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Volumn 1473, Issue 1, 1999, Pages 21-34

Glycoprotein glycosylation and cancer progression

Author keywords

Adhesion; Cancer; GlcNAc TV; Metastasis; Motility; Receptors

Indexed keywords

GLYCAN DERIVATIVE; N ACETYLGLUCOSAMINYLTRANSFERASE; T LYMPHOCYTE RECEPTOR;

EID: 0032714567     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-4165(99)00167-1     Document Type: Review
Times cited : (620)

References (112)
  • 2
    • 0031767247 scopus 로고    scopus 로고
    • Genetics of RAS signaling in C. elegans
    • Sternberg P.W., Han M. Genetics of RAS signaling in C. elegans. Trends Genet. 14:1998;466-472.
    • (1998) Trends Genet. , vol.14 , pp. 466-472
    • Sternberg, P.W.1    Han, M.2
  • 3
    • 0022462129 scopus 로고
    • Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides
    • Schachter H. Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides. Biochem. Cell Biol. 64:1986;163-181.
    • (1986) Biochem. Cell Biol. , vol.64 , pp. 163-181
    • Schachter, H.1
  • 5
    • 0021227742 scopus 로고
    • The distribution of repeating Gal β1-4GlcNAc β1-3 sequences in asparagine-linked oligosaccharides of the mouse lymphoma cell line BW5147 and PHAR 2.1
    • Cummings R.D., Kornfeld S. The distribution of repeating Gal β1-4GlcNAc β1-3 sequences in asparagine-linked oligosaccharides of the mouse lymphoma cell line BW5147 and PHAR 2.1. J. Biol. Chem. 259:1984;6253-6260.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6253-6260
    • Cummings, R.D.1    Kornfeld, S.2
  • 6
    • 0026086828 scopus 로고
    • Increased UDP-GlcNAc:Gal β1-3GalNAc-R (GlcNAc to GalNAc) β1-6 N-acetylglucosaminyltransferase activity in transformed and metastatic murine tumor cell lines: Control of polylactosamine-synthesis
    • Yousefi S., Higgins E., Doaling Z., Hindsgaul O., Pollex-Kruger A., Dennis J.W. Increased UDP-GlcNAc:Gal β1-3GalNAc-R (GlcNAc to GalNAc) β1-6 N-acetylglucosaminyltransferase activity in transformed and metastatic murine tumor cell lines: control of polylactosamine-synthesis. J. Biol. Chem. 266:1991;1772-1783.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1772-1783
    • Yousefi, S.1    Higgins, E.2    Doaling, Z.3    Hindsgaul, O.4    Pollex-Kruger, A.5    Dennis, J.W.6
  • 7
    • 0023634937 scopus 로고
    • Synthesis of type 1 and 2 lacto series glycolipid antigens in human colonic adenocarcinoma and derived cell lines is due to activation of a normally unexpressed β1-3N-acetylglucosaminyltransferase
    • Holmes E.H., Hakomori S.-I., Ostrander G.K. Synthesis of type 1 and 2 lacto series glycolipid antigens in human colonic adenocarcinoma and derived cell lines is due to activation of a normally unexpressed β1-3N-acetylglucosaminyltransferase. J. Biol. Chem. 262:1987;15649-15657.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15649-15657
    • Holmes, E.H.1    Hakomori, S.-I.2    Ostrander, G.K.3
  • 8
    • 0026333183 scopus 로고
    • The poly-N-acetyllactosamines attached to lysosomal membrane glycoproteins are increased by the prolonged association with the Golgi complex
    • Wang W.C., Lee N., Aoki D., Fukuda M.N., Fukuda M. The poly-N-acetyllactosamines attached to lysosomal membrane glycoproteins are increased by the prolonged association with the Golgi complex. J. Biol. Chem. 266:1991;23185-23190.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23185-23190
    • Wang, W.C.1    Lee, N.2    Aoki, D.3    Fukuda, M.N.4    Fukuda, M.5
  • 9
    • 0031019168 scopus 로고    scopus 로고
    • Expression of human H-type α1,2-fucosyltransferase encoding for blood group H (0) antigen in Chinese hamster ovary cells
    • Prieto P.A., Larsen R.D., Cho M., Rivera H.N., Shilatifard A., Lowe J.B., Cummings R.D., Smith D.F. Expression of human H-type α1,2-fucosyltransferase encoding for blood group H (0) antigen in Chinese hamster ovary cells. J. Biol. Chem. 272:1997;2089-2097.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2089-2097
    • Prieto, P.A.1    Larsen, R.D.2    Cho, M.3    Rivera, H.N.4    Shilatifard, A.5    Lowe, J.B.6    Cummings, R.D.7    Smith, D.F.8
  • 12
    • 0025918707 scopus 로고
    • Structures and functional roles of the sugar chains of human erythropoietins
    • Takeuchi M., Kobata A. Structures and functional roles of the sugar chains of human erythropoietins. Glycobiology. 1:1991;337-346.
    • (1991) Glycobiology , vol.1 , pp. 337-346
    • Takeuchi, M.1    Kobata, A.2
  • 13
    • 0032567715 scopus 로고    scopus 로고
    • Glycosylation provides both stimulatory and inhibitory effects on cell surface and soluble CD44 binding to hyaluronan
    • Skelton T.P., Zeng C., Nocks A., Stamenkovic I. Glycosylation provides both stimulatory and inhibitory effects on cell surface and soluble CD44 binding to hyaluronan. J. Cell Biol. 140:1998;431-446.
    • (1998) J. Cell Biol. , vol.140 , pp. 431-446
    • Skelton, T.P.1    Zeng, C.2    Nocks, A.3    Stamenkovic, I.4
  • 14
    • 0025759969 scopus 로고
    • Binding of the integrin Mac-1 (CD11b/CD18) to the third immunoglobulin-like domain of ICAM-1 (CD54) and its regulation by glycosylation
    • Diamond M.S., Staunton D.E., Martin S.D., Springer T.A. Binding of the integrin Mac-1 (CD11b/CD18) to the third immunoglobulin-like domain of ICAM-1 (CD54) and its regulation by glycosylation. Cell. 65:1991;961-971.
