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Volumn 196, Issue 1, 2003, Pages 101-107

Differences in glycosylation of intracellular proteins between benign and malignant thyroid neoplasms

Author keywords

Enzyme linked lectino solid phase assay; Intracellular glycoproteins; Lectins; Thyroid lesions

Indexed keywords

AGGLUTININ; CELL PROTEIN; LECTIN; NUCLEAR PROTEIN; VEGETABLE PROTEIN;

EID: 0038645282     PISSN: 03043835     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-3835(03)00206-4     Document Type: Article
Times cited : (14)

References (33)
  • 1
    • 0032168441 scopus 로고    scopus 로고
    • Evolving views of protein glycosylation
    • Drickamer K., Taylor M.E. Evolving views of protein glycosylation. TIBS. 23:1998;321-324.
    • (1998) TIBS , vol.23 , pp. 321-324
    • Drickamer, K.1    Taylor, M.E.2
  • 2
    • 0033566020 scopus 로고    scopus 로고
    • Glycoproteins: Glycan presentation and protein-fold stability
    • Wormald M.R., Dwek R.A. Glycoproteins: glycan presentation and protein-fold stability. Structure. 7:1999;155-160.
    • (1999) Structure , vol.7 , pp. 155-160
    • Wormald, M.R.1    Dwek, R.A.2
  • 3
    • 0031305493 scopus 로고    scopus 로고
    • Effect of carbohydrate moieties on the stability of nuclear glycoproteins from hamster liver
    • Krzeslak A., Lipinska A. Effect of carbohydrate moieties on the stability of nuclear glycoproteins from hamster liver. Cytobios. 89:1997;161-171.
    • (1997) Cytobios , vol.89 , pp. 161-171
    • Krzeslak, A.1    Lipinska, A.2
  • 4
    • 0032734974 scopus 로고    scopus 로고
    • O-GlcNAc and the control of gene expression
    • Comer F.I., Hart G.W. O-GlcNAc and the control of gene expression. Biochim. Biophys. Acta. 1473:1999;161-171.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 161-171
    • Comer, F.I.1    Hart, G.W.2
  • 5
    • 0034703095 scopus 로고    scopus 로고
    • O-glycosylation of nuclear and cytosolic proteins. Dynamic interplay between O-GlcNAc and O-phosphate
    • Comer F.I., Hart G.W. O-glycosylation of nuclear and cytosolic proteins. Dynamic interplay between O-GlcNAc and O-phosphate. J. Biol. Chem. 275:2000;179-182.
    • (2000) J. Biol. Chem. , vol.275 , pp. 179-182
    • Comer, F.I.1    Hart, G.W.2
  • 6
    • 0035937586 scopus 로고    scopus 로고
    • Glycosylation of nucleocytoplasmic proteins: Signal transduction and O-GlcNAc
    • Wells L., Vosseller K., Hart G.W. Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc. Science. 291:2001;2376-2378.
    • (2001) Science , vol.291 , pp. 2376-2378
    • Wells, L.1    Vosseller, K.2    Hart, G.W.3
  • 7
    • 0034851055 scopus 로고    scopus 로고
    • Nucleocytoplasmic O-glycosylation: O-GlcNAc and functional proteomics
    • Vosseller K., Wells L., Hart G.W. Nucleocytoplasmic O-glycosylation: O-GlcNAc and functional proteomics. Biochimie. 83:2001;575-581.
    • (2001) Biochimie , vol.83 , pp. 575-581
    • Vosseller, K.1    Wells, L.2    Hart, G.W.3
  • 9
    • 0030745147 scopus 로고    scopus 로고
    • Perspectives on the significance of altered glycosylation of glycoproteins in cancer
    • Kim Y.J., Varki A. Perspectives on the significance of altered glycosylation of glycoproteins in cancer. Glycoconjugate J. 14:1997;569-576.
    • (1997) Glycoconjugate J. , vol.14 , pp. 569-576
    • Kim, Y.J.1    Varki, A.2
  • 10
