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Volumn 287, Issue 43, 2012, Pages 35873-35886

Evaluation of riproximin binding properties reveals a novel mechanism for cellular targeting

Author keywords

[No Author keywords available]

Indexed keywords

ASIALOFETUIN; BINDING INTERACTION; BINDING PROPERTIES; BINDING SPECIFICITIES; BIOLOGICAL IMPLICATIONS; CARBOHYDRATE MICROARRAYS; CELL SURFACES; CELLULAR ASSAYS; CROSS-LINKING ABILITY; CROSSLINKS; CYTOTOXIC; DEGREE OF SPECIFICITY; GLYCANS; GLYCOCONJUGATES; HIGH SELECTIVITY; MODEL PROTEINS; N-ACETYL-D-GALACTOSAMINE; N-GLYCAN STRUCTURES; ON DYNAMICS; RIBOSOME-INACTIVATING PROTEIN; SUGAR BINDING; TUMOR CELL LINES; TYPE II;

EID: 84867753157     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.368548     Document Type: Article
Times cited : (18)

References (61)
  • 1
    • 33644971594 scopus 로고    scopus 로고
    • Identification of potent anti-cancer activity in Ximenia americana aqueous extracts used by African traditional medicine
    • Voss, C., Eyol, E., and Berger, M. R. (2006) Identification of potent anti-cancer activity in Ximenia americana aqueous extracts used by African traditional medicine. Toxicol. Appl. Pharmacol. 211, 177-187
    • (2006) Toxicol. Appl. Pharmacol. , vol.211 , pp. 177-187
    • Voss, C.1    Eyol, E.2    Berger, M.R.3
  • 2
    • 33845649761 scopus 로고    scopus 로고
    • Identification and characterization of riproximin, a new type II ribosome-inactivating protein with antineoplastic activity from Ximenia americana
    • Voss, C., Eyol, E., Frank, M., von der Lieth, C. W., and Berger, M. R. (2006) Identification and characterization of riproximin, a new type II ribosome-inactivating protein with antineoplastic activity from Ximenia americana. FASEB J. 20, 1194-1196
    • (2006) FASEB J. , vol.20 , pp. 1194-1196
    • Voss, C.1    Eyol, E.2    Frank, M.3    Von Der Lieth, C.W.4    Berger, M.R.5
  • 4
    • 33747229123 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins. Progress and problems
    • Stirpe, F., and Battelli, M. G. (2006) Ribosome-inactivating proteins. Progress and problems. Cell Mol. Life Sci. 63, 1850-1866
    • (2006) Cell Mol. Life Sci. , vol.63 , pp. 1850-1866
    • Stirpe, F.1    Battelli, M.G.2
  • 5
    • 0023947126 scopus 로고
    • The RNA N-glycosidase activity of ricin A-chain. The characteristics of the enzymatic activity of ricin A-chain with ribosomes and with rRNA
    • Endo, Y., and Tsurugi, K. (1988) The RNA N-glycosidase activity of ricin A-chain. The characteristics of the enzymatic activity of ricin A-chain with ribosomes and with rRNA. J. Biol. Chem. 263, 8735-8739
    • (1988) J. Biol. Chem. , vol.263 , pp. 8735-8739
    • Endo, Y.1    Tsurugi, K.2
  • 6
    • 79953695935 scopus 로고    scopus 로고
    • Plant ribosome-inactivating proteins type II induce the unfolded protein response in human cancer cells
    • Horrix, C., Raviv, Z., Flescher, E., Voss, C., and Berger, M. R. (2011) Plant ribosome-inactivating proteins type II induce the unfolded protein response in human cancer cells. Cell Mol. Life Sci. 68, 1269-1281
    • (2011) Cell Mol. Life Sci. , vol.68 , pp. 1269-1281
    • Horrix, C.1    Raviv, Z.2    Flescher, E.3    Voss, C.4    Berger, M.R.5
  • 8
    • 77950410995 scopus 로고    scopus 로고
    • Alterations in glycosylation as biomarkers for cancer detection