    • (1991) Cell , vol.65 , pp. 961-971
    • Diamond, M.S.1    Staunton, D.E.2    Martin, S.D.3    Springer, T.A.4
  • 16
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld R., Kornfeld S. Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54:1985;631-664.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 17
    • 0028273766 scopus 로고
    • Complementation of an Arabidopsis thaliana mutant that lacks complex asparagine-linked glycans with the human cDNA encoding N-acetylglucosaminyltransferase I
    • Gomez L., Chrispeels M.J. Complementation of an Arabidopsis thaliana mutant that lacks complex asparagine-linked glycans with the human cDNA encoding N-acetylglucosaminyltransferase I. Proc. Natl. Acad. Sci. USA. 91:1994;1829-1833.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1829-1833
    • Gomez, L.1    Chrispeels, M.J.2
  • 18
    • 0028213962 scopus 로고
    • Complex asparagine-linked oligosaccharides are required for morphogenic events during post-implantation development
    • Metzler M., Gertz A., Sarkar M., Schachter H., Schrader J.W., Marth J.D. Complex asparagine-linked oligosaccharides are required for morphogenic events during post-implantation development. EMBO J. 13:1994;2056-2065.
    • (1994) EMBO J. , vol.13 , pp. 2056-2065
    • Metzler, M.1    Gertz, A.2    Sarkar, M.3    Schachter, H.4    Schrader, J.W.5    Marth, J.D.6
  • 19
    • 0028012014 scopus 로고
    • Mice lacking N-acetylglucosaminyltransferase I activity die at mid-gestation, revealing an essential role for complex or hybrid N-linked carbohydrates
    • Ioffe E., Stanley P. Mice lacking N-acetylglucosaminyltransferase I activity die at mid-gestation, revealing an essential role for complex or hybrid N-linked carbohydrates. Proc. Natl. Acad. Sci. USA. 91:1994;728-732.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 728-732
    • Ioffe, E.1    Stanley, P.2
  • 20
    • 0028575328 scopus 로고
    • Lectin domains in the toxin of Bordetella pertussis: Selectin mimicry linked to microbial pathogenesis
    • Sandros J., Rozdzinski E., Zheng J., Cowburn D., Tuomanen E. Lectin domains in the toxin of Bordetella pertussis: selectin mimicry linked to microbial pathogenesis. Glycoconjugate J. 11:1994;501-506.
    • (1994) Glycoconjugate J. , vol.11 , pp. 501-506
    • Sandros, J.1    Rozdzinski, E.2    Zheng, J.3    Cowburn, D.4    Tuomanen, E.5
  • 21
    • 0023433835 scopus 로고
    • Recognition of monovalent sialosides by influenza virus H3 hemagglutinin
    • Pritchett T.J., Brossmer R., Rose U., Paulson J.C. Recognition of monovalent sialosides by influenza virus H3 hemagglutinin. Virology. 160:1987;502-506.
    • (1987) Virology , vol.160 , pp. 502-506
    • Pritchett, T.J.1    Brossmer, R.2    Rose, U.3    Paulson, J.C.4
  • 22
    • 0033135747 scopus 로고    scopus 로고
    • Protein glycosylation in development and disease
    • Dennis J.W., Granovsky M., Warren C.E. Protein glycosylation in development and disease. BioEssays. 21:1999;412-421.
    • (1999) BioEssays , vol.21 , pp. 412-421
    • Dennis, J.W.1    Granovsky, M.2    Warren, C.E.3
  • 23
    • 0030977266 scopus 로고    scopus 로고
    • Growth retardation and early death of β1,4-galactosyltransferase knockout mice with augmented proliferation and abnormal differentiation of epithelial cells
    • Asano M., Furukawa K., Kido M., Matsumoto S., Umesaki Y., Kochibe N., Iwakura Y. Growth retardation and early death of β1,4-galactosyltransferase knockout mice with augmented proliferation and abnormal differentiation of epithelial cells. EMBO J. 16:1997;1850-1857.
    • (1997) EMBO J. , vol.16 , pp. 1850-1857
    • Asano, M.1    Furukawa, K.2    Kido, M.3    Matsumoto, S.4    Umesaki, Y.5    Kochibe, N.6    Iwakura, Y.7
  • 24
    • 0031054637 scopus 로고    scopus 로고
    • Isolation, characterization and inactivation of the mouse Mgat3 gene: The bisecting N-acetylglucosamine in asparagine-linked oligosaccharides appears dispensable for viability and reproduction
    • Priatel J.J., Sarkar M., Schachter H., Marth J.D. Isolation, characterization and inactivation of the mouse Mgat3 gene: the bisecting N-acetylglucosamine in asparagine-linked oligosaccharides appears dispensable for viability and reproduction. Glycobiology. 7:1997;45-56.
    • (1997) Glycobiology , vol.7 , pp. 45-56
    • Priatel, J.J.1    Sarkar, M.2    Schachter, H.3    Marth, J.D.4
  • 26
    • 0345319445 scopus 로고    scopus 로고
    • Structure function analysis of rat N-acetylglucosaminyltransferase V
    • Abstract 346
    • B., Korczak, T. Le, S. Elowe, J.W. Dennis, Structure function analysis of rat N-acetylglucosaminyltransferase V. Glycoconjugate J., S123 (1997) Abstract 346.