    • 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
  • 11
    • 0038564462 scopus 로고    scopus 로고
    • Glycoproteins and glycosylation changes in cancer
    • J.R. Bertino. New York: Academic Press
    • Ho S.B., Kim Y.S. Glycoproteins and glycosylation changes in cancer. Bertino J.R. Encyclopedia of Cancer. 1996;744-759 Academic Press, New York.
    • (1996) Encyclopedia of Cancer , pp. 744-759
    • Ho, S.B.1    Kim, Y.S.2
  • 13
    • 0032760680 scopus 로고    scopus 로고
    • Pathways of Oglycan biosynthesis in cancer cells
    • Brockhausen I. Pathways of Oglycan biosynthesis in cancer cells. Biochim. Biophys. Acta. 1473:1999;67-95.
    • (1999) Biochim. Biophys. Acta. , vol.1473 , pp. 67-95
    • Brockhausen, I.1
  • 14
    • 0000245728 scopus 로고
    • Isolation of pure and unaltered liver nuclei morphology and biochemical composition
    • Chauveau J., Moulé Y., Rouiller C. Isolation of pure and unaltered liver nuclei morphology and biochemical composition. Exp. Cell. Res. 11:1956;317-321.
    • (1956) Exp. Cell. Res. , vol.11 , pp. 317-321
    • Chauveau, J.1    Moulé, Y.2    Rouiller, C.3
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0015236352 scopus 로고
    • Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane
    • Fairbanks G., Steck T.L., Wallach D.F. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 10:1971;2606-2617.
    • (1971) Biochemistry , vol.10 , pp. 2606-2617
    • Fairbanks, G.1    Steck, T.L.2    Wallach, D.F.3
  • 17
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets; Procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets; procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:1979;4350-4355.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4355
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 18
    • 0021103795 scopus 로고
    • 4 isolectin for the detection of α-D-galactopyranosyl end groups
    • 4 isolectin for the detection of α-D-galactopyranosyl end groups. Anal. Biochem. 130:1983;437-444.
    • (1983) Anal. Biochem. , vol.130 , pp. 437-444
    • McCoy, J.P.1    Varani, J.2    Goldstein, I.J.3
  • 21
    • 0242499609 scopus 로고    scopus 로고
    • Galectin-3 and laminin expression in neoplastic and non-neoplastic thyroid tissue
    • Fernandez P.L., Merino M.J., Gomez M., et al. Galectin-3 and laminin expression in neoplastic and non-neoplastic thyroid tissue. J. Pathol. 181:1997;80-86.
    • (1997) J. Pathol. , vol.181 , pp. 80-86
    • Fernandez, P.L.1    Merino, M.J.2    Gomez, M.3
  • 22
    • 0032527914 scopus 로고    scopus 로고
    • Galectin-3 is a presurgical marker of human thyroid carcinoma
    • Orlandi F., Saggiorato E., Pivano G., et al. Galectin-3 is a presurgical marker of human thyroid carcinoma. Cancer Res. 58:1998;3015-3020.
    • (1998) Cancer Res. , vol.58 , pp. 3015-3020
    • Orlandi, F.1    Saggiorato, E.2    Pivano, G.3
  • 23
    • 0033151803 scopus 로고    scopus 로고
    • Expression of galectin-3 in fine-needle aspirates as a diagnostic marker differentiating benign from malignant thyroid neoplasms
    • Inohara H., Honjo Y., Yoshii T., et al. Expression of galectin-3 in fine-needle aspirates as a diagnostic marker differentiating benign from malignant thyroid neoplasms. Cancer. 11:1999;2475-2484.
    • (1999) Cancer , vol.11 , pp. 2475-2484
    • Inohara, H.1    Honjo, Y.2    Yoshii, T.3