    • Reis, C. A., Osorio, H., Silva, L., Gomes, C., and David, L. (2010) Alterations in glycosylation as biomarkers for cancer detection. J. Clin. Pathol. 63, 322-329
    • (2010) J. Clin. Pathol. , vol.63 , pp. 322-329
    • Reis, C.A.1    Osorio, H.2    Silva, L.3    Gomes, C.4    David, L.5
  • 10
    • 50449083310 scopus 로고    scopus 로고
    • Evaluation of the serum N-linked glycome for the diagnosis of cancer and chronic inflammation
    • Arnold, J. N., Saldova, R., Hamid, U. M., and Rudd, P. M. (2008) Evaluation of the serum N-linked glycome for the diagnosis of cancer and chronic inflammation. Proteomics. 8, 3284-3293
    • (2008) Proteomics. , vol.8 , pp. 3284-3293
    • Arnold, J.N.1    Saldova, R.2    Hamid, U.M.3    Rudd, P.M.4
  • 15
    • 79551697660 scopus 로고    scopus 로고
    • N-Glycosylation of total cellular glycoproteins from the human ovarian carcinoma SKOV3 cell line and of recombinantly expressed human erythropoietin
    • Machado, E., Kandzia, S., Carilho, R., Altevogt, P., Conradt, H. S., and Costa, J. (2011) N-Glycosylation of total cellular glycoproteins from the human ovarian carcinoma SKOV3 cell line and of recombinantly expressed human erythropoietin. Glycobiology 21, 376-386
    • (2011) Glycobiology , vol.21 , pp. 376-386
    • Machado, E.1    Kandzia, S.2    Carilho, R.3    Altevogt, P.4    Conradt, H.S.5    Costa, J.6
  • 16
    • 0014954212 scopus 로고
    • Abrin and ricin. New anti-tumor substances
    • Lin, J. Y., Tserng, K. Y., Chen, C. C., Lin, L. T., and Tung, T. C. (1970) Abrin and ricin. New anti-tumor substances. Nature 227, 292-293
    • (1970) Nature , vol.227 , pp. 292-293
    • Lin, J.Y.1    Tserng, K.Y.2    Chen, C.C.3    Lin, L.T.4    Tung, T.C.5
  • 17
    • 0021369395 scopus 로고
    • Phase I study of the plant protein ricin
    • Fodstad, O., Kvalheim, G., Godal, A., Lotsberg, J., Aamdal, S., Høst, H., and Pihl, A. (1984) Phase I study of the plant protein ricin. Cancer Res. 44, 862-865 (Pubitemid 14184632)
    • (1984) Cancer Research , vol.44 , Issue.2 , pp. 862-865
    • Fodstad, O.1    Kvalheim, G.2    Godal, A.3
  • 18
    • 77956404731 scopus 로고    scopus 로고
    • Multivalent lectin-carbohydrate interactions energetics and mechanisms of binding
    • Dam, T. K., and Brewer, C. F. (2010) Multivalent lectin-carbohydrate interactions energetics and mechanisms of binding. Adv. Carbohydr. Chem. Biochem. 63, 139-164
    • (2010) Adv. Carbohydr. Chem. Biochem. , vol.63 , pp. 139-164
    • Dam, T.K.1    Brewer, C.F.2
  • 19
    • 24944450621 scopus 로고    scopus 로고
    • Galectins bind to the multivalent glycoprotein asialofetuin with enhanced affinities and a gradient of decreasing binding constants
    • DOI 10.1021/bi051144z
    • Dam, T. K., Gabius, H. J., André, S., Kaltner, H., Lensch, M., and Brewer, C. F. (2005) Galectins bind to the multivalent glycoprotein asialofetuin with enhanced affinities and a gradient of decreasing binding constants. Biochemistry 44, 12564-12571 (Pubitemid 41324347)
    • (2005) Biochemistry , vol.44 , Issue.37 , pp. 12564-12571
    • Dam, T.K.1    Gabius, H.-J.2    Andre, S.3    Kaltner, H.4    Lensch, M.5    Brewer, C.F.6
  • 20
    • 34948892209 scopus 로고    scopus 로고
    • Binding studies of α-GalNAc-specific lectins to the alpha-GalNAc (Tn-antigen) form of porcine submaxillary mucin and its smaller fragments