    • (1997) Glycoconjugate J. , vol.S123
    • Korczak, B.1    Le, T.2    Elowe, S.3    Dennis, J.W.4
  • 27
    • 0029861621 scopus 로고    scopus 로고
    • A point mutation causes mistargeting of golgi GlcNAc-TV in the Lec4A Chinese hamster ovary glycosylation mutant
    • Weinstein J., Sundaram S., Wang X., Delgado D., Basu R., Stanley P. A point mutation causes mistargeting of golgi GlcNAc-TV in the Lec4A Chinese hamster ovary glycosylation mutant. J. Biol. Chem. 271:1996;27462-27469.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27462-27469
    • Weinstein, J.1    Sundaram, S.2    Wang, X.3    Delgado, D.4    Basu, R.5    Stanley, P.6
  • 29
    • 0021208290 scopus 로고
    • Comparative study of the oligosaccharides released from baby hamster kidney cells and their polyoma transformant by hydrazinolysis
    • Yamashita K., Ohkura T., Tachibana Y., Takasaki S., Kobata A. Comparative study of the oligosaccharides released from baby hamster kidney cells and their polyoma transformant by hydrazinolysis. J. Biol. Chem. 259:1984;10834-10840.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10834-10840
    • Yamashita, K.1    Ohkura, T.2    Tachibana, Y.3    Takasaki, S.4    Kobata, A.5
  • 30
    • 0021990008 scopus 로고
    • Enzymatic basis for the structural changes of asparagine-linked sugar chains of membrane glycoproteins of baby hamster kidney cells induced by polyoma transformation
    • Yamashita K., Tachibana Y., Ohkura T., Kobata A. Enzymatic basis for the structural changes of asparagine-linked sugar chains of membrane glycoproteins of baby hamster kidney cells induced by polyoma transformation. J. Biol. Chem. 260:1985;3963-3969.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3963-3969
    • Yamashita, K.1    Tachibana, Y.2    Ohkura, T.3    Kobata, A.4
  • 31
    • 0025788280 scopus 로고
    • Enzymatic amplification involving glycosyltransferases forms the basis for the increased size of asparagine-linked glycans at the surface of NIH 3T3 cells expressing the N-ras proto-oncogene
    • Easton E.W., Bolscher J.G.M., van den Eijnden D.H. Enzymatic amplification involving glycosyltransferases forms the basis for the increased size of asparagine-linked glycans at the surface of NIH 3T3 cells expressing the N-ras proto-oncogene. J. Biol. Chem. 266:1991;21674-21680.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21674-21680
    • Easton, E.W.1    Bolscher, J.G.M.2    Van Den Eijnden, D.H.3
  • 32
    • 0027174294 scopus 로고
    • Induction of N-acetylglucosaminyltransferase V by elevated expression of activated or proto-Ha-ras oncogenes
    • Lu Y., Chaney W. Induction of N-acetylglucosaminyltransferase V by elevated expression of activated or proto-Ha-ras oncogenes. Mol. Cell. Biochem. 122:1993;85-92.
    • (1993) Mol. Cell. Biochem. , vol.122 , pp. 85-92
    • Lu, Y.1    Chaney, W.2
  • 33
    • 0023255440 scopus 로고
    • β 1-6 branching of Asn-linked oligosaccharides is directly associated with metastasis
    • Dennis J.W., Laferte S., Waghorne C., Breitman M.L., Kerbel R.S. β 1-6 branching of Asn-linked oligosaccharides is directly associated with metastasis. Science. 236:1987;582-585.
    • (1987) Science , vol.236 , pp. 582-585
    • Dennis, J.W.1    Laferte, S.2    Waghorne, C.3    Breitman, M.L.4    Kerbel, R.S.5
  • 34
    • 0024321039 scopus 로고
    • Oncogenes conferring metastatic potential induce increased branching of Asn-linked oligosaccharides in rat2 fibroblasts
    • Dennis J.W., Kosh K., Bryce D.-M., Breitman M.L. Oncogenes conferring metastatic potential induce increased branching of Asn-linked oligosaccharides in rat2 fibroblasts. Oncogene. 4:1989;853-860.
    • (1989) Oncogene , vol.4 , pp. 853-860
    • Dennis, J.W.1    Kosh, K.2    Bryce, D.-M.3    Breitman, M.L.4
  • 35
    • 0015493417 scopus 로고
    • Surface glycoproteins and glycolipids of chicken embryo cells transformed by a temperature-sensitive mutant of rous sarcoma virus
    • Warren L., Critchley D., Macpherson I. Surface glycoproteins and glycolipids of chicken embryo cells transformed by a temperature-sensitive mutant of rous sarcoma virus. Nature. 235:1972;275-278.
    • (1972) Nature , vol.235 , pp. 275-278
    • Warren, L.1    Critchley, D.2    Macpherson, I.3
  • 36
    • 0021350564 scopus 로고
    • Transient versus permanent expression of cancer-related glycopeptides on normal versus leukemic myeloid cells coinciding with marrow egress
    • van Beek W., Tulp A., Bolscher J., Blanken G., Roozendaal K., Egbers M. Transient versus permanent expression of cancer-related glycopeptides on normal versus leukemic myeloid cells coinciding with marrow egress. Blood. 63:1984;170-176.
    • (1984) Blood , vol.63 , pp. 170-176
    • Van Beek, W.1    Tulp, A.2    Bolscher, J.3    Blanken, G.4    Roozendaal, K.5    Egbers, M.6
  • 37
    • 0026014062 scopus 로고
    • β1-6 branched oligosaccharides as a marker of tumor progression in human breast and colon neoplasia
    • Fernandes B., Sagman U., Auger M., Demetriou M., Dennis J.W. β1-6 branched oligosaccharides as a marker of tumor progression in human breast and colon neoplasia. Cancer Res. 51:1991;718-723.
    • (1991) Cancer Res. , vol.51 , pp. 718-723
    • Fernandes, B.1    Sagman, U.2    Auger, M.3    Demetriou, M.4    Dennis, J.W.5
  • 38
    • 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 lectin
    • Cummings R.D., Kornfeld S. Characterization of the structural determinants required for the high affinity interaction of asparagine-linked oligosaccharides with immobilized Phaseolus vulgaris leukoagglutinating and erythroagglutinating lectin. J. Biol. Chem. 257:1982;11230-11234.
    • (1982) J. Biol. Chem. , vol.257 , pp. 11230-11234
    • Cummings, R.D.1    Kornfeld, S.2
  • 40
    • 0025254569 scopus 로고
    • Increase of β1-6-branched oligosaccharides in human esophageal carcinomas invasive against surrounding tissue in vivo and in vitro
    • Takano R., Nose M., Nishihira I., Kyogoku M. Increase of β1-6-branched oligosaccharides in human esophageal carcinomas invasive against surrounding tissue in vivo and in vitro. Am. J. Pathol. 137:1990;1007-1011.
    • (1990) Am. J. Pathol. , vol.137 , pp. 1007-1011
    • Takano, R.1    Nose, M.2    Nishihira, I.3    Kyogoku, M.4
  • 41
    • 0032530215 scopus 로고    scopus 로고
    • Molecular epidemiology of human cancer: Contribution of mutation spectra studies of tumor suppressor genes
    • Hussain S.P., Harris C.C. Molecular epidemiology of human cancer: contribution of mutation spectra studies of tumor suppressor genes. Cancer Res. 58:1998;4023-4037.