  • 24
    • 0034065728 scopus 로고    scopus 로고
    • Galectin-3 expression in various thyroid neoplasms and its possible role in metastasis formation
    • Kawachi K., Matsushita Y., Yonezawa S., et al. Galectin-3 expression in various thyroid neoplasms and its possible role in metastasis formation. Human Pathol. 31:2000;428-433.
    • (2000) Human Pathol. , vol.31 , pp. 428-433
    • Kawachi, K.1    Matsushita, Y.2    Yonezawa, S.3
  • 25
    • 0035319230 scopus 로고    scopus 로고
    • Galectin-3 maintains the transformed phenotype of thyroid papillary carcinoma cells
    • Yoshii T., Inohara H., Takenaka Y., et al. Galectin-3 maintains the transformed phenotype of thyroid papillary carcinoma cells. Int. J. Oncol. 18:2001;787-792.
    • (2001) Int. J. Oncol. , vol.18 , pp. 787-792
    • Yoshii, T.1    Inohara, H.2    Takenaka, Y.3
  • 26
    • 0036156211 scopus 로고    scopus 로고
    • Galectin-3, a marker of well differentiated thyroid carcinoma, is expressed in thyroid nodules with cytological atypia
    • Coli A., Bigotti G., Zuccheti F., Negro F., Massi G. Galectin-3, a marker of well differentiated thyroid carcinoma, is expressed in thyroid nodules with cytological atypia. Histopathology. 40:2002;80-87.
    • (2002) Histopathology , vol.40 , pp. 80-87
    • Coli, A.1    Bigotti, G.2    Zuccheti, F.3    Negro, F.4    Massi, G.5
  • 29
    • 0035258771 scopus 로고    scopus 로고
    • Galectins, galactoside-binding mammalian lectins: Clinical application of multi-functional proteins
    • Wada J., Makino H. Galectins, galactoside-binding mammalian lectins: clinical application of multi-functional proteins. Acta. Med. Okayama. 55:2001;11-17.
    • (2001) Acta. Med. Okayama , vol.55 , pp. 11-17
    • Wada, J.1    Makino, H.2
  • 30
    • 0036606914 scopus 로고    scopus 로고
    • Galectins and their ligands: Amplifiers, silencers or tuners of the inflammatory response?
    • Rabinovich G.A., Baum L.G., Tinari N., et al. Galectins and their ligands: amplifiers, silencers or tuners of the inflammatory response? Trends Immunol. 23:2002;313-320.
    • (2002) Trends Immunol. , vol.23 , pp. 313-320
    • Rabinovich, G.A.1    Baum, L.G.2    Tinari, N.3
  • 31
    • 0034851982 scopus 로고    scopus 로고
    • Galectins as modulators of cell adhesion
    • Hughes R.C. Galectins as modulators of cell adhesion. Biochimie. 83:2001;667-676.
    • (2001) Biochimie , vol.83 , pp. 667-676
    • Hughes, R.C.1
  • 32
    • 0346975145 scopus 로고
    • Use of lectins
    • Verbert A. Switzerland: Harwood Academic Publishers GmbH
    • Debray H. Use of lectins. Verbert A. Methods on Glycoconjugates Harwood. 1995:1995;103-133 Harwood Academic Publishers GmbH, Switzerland.
    • (1995) Methods on Glycoconjugates Harwood , vol.1995 , pp. 103-133
    • Debray, H.1
  • 33
    • 0035181926 scopus 로고    scopus 로고
    • Galectin-3 as a presurgical immunocytodiagnostic marker of minimally invasive follicular thyroid carcinoma
    • Saggiorato E., Cappia S., De Giuli P., et al. Galectin-3 as a presurgical immunocytodiagnostic marker of minimally invasive follicular thyroid carcinoma. J. Clin. Endocrinol. Metabol. 86:2001;5152-5158.
    • (2001) J. Clin. Endocrinol. Metabol. , vol.86 , pp. 5152-5158
    • Saggiorato, E.1    Cappia, S.2    De Giuli, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.