    • DOI 10.1074/jbc.M704677200
    • Dam, T. K., Gerken, T. A., Cavada, B. S., Nascimento, K. S., Moura, T. R., and Brewer, C. F. (2007) Binding studies of α-GalNAc-specific lectins to the alpha-GalNAc (Tn-antigen) form of porcine submaxillary mucin and its smaller fragments. J. Biol. Chem. 282, 28256-28263 (Pubitemid 47529520)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.38 , pp. 28256-28263
    • Dam, T.K.1    Gerken, T.A.2    Cavada, B.S.3    Nascimento, K.S.4    Moura, T.R.5    Brewer, C.F.6
  • 21
    • 67650351512 scopus 로고    scopus 로고
    • Microarrays with varying carbohydrate density reveal distinct subpopulations of serum antibodies
    • Oyelaran, O., Li, Q., Farnsworth, D., and Gildersleeve, J. C. (2009) Microarrays with varying carbohydrate density reveal distinct subpopulations of serum antibodies. J. Proteome. Res. 8, 3529-3538
    • (2009) J. Proteome. Res. , vol.8 , pp. 3529-3538
    • Oyelaran, O.1    Li, Q.2    Farnsworth, D.3    Gildersleeve, J.C.4
  • 22
    • 0036193564 scopus 로고    scopus 로고
    • Carbohydrate microarrays for the recognition of cross-reactive molecular markers of microbes and host cells
    • DOI 10.1038/nbt0302-275
    • Wang, D., Liu, S., Trummer, B. J., Deng, C., and Wang, A. (2002) Carbohydrate microarrays for the recognition of cross-reactive molecular markers of microbes and host cells. Nat. Biotechnol. 20, 275-281 (Pubitemid 34205421)
    • (2002) Nature Biotechnology , vol.20 , Issue.3 , pp. 275-281
    • Wang, D.1    Liu, S.2    Trummer, B.J.3    Deng, C.4    Wang, A.5
  • 24
    • 58249137027 scopus 로고    scopus 로고
    • A small-scale method for the preparation of plant N-linked glycans from soluble proteins for analysis by MALDI-TOF mass spectrometry
    • Karg, S. R., Frey, A. D., Ferrara, C., Streich, D. K., Umaña, P., and Kallio, P. T. (2009) A small-scale method for the preparation of plant N-linked glycans from soluble proteins for analysis by MALDI-TOF mass spectrometry. Plant Physiol. Biochem. 47, 160-166
    • (2009) Plant Physiol. Biochem. , vol.47 , pp. 160-166
    • Karg, S.R.1    Frey, A.D.2    Ferrara, C.3    Streich, D.K.4    Umaña, P.5    Kallio, P.T.6
  • 25
    • 0014501234 scopus 로고
    • Preparation of glycopeptides from bovine submaxillary mucin by chemical degradation
    • Downs, F., and Pigman, W. (1969) Preparation of glycopeptides from bovine submaxillary mucin by chemical degradation. Biochemistry 8, 1760-1766
    • (1969) Biochemistry , vol.8 , pp. 1760-1766
    • Downs, F.1    Pigman, W.2
  • 26
    • 0014423859 scopus 로고
    • Purification and characterization of bovine and ovine submaxillary mucins
    • Tettamanti, G., and Pigman, W. (1968) Purification and characterization of bovine and ovine submaxillary mucins. Arch. Biochem. Biophys. 124, 41-50
    • (1968) Arch. Biochem. Biophys. , vol.124 , pp. 41-50
    • Tettamanti, G.1    Pigman, W.2
  • 27
    • 79953298901 scopus 로고    scopus 로고
    • Confidence intervals of interaction index for assessing multiple drug interaction
    • Lee, J. J., and Kong, M. (2009) Confidence intervals of interaction index for assessing multiple drug interaction. Stat. Biopharm. Res. 1, 4-17
    • (2009) Stat. Biopharm. Res. , vol.1 , pp. 4-17
    • Lee, J.J.1    Kong, M.2
  • 28
    • 1442300119 scopus 로고    scopus 로고