    • (1998) Cancer Res. , vol.58 , pp. 4023-4037
    • Hussain, S.P.1    Harris, C.C.2
  • 42
    • 0029849620 scopus 로고    scopus 로고
    • Cancer cell cycles
    • Sherr C.J. Cancer cell cycles. Science. 274:1996;1672-1677.
    • (1996) Science , vol.274 , pp. 1672-1677
    • Sherr, C.J.1
  • 43
    • 0022450555 scopus 로고
    • Primary rat embryo cells transformed by one or two oncogenes show different metastatic potentials
    • Pozzatti R., Muschel R., Williams J., Padmanabhan R., Howard B., Liotta L., Khoury G. Primary rat embryo cells transformed by one or two oncogenes show different metastatic potentials. Science. 232:1986;223-225.
    • (1986) Science , vol.232 , pp. 223-225
    • Pozzatti, R.1    Muschel, R.2    Williams, J.3    Padmanabhan, R.4    Howard, B.5    Liotta, L.6    Khoury, G.7
  • 46
    • 0030480250 scopus 로고    scopus 로고
    • Tumor malignancy defined by aberrant glycosylation and sphingo(glyco)lipid metabolism
    • Hakomori S.-I. Tumor malignancy defined by aberrant glycosylation and sphingo(glyco)lipid metabolism. Cancer Res. 56:1996;5309-5318.
    • (1996) Cancer Res. , vol.56 , pp. 5309-5318
    • Hakomori, S.-I.1
  • 47
    • 0031947714 scopus 로고    scopus 로고
    • A retrospective and prospective view of glycopathology
    • Kobata A. A retrospective and prospective view of glycopathology. Glycoconjugate J. 15:1998;323-331.
    • (1998) Glycoconjugate J. , vol.15 , pp. 323-331
    • Kobata, A.1
  • 48
    • 0032103332 scopus 로고    scopus 로고
    • Ets transcription factors: Nuclear effectors of the Ras-MAP-kinase signaling pathways
    • Wasylyk B., Hagman J., Gutierrez-Hartmann A. Ets transcription factors: nuclear effectors of the Ras-MAP-kinase signaling pathways. Trends Biochem. Sci. 23:1998;213-216.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 213-216
    • Wasylyk, B.1    Hagman, J.2    Gutierrez-Hartmann, A.3
  • 51
    • 0030754637 scopus 로고    scopus 로고
    • Transcriptional regulation of N-acetylglucosaminyltransferase V by the src oncogene
    • Buckhaults P., Chen L., Fregien N., Pierce M. Transcriptional regulation of N-acetylglucosaminyltransferase V by the src oncogene. J. Biol. Chem. 272:1997;19575-19581.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19575-19581
    • Buckhaults, P.1    Chen, L.2    Fregien, N.3    Pierce, M.4
  • 52
    • 0029932755 scopus 로고    scopus 로고
    • Oncogenic Neu/ErbB-2 increases ets, AP-1, and NF-kappaB-dependent gene expression, and inhibiting ets activation blocks Neu-mediated cellular transformation
    • Galang C.K., Garcia-Ramirez J., Solski P.A., Westwick J.K., Der C.J., Neznanov N.N., Oshima R.G., Hauser C.A. Oncogenic Neu/ErbB-2 increases ets, AP-1, and NF-kappaB-dependent gene expression, and inhibiting ets activation blocks Neu-mediated cellular transformation. J. Biol. Chem. 271:1996;7992-7998.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7992-7998
    • Galang, C.K.1    Garcia-Ramirez, J.2    Solski, P.A.3    Westwick, J.K.4    Der, C.J.5    Neznanov, N.N.6    Oshima, R.G.7    Hauser, C.A.8
  • 53
    • 0032558738 scopus 로고    scopus 로고
    • The her-2/neu oncogene stimulates the transcription of N-acetylglucosaminyltransferase V and expression of its cell surface oligosaccharide products
    • Chen L., Zhang W., Fregien N., Pierce M. The her-2/neu oncogene stimulates the transcription of N-acetylglucosaminyltransferase V and expression of its cell surface oligosaccharide products. Oncogene. 17:1998;2087-2093.
    • (1998) Oncogene , vol.17 , pp. 2087-2093
    • Chen, L.1    Zhang, W.2    Fregien, N.3    Pierce, M.4
  • 55
    • 37049183697 scopus 로고
    • Human breast cancer: Correlation of relapse and survival with amplification of the Her-2/neu oncogene
    • Slamon D.J., Clark G.M., Wong S.G., Levin W.J., Ulrich A., McGuire W.L. Human breast cancer: correlation of relapse and survival with amplification of the Her-2/neu oncogene. Science. 235:1987;177-182.
    • (1987) Science , vol.235 , pp. 177-182
    • Slamon, D.J.1    Clark, G.M.2    Wong, S.G.3    Levin, W.J.4    Ulrich, A.5    McGuire, W.L.6
  • 56
    • 0029021007 scopus 로고
    • Reduced contact-inhibition and substratum adhesion in epithelial cells expressing GlcNAc-transferase V
    • Demetriou M., Nabi I.R., Coppolino M., Dedhar S., Dennis J.W. Reduced contact-inhibition and substratum adhesion in epithelial cells expressing GlcNAc-transferase V. J. Cell Biol. 130:1995;383-392.
    • (1995) J. Cell Biol. , vol.130 , pp. 383-392
    • Demetriou, M.1    Nabi, I.R.2    Coppolino, M.3    Dedhar, S.4    Dennis, J.W.5
  • 57
    • 0033031839 scopus 로고    scopus 로고
    • Control of metastasis by asn-linked, β1-6 branched oligosaccharides in mouse mammary cancer cells
    • Seberger P.J., Chaney W.G. Control of metastasis by asn-linked, β1-6 branched oligosaccharides in mouse mammary cancer cells. Glycobiology. 9:1999;235-241.
