris and Pisum sativum using frontal affinity chromatography
    • Tateno H, Nakamura-Tsuruta S, Hirabayashi J. 2009. Comparative analysis of core-fucose-binding lectins from Lens culinaris and Pisum sativum using frontal affinity chromatography. Glycobiology. 19:527-536.
    • (2009) Glycobiology , vol.19 , pp. 527-536
    • Tateno, H.1    Nakamura-Tsuruta, S.2    Hirabayashi, J.3
  • 53
    • 16344384394 scopus 로고    scopus 로고
    • Renal and urinary proteomics: Current applications and challenges
    • DOI 10.1002/pmic.200401012
    • Thongboonkerd V, Malasit P. 2005. Renal and urinary proteomics: Current applications and challenges. Proteomics. 5:1033-1042. (Pubitemid 40469033)
    • (2005) Proteomics , vol.5 , Issue.4 , pp. 1033-1042
    • Thongboonkerd, V.1    Malasit, P.2
  • 54
    • 0030584096 scopus 로고    scopus 로고
    • The NeuAc(α-2,6)-Gal/GalNAc-binding lectin from elderberry (Sambucus nigra) bark, a type-2 ribosome-inactivating protein with an unusual specificity and structure
    • Van Damme EJ, Barre A, Rouge P, Van Leuven F, Peumans WJ. 1996. The NeuAc(α-2,6)-Gal/GalNAc-binding lectin from elderberry (Sambucus nigra) bark, a type-2 ribosome-inactivating protein with an unusual specificity and structure. Eur J Biochem. 235:128-137.
    • (1996) Eur J Biochem , vol.235 , pp. 128-137
    • Van Damme, E.J.1    Barre, A.2    Rouge, P.3    Van Leuven, F.4    Peumans, W.J.5
  • 55
    • 77749343015 scopus 로고    scopus 로고
    • Glycome profiling using modern glycomics technology: Technical aspects and applications
    • Vanderschaeghe D, Festjens N, Delanghe J, Callewaert N. 2010. Glycome profiling using modern glycomics technology: Technical aspects and applications. Biol Chem. 391:149-161.
    • (2010) Biol Chem , vol.391 , pp. 149-161
    • Vanderschaeghe, D.1    Festjens, N.2    Delanghe, J.3    Callewaert, N.4
  • 56
    • 17744387316 scopus 로고    scopus 로고
    • α) as the most potent recognition factors involved in Maclura pomifera agglutinin-glycan interactions
    • DOI 10.1007/s11373-004-8178-4
    • Wu AM. 2005. Polyvalent GalNAcα1-Ser/Thr (Tn) and Galβ1-3GalNAcα1-Ser/Thr (T α) as the most potent recognition factors involved in Maclura pomifera agglutinin-glycan interactions. J Biomed Sci. 12:135-152. (Pubitemid 40576771)
    • (2005) Journal of Biomedical Science , vol.12 , Issue.1 , pp. 135-152
    • Wu, A.M.1
  • 57
    • 0038641868 scopus 로고    scopus 로고
    • Effect of polyvalencies of glycotopes on the binding of a lectin from the edible mushroom, Agaricus bisporus
    • DOI 10.1042/BJ20021361
    • Wu AM, Wu JH, Herp A, Liu JH. 2003. Effect of polyvalencies of glyco-topes on the binding of a lectin from the edible mushroom, Agaricus bis-porus. Biochem J. 371:311-320. (Pubitemid 36547613)
    • (2003) Biochemical Journal , vol.371 , Issue.2 , pp. 311-320
    • Wu, A.M.1    Wu, J.H.2    Herp, A.3    Liu, J.-H.4
  • 58
    • 1642564606 scopus 로고    scopus 로고
    • Recognition profile of Bauhinia purpurea agglutinin (BPA)
    • DOI 10.1016/j.lfs.2003.08.031
    • Wu AM, Wu JH, Liu JH, Singh T. 2004. Recognition profile of Bauhinia pur-purea agglutinin (BPA). Life Sci. 74:1763-1779. (Pubitemid 38117103)
    • (2004) Life Sciences , vol.74 , Issue.14 , pp. 1763-1779
    • Wu, A.M.1    Wu, J.H.2    Liu, J.-H.3    Singh, T.4
  • 59
    • 0030566395 scopus 로고    scopus 로고
    • 4, reacting with Tn (GalNAcα1→Ser/Thr) or galabiose (Galα1→ 4Gal) containing ligands
    • DOI 10.1016/S0014-5793(96)01227-6, PII S0014579396012276
    • Wu AM, Wu JH, Song SC, Kabat EA. 1996. Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A4, reacting with Tn (Ga1NAcα1-Ser/Thr) or galabiose (Ga1α1-4Ga1) containing ligands. FEBS Lett. 398:183-186. (Pubitemid 26414306)
    • (1996) FEBS Letters , vol.398 , Issue.2-3 , pp. 183-186
    • Wu, A.M.1    Wu, J.H.2    Song, S.-C.3    Kabat, E.A.4
  • 60
    • 0026461130 scopus 로고
    • Purification and characterization of a Fucα1-2Galβ1-and GalNAcβ1-specific lectin in root tubers of Trichosanthes japonica
    • Yamashita K, Ohkura T, Umetsu K, Suzuki T. 1992. Purification and characterization of a Fucα1-2Galβ1-and GalNAcβ1-specific lectin in root tubers of Trichosanthes japonica. J Biol Chem. 267:25414-25422.
    • (1992) J Biol Chem , vol.267 , pp. 25414-25422
    • Yamashita, K.1    Ohkura, T.2    Umetsu, K.3    Suzuki, T.4
  • 61
    • 0026439093 scopus 로고
    • Purification and characterization of a Neu5Ac alpha 2-6Gal beta 1-4GlcNAc and HSO3(-)-6Gal beta 1-GlcNAc specific lectin in tuberous roots of Trichosanthes japonica
    • Yamashita K, Umetsu K, Suzuki T, Ohkura T. 1992. Purification and characterization of a Neu5Ac alpha 2-6Gal beta 1-4GlcNAc and HSO3(-)-6Gal beta 1-GlcNAc specific lectin in tuberous roots of Trichosanthes japonica. Biochemistry. 31:11647-11650.
    • (1992) Biochemistry , vol.31 , pp. 11647-11650
    • Yamashita, K.1    Umetsu, K.2    Suzuki, T.3    Ohkura, T.4
  • 62
    • 22244436325 scopus 로고    scopus 로고
    • Lectin arrays for profiling cell surface carbohydrate expression
    • DOI 10.1021/ja0505550
    • Zheng T, Peelen D, Smith LM. 2005. Lectin arrays for profiling cell surface carbohydrate expression. J Am Chem Soc. 127:9982-9983. (Pubitemid 40995426)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.28 , pp. 9982-9983
    • Zheng, T.1    Peelen, D.2    Smith, L.M.3


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