    • Identification of Common Structural Features of Binding Sites in Galactose-Specific Proteins
    • DOI 10.1002/prot.10612
    • Sujatha, M. S., and Balaji, P. V. (2004) Identification of common structural features of binding sites in galactose-specific proteins. Proteins 55, 44-65 (Pubitemid 38292833)
    • (2004) Proteins: Structure, Function and Genetics , vol.55 , Issue.1 , pp. 44-65
    • Sujatha, M.S.1    Balaji, P.V.2
  • 29
    • 27944471904 scopus 로고    scopus 로고
    • Carbohydrate recognition factors of the lectin domains present in the Ricinus communis toxic protein (ricin)
    • DOI 10.1016/j.biochi.2005.07.007, PII S0300908405001859
    • Wu, J. H., Singh, T., Herp, A., and Wu, A. M. (2006) Carbohydrate recognition factors of the lectin domains present in the Ricinus communis toxic protein (ricin). Biochimie 88, 201-217 (Pubitemid 41668611)
    • (2006) Biochimie , vol.88 , Issue.2 , pp. 201-217
    • Wu, J.H.1    Singh, T.2    Herp, A.3    Wu, A.M.4
  • 30
    • 1242337458 scopus 로고    scopus 로고
    • Mucins and mucin binding proteins in colorectal cancer
    • DOI 10.1023/A:1025815113599
    • Byrd, J. C., and Bresalier, R. S. (2004) Mucins and mucin binding proteins in colorectal cancer. Cancer Metastasis Rev. 23, 77-99 (Pubitemid 38221597)
    • (2004) Cancer and Metastasis Reviews , vol.23 , Issue.1-2 , pp. 77-99
    • Byrd, J.C.1    Bresalier, R.S.2
  • 31
    • 79951801155 scopus 로고    scopus 로고
    • The Tn antigen. Structural simplicity and biological complexity
    • Ju, T., Otto, V. I., and Cummings, R. D. (2011) The Tn antigen. Structural simplicity and biological complexity. Angew. Chem. Int. Ed Engl. 50, 1770-1791
    • (2011) Angew. Chem. Int. Ed Engl. , vol.50 , pp. 1770-1791
    • Ju, T.1    Otto, V.I.2    Cummings, R.D.3
  • 32
    • 0021141716 scopus 로고
    • T and Tn, general carcinoma autoantigens
    • Springer, G. F. (1984) T and Tn, general carcinoma autoantigens. Science 224, 1198-1206
    • (1984) Science , vol.224 , pp. 1198-1206
    • Springer, G.F.1
  • 33
    • 24744436431 scopus 로고    scopus 로고
    • Molecular basis of incomplete O-glycan synthesis in MCF-7 breast cancer cells: Putative role of MUC6 in Tn antigen expression
    • DOI 10.1158/0008-5472.CAN-04-3746
    • Freire, T., Bay, S., von Mensdorff-Pouilly, S., and Osinaga, E. (2005) Molecular basis of incomplete O-glycan synthesis in MCF-7 breast cancer cells. Putative role of MUC6 in Tn antigen expression. Cancer Res. 65, 7880-7887 (Pubitemid 41297265)
    • (2005) Cancer Research , vol.65 , Issue.17 , pp. 7880-7887
    • Freire, T.1    Bay, S.2    Von Mensdorff-Pouilly, S.3    Osinaga, E.4
  • 34
    • 0035110785 scopus 로고    scopus 로고
    • High density O-glycosylation of the MUC2 tandem repeat unit by N-acetylgalactosaminyltransferase-3 in colonic adenocarcinoma extracts
    • Inoue, M., Takahashi, S., Yamashina, I., Kaibori, M., Okumura, T., Kamiyama, Y., Vichier-Guerre, S., Cantacuzène, D., and Nakada, H. (2001) High density O-glycosylation of the MUC2 tandem repeat unit by N-acetylgalactosaminyltransferase-3 in colonic adenocarcinoma extracts. Cancer Res. 61, 950-956 (Pubitemid 32174410)
    • (2001) Cancer Research , vol.61 , Issue.3 , pp. 950-956
    • Inoue, M.1    Takahashi, S.2    Yamashina, I.3    Kaibori, M.4    Okumura, T.5    Kamiyama, Y.6    Viehier-Guerre, S.7    Cantacuzene, D.8    Nakada, H.9