    • (1999) Glycobiology , vol.9 , pp. 235-241
    • Seberger, P.J.1    Chaney, W.G.2
  • 58
    • 0029027831 scopus 로고
    • Suppression of lung metastasis of B16 mouse melanoma by N-acetylglucosaminyltransferase II gene transfection
    • Yoshimura M., Nishikawa A., Ihara Y., Taniguchi S., Taniguchi N. Suppression of lung metastasis of B16 mouse melanoma by N-acetylglucosaminyltransferase II gene transfection. Proc. Natl. Acad. Sci. USA. 92:1995;8753-8758.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8753-8758
    • Yoshimura, M.1    Nishikawa, A.2    Ihara, Y.3    Taniguchi, S.4    Taniguchi, N.5
  • 59
    • 0029933659 scopus 로고    scopus 로고
    • Aberrant glycosylation of E-cadherin enhances cell-cell binding to suppress metastasis
    • Yoshimura M., Ihara Y., Matsuzawa Y., Taniguchi N. Aberrant glycosylation of E-cadherin enhances cell-cell binding to suppress metastasis. J. Biol. Chem. 271:1996;13811-13815.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13811-13815
    • Yoshimura, M.1    Ihara, Y.2    Matsuzawa, Y.3    Taniguchi, N.4
  • 60
    • 0031564104 scopus 로고    scopus 로고
    • Remodeling of glycoconjugates on CD44 enhances cell adhesion to hyaluronate, tumor growth and metastasis in B16 melanoma cells expressing β1,4-N-acetylglucosaminyltransferase III
    • Sheng Y., Yoshimura M., Inoue S., Oritani K., Nishiura T., Yoshida H., Ogawa M., Okajima Y., Matsuzawa Y., Taniguchi N. Remodeling of glycoconjugates on CD44 enhances cell adhesion to hyaluronate, tumor growth and metastasis in B16 melanoma cells expressing β1,4-N-acetylglucosaminyltransferase III. Int. J. Cancer. 73:1997;850-858.
    • (1997) Int. J. Cancer , vol.73 , pp. 850-858
    • Sheng, Y.1    Yoshimura, M.2    Inoue, S.3    Oritani, K.4    Nishiura, T.5    Yoshida, H.6    Ogawa, M.7    Okajima, Y.8    Matsuzawa, Y.9    Taniguchi, N.10
  • 61
    • 0029240438 scopus 로고
    • E-cadherin as a tumor (invasion) suppressor gene
    • Birchmeier W. E-cadherin as a tumor (invasion) suppressor gene. BioEssays. 17:1995;97-99.
    • (1995) BioEssays , vol.17 , pp. 97-99
    • Birchmeier, W.1
  • 63
    • 0030983084 scopus 로고    scopus 로고
    • Gene transfection-mediated overexpression of β1,4-N-acetylglucosamine bisecting oligosaccharides in glioma cell line U373 MG inhibits epidermal growth factor receptor function
    • Rebbaa A., Yamamoto H., Saito T., Meuillet E., Kim P., Kersey D.S., Bremer E.G., Taniguchi N., Moskal J.R. Gene transfection-mediated overexpression of β1,4-N-acetylglucosamine bisecting oligosaccharides in glioma cell line U373 MG inhibits epidermal growth factor receptor function. J. Biol. Chem. 272:1997;9275-9279.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9275-9279
    • Rebbaa, A.1    Yamamoto, H.2    Saito, T.3    Meuillet, E.4    Kim, P.5    Kersey, D.S.6    Bremer, E.G.7    Taniguchi, N.8    Moskal, J.R.9
  • 64
    • 0030970043 scopus 로고    scopus 로고
    • Overexpression of N-acetylglucosaminyltransferase III disrupts the tyrosine phosphorylation of Trk with resultant signaling dysfunction in PC12 cells treated with nerve growth factor
    • Ihara Y., Sakamoto Y., Mihara M., Shimizu K., Taniguchi N. Overexpression of N-acetylglucosaminyltransferase III disrupts the tyrosine phosphorylation of Trk with resultant signaling dysfunction in PC12 cells treated with nerve growth factor. J. Biol. Chem. 272:1997;9629-9634.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9629-9634
    • Ihara, Y.1    Sakamoto, Y.2    Mihara, M.3    Shimizu, K.4    Taniguchi, N.5
  • 65
    • 0033118791 scopus 로고    scopus 로고
    • Signaling specificity: The RTK/RAS/MAP kinase pathway in metazoans
    • Tan P.B.O., Kim S.K. Signaling specificity: the RTK/RAS/MAP kinase pathway in metazoans. Trends Genet. 15:1999;145-149.
    • (1999) Trends Genet. , vol.15 , pp. 145-149
    • Tan, P.B.O.1    Kim, S.K.2
  • 66
    • 0028176313 scopus 로고
    • Expression of β1-6-branched N-linked oligosaccharides is associated with activation in human T4 and T8 cell populations
    • Lemaire S., Derappe C., Michalski J.C., Aubery M., Neel D. Expression of β1-6-branched N-linked oligosaccharides is associated with activation in human T4 and T8 cell populations. J. Biol. Chem. 269:1994;8069-8074.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8069-8074
    • Lemaire, S.1    Derappe, C.2    Michalski, J.C.3    Aubery, M.4    Neel, D.5
  • 67
    • 0028047269 scopus 로고
    • Tumor cell surface beta 1-6 branched oligosaccharides and lung metastasis
    • Lu Y., Pelling J.C., Chaney W.G. Tumor cell surface beta 1-6 branched oligosaccharides and lung metastasis. Clin. Exp. Metastasis. 12:1994;47-54.
    • (1994) Clin. Exp. Metastasis , vol.12 , pp. 47-54
    • Lu, Y.1    Pelling, J.C.2    Chaney, W.G.3
  • 68
    • 0026587657 scopus 로고
    • Induction of mammary tumors by expression of polyomavirus middle T oncogene: A transgenic mouse model for metastatic disease
    • Guy C.T., Cardiff R.D., Muller W.J. Induction of mammary tumors by expression of polyomavirus middle T oncogene: a transgenic mouse model for metastatic disease. Mol. Cell. Biol. 12:1992;954-961.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 954-961
    • Guy, C.T.1    Cardiff, R.D.2    Muller, W.J.3
  • 69
    • 0027954475 scopus 로고
    • Activation of the c-Src tyrosine kinase is required for the induction of mammary tumors in transgenic mice
    • Guy C.T., Muthuswamy S.K., Cardiff R.D., Soriano P., Muller W.J. Activation of the c-Src tyrosine kinase is required for the induction of mammary tumors in transgenic mice. Genes Dev. 8:1994;23-32.