  • 35
    • 0030466993 scopus 로고    scopus 로고
    • Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines: Demonstration of simpler and fewer glycan chains in tumor cells
    • DOI 10.1074/jbc.271.52.33325
    • Lloyd, K. O., Burchell, J., Kudryashov, V., Yin, B. W., and Taylor-Papadimitriou, J. (1996) Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines. Demonstration of simpler and fewer glycan chains in tumor cells. J. Biol. Chem. 271, 33325-33334 (Pubitemid 27010142)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.52 , pp. 33325-33334
    • Lloyd, K.O.1    Burchell, J.2    Kudryashov, V.3    Yin, B.W.T.4    Taylor-Papadimitriou, J.5
  • 37
    • 0344719239 scopus 로고    scopus 로고
    • Alteration of N-acetylglucosaminyltransferases in pancreatic carcinoma
    • DOI 10.1023/A:1006950311937
    • Nan, B. C., Shao, D. M., Chen, H. L., Huang, Y., Gu, J. X., Zhang, Y. B., and Wu, Z. G. (1998) Alteration of N-acetylglucosaminyltransferases in pancreatic carcinoma. Glycoconj. J. 15, 1033-1037 (Pubitemid 29129202)
    • (1998) Glycoconjugate Journal , vol.15 , Issue.10 , pp. 1033-1037
    • Nan, B.-C.1    Shao, D.-M.2    Chen, H.-L.3    Huang, Y.4    Gu, J.-X.5    Zhang, Y.-B.6    Wu, Z.-G.7
  • 38
    • 79551481037 scopus 로고    scopus 로고
    • Levels of specific serum N-glycans identify breast cancer patients with higher circulating tumor cell counts
    • Saldova, R., Reuben, J. M., Abd Hamid, U. M., Rudd, P. M., and Cristofanilli, M. (2011) Levels of specific serum N-glycans identify breast cancer patients with higher circulating tumor cell counts. Ann. Oncol. 22, 1113-1119
    • (2011) Ann. Oncol. , vol.22 , pp. 1113-1119
    • Saldova, R.1    Reuben, J.M.2    Abd Hamid, U.M.3    Rudd, P.M.4    Cristofanilli, M.5
  • 40
    • 50449090546 scopus 로고    scopus 로고
    • Glycoproteomics and glycomics investigation of membrane N-glycosylproteins from human colon carcinoma cells
    • Vercoutter-Edouart, A. S., Slomianny, M. C., Dekeyzer-Beseme, O., Haeuw, J. F., and Michalski, J. C. (2008) Glycoproteomics and glycomics investigation of membrane N-glycosylproteins from human colon carcinoma cells. Proteomics 8, 3236-3256
    • (2008) Proteomics , vol.8 , pp. 3236-3256
    • Vercoutter-Edouart, A.S.1    Slomianny, M.C.2    Dekeyzer-Beseme, O.3    Haeuw, J.F.4    Michalski, J.C.5
  • 41
    • 0038618896 scopus 로고    scopus 로고
    • Altered glycosylation pattern allows the distinction between prostate-specific antigen (PSA) from normal and tumor origins
    • DOI 10.1093/glycob/cwg041
    • Peracaula, R., Tabarés, G., Royle, L., Harvey, D. J., Dwek, R. A., Rudd, P. M., and de Llorens, R. (2003) Altered glycosylation pattern allows the distinction between prostate-specific antigen (PSA) from normal and tumor origins. Glycobiology 13, 457-470 (Pubitemid 36665420)
    • (2003) Glycobiology , vol.13 , Issue.6 , pp. 457-470
    • Peracaula, R.1    Tabares, G.2    Royle, L.3    Harvey, D.J.4    Dwek, R.A.5    Rudd, P.M.6    De Llorens, R.7
  • 44
    • 33744799438 scopus 로고    scopus 로고
    • Mucin-type O-glycans in human colon and breast cancer. Glycodynamics and functions
    • Brockhausen, I. (2006) Mucin-type O-glycans in human colon and breast cancer. Glycodynamics and functions. EMBO Rep. 7, 599-604
    • (2006) EMBO Rep. , vol.7 , pp. 599-604
    • Brockhausen, I.1
  • 45
    • 0036678137 scopus 로고    scopus 로고
    • Up-regulation of plasma membrane-associated ganglioside sialidase (Neu3) in human colon cancer and its involvement in apoptosis suppression
    • Kakugawa, Y., Wada, T., Yamaguchi, K., Yamanami, H., Ouchi, K., Sato, I., and Miyagi, T. (2002) Up-regulation of plasma membrane-associated ganglioside sialidase (Neu3) in human colon cancer and its involvement in apoptosis suppression. Proc. Natl. Acad. Sci. U.S.A. 99, 10718-10723
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 10718-10723
    • Kakugawa, Y.1    Wada, T.2    Yamaguchi, K.3    Yamanami, H.4    Ouchi, K.5    Sato, I.6    Miyagi, T.7
  • 46
    • 44449107032 scopus 로고    scopus 로고
    • The O-linked glycosylation of secretory/shed MUC1 from an advanced breast cancer patient's serum
    • DOI 10.1093/glycob/cwn022
    • Storr, S. J., Royle, L., Chapman, C. J., Hamid, U. M., Robertson, J. F., Murray, A., Dwek, R. A., and Rudd, P. M. (2008) The O-Linked glycosylation of secretory/shed MUC1 from an advanced breast cancer patient's serum. Glycobiology 18, 456-462 (Pubitemid 351753549)
    • (2008) Glycobiology , vol.18 , Issue.6 , pp. 456-462
    • Storr, S.J.1    Royle, L.2    Chapman, C.J.3    Hamid, U.M.Abd.4    Robertson, J.F.5    Murray, A.6    Dwek, R.A.7    Rudd, P.M.8
  • 47
    • 73549115380 scopus 로고    scopus 로고
    • GalNAcα1-3Gal, a new prognostic marker for cervical cancer
    • Li, Q., Anver, M. R., Li, Z., Butcher, D. O., and Gildersleeve, J. C. (2010) GalNAcα1-3Gal, a new prognostic marker for cervical cancer. Int. J. Cancer 126, 459-468
    • (2010) Int. J. Cancer , vol.126 , pp. 459-468
    • Li, Q.1    Anver, M.R.2    Li, Z.3    Butcher, D.O.4    Gildersleeve, J.C.5
  • 48
    • 0021572879 scopus 로고
    • Tumor-associated carbohydrate antigens
    • Hakomori, S. (1984) Tumor-associated carbohydrate antigens. Annu. Rev. Immunol. 2, 103-126
    • (1984) Annu. Rev. Immunol. , vol.2 , pp. 103-126
    • Hakomori, S.1
  • 49
    • 26444452697 scopus 로고    scopus 로고
    • Thomsen-Friedenreich and Tn antigens in nipple fluid: Carbohydrate biomarkers for breast cancer detection
    • DOI 10.1158/1078-0432.CCR-05-0146
    • Kumar, S. R., Sauter, E. R., Quinn, T. P., and Deutscher, S. L. (2005) Thom-sen-Friedenreich and Tn antigens in nipple fluid. Carbohydrate biomarkers for breast cancer detection. Clin. Cancer Res. 11, 6868-6871 (Pubitemid 41428742)
    • (2005) Clinical Cancer Research , vol.11 , Issue.19 I , pp. 6868-6871
    • Kumar, S.R.1    Sauter, E.R.2    Quinn, T.P.3    Deutscher, S.L.4
  • 51
    • 0024003044 scopus 로고
    • Binding and precipitation of lectins from Erythrina indica and Ricinus communis (agglutinin I) with synthetic cluster glycosides
    • Bhattacharyya, L., and Brewer, C. F. (1988) Binding and precipitation of lectins from Erythrina indica and Ricinus communis (agglutinin I) with synthetic cluster glycosides. Arch. Biochem. Biophys. 262, 605-608
    • (1988) Arch. Biochem. Biophys. , vol.262 , pp. 605-608
    • Bhattacharyya, L.1    Brewer, C.F.2
  • 52
    • 0024260839 scopus 로고
    • 1H NMR spectroscopy