    • (1994) Genes Dev. , vol.8 , pp. 23-32
    • Guy, C.T.1    Muthuswamy, S.K.2    Cardiff, R.D.3    Soriano, P.4    Muller, W.J.5
  • 73
    • 0029150292 scopus 로고
    • Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains
    • Schaller M.D., Otey C.A., Hildebrand J.D., Parsons J.T. Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains. J. Cell. Biol. 130:1995;1181-1187.
    • (1995) J. Cell. Biol. , vol.130 , pp. 1181-1187
    • Schaller, M.D.1    Otey, C.A.2    Hildebrand, J.D.3    Parsons, J.T.4
  • 74
    • 0029066887 scopus 로고
    • Increased glycosylation of beta 1 integrins affects the interaction of transformed S115 mammary epithelial cells with laminin-1
    • Leppa S., Heino J., Jalkanen M. Increased glycosylation of beta 1 integrins affects the interaction of transformed S115 mammary epithelial cells with laminin-1. Cell Growth Differ. 6:1995;853-861.
    • (1995) Cell Growth Differ. , vol.6 , pp. 853-861
    • Leppa, S.1    Heino, J.2    Jalkanen, M.3
  • 75
    • 0032173448 scopus 로고    scopus 로고
    • T lymphocytes from sezary syndrome patients express beta1 integrins whose β1,6-branched N-linked oligosaccharides reflect their adhesive capacity
    • Braut-Boucher F., Font J., Pichon J., Paulin Y., Boukhelifa M., Aubery M., Derappe C. T lymphocytes from sezary syndrome patients express beta1 integrins whose β1,6-branched N-linked oligosaccharides reflect their adhesive capacity. Leuk. Res. 22:1998;947-952.
    • (1998) Leuk. Res. , vol.22 , pp. 947-952
    • Braut-Boucher, F.1    Font, J.2    Pichon, J.3    Paulin, Y.4    Boukhelifa, M.5    Aubery, M.6    Derappe, C.7
  • 76
    • 0032126529 scopus 로고    scopus 로고
    • Progression of hepatic neoplasms in severely retarded in mice lacking the bisecting N-acetylglucosamine on N-glycans: Evidence for a glycoprotein factor that facilitates hepatic tumor progression
    • Bhaumik M., Harris T., Sundaram S., Johnson L., Guttenplan J., Rogler C., Stanley P. Progression of hepatic neoplasms in severely retarded in mice lacking the bisecting N-acetylglucosamine on N-glycans: evidence for a glycoprotein factor that facilitates hepatic tumor progression. Cancer Res. 58:1998;2881-2887.
    • (1998) Cancer Res. , vol.58 , pp. 2881-2887
    • Bhaumik, M.1    Harris, T.2    Sundaram, S.3    Johnson, L.4    Guttenplan, J.5    Rogler, C.6    Stanley, P.7
  • 77
    • 0030658888 scopus 로고    scopus 로고
    • Carcinoma-associated expression of core 2 β-1,6-N-Acetylglucosaminyltransferase gene in human colorectal cancer: Role of O-glycans in tumor progression
    • Shimodaira K., Nakayama J., Nakamura N., Hasebe O., Katsuyama T., Fukuda M. Carcinoma-associated expression of core 2 β-1,6-N-Acetylglucosaminyltransferase gene in human colorectal cancer: role of O-glycans in tumor progression. Cancer Res. 57:1997;5201-5206.
    • (1997) Cancer Res. , vol.57 , pp. 5201-5206
    • Shimodaira, K.1    Nakayama, J.2    Nakamura, N.3    Hasebe, O.4    Katsuyama, T.5    Fukuda, M.6
  • 78
    • 0025778637 scopus 로고
    • Mucin production by human colonic carcinoma cells correlates with their metastatic potential in animal models of colon cancer metastasis
    • Bresalier R.S., Niv Y., Byrd J.C., Duh Q.Y., Toribara N.W., Rockwell R.W., Dahiya R., Kim Y.S. Mucin production by human colonic carcinoma cells correlates with their metastatic potential in animal models of colon cancer metastasis. J. Clin. Invest. 87:1991;1037-1045.
    • (1991) J. Clin. Invest. , vol.87 , pp. 1037-1045
    • Bresalier, R.S.1    Niv, Y.2    Byrd, J.C.3    Duh, Q.Y.4    Toribara, N.W.5    Rockwell, R.W.6    Dahiya, R.7    Kim, Y.S.8
  • 79
    • 0019720921 scopus 로고
    • Apparent reversion of stable in vivo genetic markers detected in tumor cells from spontaneous metastases
    • Dennis J.W., Donaghue T., Florian M., Kerbel R.S. Apparent reversion of stable in vivo genetic markers detected in tumor cells from spontaneous metastases. Nature. 292:1981;242-245.
    • (1981) Nature , vol.292 , pp. 242-245
    • Dennis, J.W.1    Donaghue, T.2    Florian, M.3    Kerbel, R.S.4
  • 80
    • 0020582781 scopus 로고
    • Spontaneous fusion in vivo between normal host and tumor cells: Possible contribution to tumor progression and metastasis studied with a lectin-resistant mutant tumor
    • Kerbel R.S., Lagarde A.E., Dennis J.W., Donaghue T.P. Spontaneous fusion in vivo between normal host and tumor cells: possible contribution to tumor progression and metastasis studied with a lectin-resistant mutant tumor. Mol. Cell. Biol. 3:1983;523-538.
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 523-538
    • Kerbel, R.S.1    Lagarde, A.E.2    Dennis, J.W.3    Donaghue, T.P.4
  • 81
    • 0022517269 scopus 로고
    • Co-reversion of a lectin-resistant mutation and non-metastatic phenotype in murine tumor cells
    • Dennis J.W., Laferte S. Co-reversion of a lectin-resistant mutation and non-metastatic phenotype in murine tumor cells. Int. J. Cancer. 38:1986;445-450.
    • (1986) Int. J. Cancer , vol.38 , pp. 445-450
    • Dennis, J.W.1    Laferte, S.2
  • 82
    • 0023847949 scopus 로고
    • Isolation and characterization of spontaneous wheat germ agglutinin-resistant human melanoma mutants displaying remarkable different metastatic profiles in nude mice
    • Ishikawa M., Dennis J.W., Kerbel R.S. Isolation and characterization of spontaneous wheat germ agglutinin-resistant human melanoma mutants displaying remarkable different metastatic profiles in nude mice. Cancer Res. 48:1988;665-670.
    • (1988) Cancer Res. , vol.48 , pp. 665-670
    • Ishikawa, M.1    Dennis, J.W.2    Kerbel, R.S.3
  • 83
    • 0029027525 scopus 로고
    • Carcinoembryonic antigen and other glycoconjugates act as ligands for galectin-3 in human colon carcinoma cells
    • Ohannesian D.W., Lotan D., Thomas P., Jessup J.M., Fukuda M., Gabius H.-J., Lotan R. Carcinoembryonic antigen and other glycoconjugates act as ligands for galectin-3 in human colon carcinoma cells. Cancer Res. 55:1995;2191-2199.
    • (1995) Cancer Res. , vol.55 , pp. 2191-2199
    • Ohannesian, D.W.1    Lotan, D.2    Thomas, P.3    Jessup, J.M.4    Fukuda, M.5    Gabius, H.-J.6    Lotan, R.7
  • 84
    • 0023149010 scopus 로고
    • Inhibition of liver metastasis in mice by blocking hepatocyte lectins with arabinogalactan infusions and D-galactose
    • Beuth J., Ko H.L., Oette K., Pulverer G., Roszkowski K., Uhlenbruck G. Inhibition of liver metastasis in mice by blocking hepatocyte lectins with arabinogalactan infusions and D-galactose. J. Cancer Res. Clin. Oncol. 113:1987;51-55.
    • (1987) J. Cancer Res. Clin. Oncol. , vol.113 , pp. 51-55
    • Beuth, J.1    Ko, H.L.2    Oette, K.3    Pulverer, G.4    Roszkowski, K.5    Uhlenbruck, G.6
  • 85
    • 0025365203 scopus 로고
    • Tumor cell surface β1-4 linked galactose binds to lectin(s) on microvascular endothelial cells and contributes to organ colonization
    • Cornil I., Kerbel R.S., Dennis J.W. Tumor cell surface β1-4 linked galactose binds to lectin(s) on microvascular endothelial cells and contributes to organ colonization. J. Cell Biol. 111:1990;773-782.
    • (1990) J. Cell Biol. , vol.111 , pp. 773-782
    • Cornil, I.1    Kerbel, R.S.2    Dennis, J.W.3
  • 86
    • 0028151276 scopus 로고
    • Sialylation and malignant potential in tumor cell glycosylation mutants
    • Takano R., Muchmore E.A., Dennis J.W. Sialylation and malignant potential in tumor cell glycosylation mutants. Glycobiology. 4:1994;665-674.
    • (1994) Glycobiology , vol.4 , pp. 665-674
    • Takano, R.1    Muchmore, E.A.2    Dennis, J.W.3
  • 87
    • 0020072919 scopus 로고
    • Enzymatic basis for a lectin resistant phenotype: Increase in a fucosyltransferase in mouse melanoma cells
    • Finne J., Burger M.M., Prieels J.P. Enzymatic basis for a lectin resistant phenotype: increase in a fucosyltransferase in mouse melanoma cells. J. Cell Biol. 92:1982;277-282.
    • (1982) J. Cell Biol. , vol.92 , pp. 277-282
    • Finne, J.1    Burger, M.M.2    Prieels, J.P.3
  • 88
    • 0022489292 scopus 로고
    • Different metastatic phenotypes in two genetic classes of WGA-resistant tumor cell mutants
    • Dennis J.W. Different metastatic phenotypes in two genetic classes of WGA-resistant tumor cell mutants. Cancer Res. 46:1986;4594-4600.
    • (1986) Cancer Res. , vol.46 , pp. 4594-4600
    • Dennis, J.W.1
  • 89
    • 0026329997 scopus 로고
    • CMP-N-acetylneuraminic acid hydroxylase activity determines the wheat germ agglutinin-binding phenotype in two mutants of the lymphoma cell line MDAY-D2
    • Shaw L., Yousefi S., Dennis J.W., Schauer R. CMP-N-acetylneuraminic acid hydroxylase activity determines the wheat germ agglutinin-binding phenotype in two mutants of the lymphoma cell line MDAY-D2. Glycoconjugate. 8:1991;434-441.
    • (1991) Glycoconjugate , vol.8 , pp. 434-441
    • Shaw, L.1    Yousefi, S.2    Dennis, J.W.3    Schauer, R.4
  • 90
    • 0028898988 scopus 로고
    • High α2,6-sialylation of N-acetyllactosamine sequences in ras-transformed rat fibroblasts correlates with high invasive potential
    • Le Marer N., Stéhelin D. High α2,6-sialylation of N-acetyllactosamine sequences in ras-transformed rat fibroblasts correlates with high invasive potential. Glycobiology. 5:1995;219-226.
    • (1995) Glycobiology , vol.5 , pp. 219-226
    • Le Marer, N.1    Stéhelin, D.2
  • 94
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte migration: The multistep paradigm
    • Springer T.A. Traffic signals for lymphocyte recirculation and leukocyte migration: the multistep paradigm. Cell. 76:1994;301-314.
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 95
    • 0030041932 scopus 로고    scopus 로고
    • Post-translational modifications of recombinant P-selectin glycoprotein ligand-1 required for binding to P- And E-selectin
    • Li F., Wilkins P.P., Crawley S., Weinstein J., Cummings R.D., McEver R.P. Post-translational modifications of recombinant P-selectin glycoprotein ligand-1 required for binding to P- and E-selectin. J. Biol. Chem. 271:1996;3255-3264.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3255-3264
    • Li, F.1    Wilkins, P.P.2    Crawley, S.3    Weinstein, J.4    Cummings, R.D.5    McEver, R.P.6
  • 98
  • 99
    • 0027363373 scopus 로고
    • Systemic metastasis of medulloblastoma through vetriculoperitoneal shunt report of a case and critical analysis of the literature
    • Jamjoom Z.A., Jamjoom A.B., Sulaiman A.H., Naim-Ur-Rahman A.R.A. Systemic metastasis of medulloblastoma through vetriculoperitoneal shunt report of a case and critical analysis of the literature. Surg. Neurol. 40:1993;403-410.
    • (1993) Surg. Neurol. , vol.40 , pp. 403-410
    • Jamjoom, Z.A.1    Jamjoom, A.B.2    Sulaiman, A.H.3    Naim-Ur-Rahman, A.R.A.4
  • 100
    • 0024435241 scopus 로고
    • Evidence that β1-6 branched Asn-linked oligosaccharides on metastatic tumor cells facilitate invasion of basement membranes
    • Yagel S., Feinmesser R., Waghorne C., Lala P.K., Breitman M.L., Dennis J.W. Evidence that β1-6 branched Asn-linked oligosaccharides on metastatic tumor cells facilitate invasion of basement membranes. Int. J. Cancer. 44:1989;685-690.
    • (1989) Int. J. Cancer , vol.44 , pp. 685-690
    • Yagel, S.1    Feinmesser, R.2    Waghorne, C.3    Lala, P.K.4    Breitman, M.L.5    Dennis, J.W.6
  • 101
    • 0027407423 scopus 로고
    • Inhibition of N-linked oligosaccharide processing in tumor cells is associated with enhanced tissue inhibitor of metalloproteinases (TIMP) gene expression
    • Korczak B., Dennis J.W. Inhibition of N-linked oligosaccharide processing in tumor cells is associated with enhanced tissue inhibitor of metalloproteinases (TIMP) gene expression. Int. J. Cancer. 53:1993;634-639.
    • (1993) Int. J. Cancer , vol.53 , pp. 634-639
    • Korczak, B.1    Dennis, J.W.2
  • 102
    • 0026134550 scopus 로고
    • Human melanoma cell invasion is inhibited in vitro by swainsonine and deoxymannojirimycin with a concomitant decrease in collagenase IV expression
    • Seftor R.E.B., Seftor E.A., Grimes W.J., Liotta L.A., Stetler-Stevenson W.G., Welch D.R., Hendrix M.J.C. Human melanoma cell invasion is inhibited in vitro by swainsonine and deoxymannojirimycin with a concomitant decrease in collagenase IV expression. Melanoma Res. 1:1991;43-54.
    • (1991) Melanoma Res. , vol.1 , pp. 43-54
    • Seftor, R.E.B.1    Seftor, E.A.2    Grimes, W.J.3    Liotta, L.A.4    Stetler-Stevenson, W.G.5    Welch, D.R.6    Hendrix, M.J.C.7
  • 103
    • 0032055870 scopus 로고    scopus 로고
    • Prognostic values of matrix metalloproteinase-2 and tissue inhibitor of metalloproteinase-2 expression in bladder cancer
    • Kanayama H., Yokota K., Kurokawa Y., Murakami Y., Nishitani M., Kagawa S. Prognostic values of matrix metalloproteinase-2 and tissue inhibitor of metalloproteinase-2 expression in bladder cancer. Cancer. 82:1998;1359-1366.
    • (1998) Cancer , vol.82 , pp. 1359-1366
    • Kanayama, H.1    Yokota, K.2    Kurokawa, Y.3    Murakami, Y.4    Nishitani, M.5    Kagawa, S.6
  • 104
    • 0029128356 scopus 로고
    • Inhibitors of carbohydrate processing: A new class of anticancer agents
    • Goss P.E., Baker M.A., Carver J.P., Dennis J.W. Inhibitors of carbohydrate processing: a new class of anticancer agents. Clin. Cancer Res. 1:1995;935-944.
    • (1995) Clin. Cancer Res. , vol.1 , pp. 935-944
    • Goss, P.E.1    Baker, M.A.2    Carver, J.P.3    Dennis, J.W.4
  • 106
    • 0030878261 scopus 로고    scopus 로고
    • Phase IB clinical trial of the oligosaccharide processing inhibitor swainsonine in patients with advanced malignancies
    • Goss P.E., Reid C.L., Bailey D., Dennis J.W. Phase IB clinical trial of the oligosaccharide processing inhibitor swainsonine in patients with advanced malignancies. Clin. Cancer Res. 3:1997;1077-1086.
    • (1997) Clin. Cancer Res. , vol.3 , pp. 1077-1086
    • Goss, P.E.1    Reid, C.L.2    Bailey, D.3    Dennis, J.W.4
  • 107
    • 0023024147 scopus 로고
    • Transfer of non-glucosylated oligosaccharides from lipid to protein in mammalian cells
    • Romero P.A., Herscovics A. Transfer of non-glucosylated oligosaccharides from lipid to protein in mammalian cells. J. Biol. Chem. 261:1986;15936-15940.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15936-15940
    • Romero, P.A.1    Herscovics, A.2
  • 108
    • 0031034352 scopus 로고    scopus 로고
    • Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness
    • Palecek S.P., Loftus J.C., Ginsberg M.H., Lauffenburger D.A., Horwitz A.F. Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness. Nature. 385:1997;537-540.
    • (1997) Nature , vol.385 , pp. 537-540
    • Palecek, S.P.1    Loftus, J.C.2    Ginsberg, M.H.3    Lauffenburger, D.A.4    Horwitz, A.F.5
  • 109
    • 0023919659 scopus 로고
    • Structures, function, and transformational changes of the sugar chains of glycohormones
    • Kobata A. Structures, function, and transformational changes of the sugar chains of glycohormones. J. Cell Biochem. 37:1988;79-90.
    • (1988) J. Cell Biochem. , vol.37 , pp. 79-90
    • Kobata, A.1
  • 110
    • 0031959770 scopus 로고    scopus 로고
    • Galectins versatile modulators of cell adhesion, cell proliferation, and cell death
    • Perillo N.L., Marcus M.E., Baum L.G. Galectins versatile modulators of cell adhesion, cell proliferation, and cell death. J. Mol. Med. 76:1998;402-412.
    • (1998) J. Mol. Med. , vol.76 , pp. 402-412
    • Perillo, N.L.1    Marcus, M.E.2    Baum, L.G.3
  • 111
    • 0030993376 scopus 로고    scopus 로고
    • CD22, a B lymphocyte-specific adhesion molecule that regulates antigen receptor signaling
    • Tedder T.F., Tuscano J., Sato S., Kehrl J.H. CD22, a B lymphocyte-specific adhesion molecule that regulates antigen receptor signaling. Annu. Rev. Immunol. 15:1997;481-504.
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 481-504
    • Tedder, T.F.1    Tuscano, J.2    Sato, S.3    Kehrl, J.H.4


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