    • Green, E. D., Adelt, G., Baenziger, J. U., Wilson, S., and Van Halbeek, H. (1988) The asparagine-linked oligosaccharides on bovine fetuin. Structural analysis of N-glycanase-released oligosaccharides by 500-megahertz1H NMR spectroscopy. J. Biol. Chem. 263, 18253-18268 (Pubitemid 19005103)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.34 , pp. 18253-18268
    • Green, E.D.1    Adelt, G.2    Baenziger, J.U.3    Wilson, S.4    Van Halbeek, H.5
  • 53
    • 0020523938 scopus 로고
    • Isolation and structures of the oligosaccharide units of carcinoembryonic antigen
    • Chandrasekaran, E. V., Davila, M., Nixon, D. W., Goldfarb, M., and Mendicino, J. (1983) Isolation and structures of the oligosaccharide units of carcinoembryonic antigen. J. Biol. Chem. 258, 7213-7222 (Pubitemid 13059974)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.11 , pp. 7213-7222
    • Chandrasekaran, E.V.1    Davila, M.2    Nixon, D.W.3
  • 54
    • 0023050165 scopus 로고
    • Carbohydrate structures of bovine submaxillary mucin
    • Tsuji, T., and Osawa, T. (1986) Carbohydrate structures of bovine submaxillary mucin. Carbohydr. Res. 151, 391-402
    • (1986) Carbohydr. Res. , vol.151 , pp. 391-402
    • Tsuji, T.1    Osawa, T.2
  • 55
    • 77955627344 scopus 로고    scopus 로고
    • Effects of hapten density on the induced antibody repertoire
    • Li, Q., Rodriguez, L. G., Farnsworth, D. F., and Gildersleeve, J. C. (2010) Effects of hapten density on the induced antibody repertoire. Chembiochem 11, 1686-1691
    • (2010) Chembiochem , vol.11 , pp. 1686-1691
    • Li, Q.1    Rodriguez, L.G.2    Farnsworth, D.F.3    Gildersleeve, J.C.4
  • 56
    • 0018786793 scopus 로고
    • Structural studies on the carbohydrate portion of fetuin
    • Nilsson, B., Nordén, N. E., and Svensson, S. (1979) Structural studies on the carbohydrate portion of fetuin. J. Biol. Chem. 254, 4545-4553
    • (1979) J. Biol. Chem. , vol.254 , pp. 4545-4553
    • Nilsson, B.1    Nordén, N.E.2    Svensson, S.3
  • 57
    • 66149148696 scopus 로고    scopus 로고
    • Thermodynamics of multivalent carbohydrate-lectin cross-linking interactions. Importance of entropy in the bind and jump mechanism
    • Dam, T. K., Gerken, T. A., and Brewer, C. F. (2009) Thermodynamics of multivalent carbohydrate-lectin cross-linking interactions. Importance of entropy in the bind and jump mechanism. Biochemistry 48, 3822-3827
    • (2009) Biochemistry , vol.48 , pp. 3822-3827
    • Dam, T.K.1    Gerken, T.A.2    Brewer, C.F.3
  • 58
    • 48149095486 scopus 로고    scopus 로고
    • The insulin receptor. A prototype for dimeric, allosteric membrane receptors?
    • De Meyts P. (2008) The insulin receptor. A prototype for dimeric, allosteric membrane receptors? Trends Biochem. Sci. 33, 376-384
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 376-384
    • De Meyts, P.1
  • 59
    • 84859786953 scopus 로고    scopus 로고
    • Caveolins and caveolae, roles in insulin signaling and diabetes
    • Strålfors, P. (2012) Caveolins and caveolae, roles in insulin signaling and diabetes. Adv. Exp. Med. Biol. 729, 111-126
    • (2012) Adv. Exp. Med. Biol. , vol.729 , pp. 111-126
    • Strålfors, P.1
  • 60
    • 77949808518 scopus 로고    scopus 로고
    • N-Glycomic changes in human breast carcinoma MCF-7 and T-lymphoblastoid cells after treatment with herceptin and herceptin/Lipoplex
    • Lattová, E., Tomanek, B., Bartusik, D., and Perreault, H. (2010) N-Glycomic changes in human breast carcinoma MCF-7 and T-lymphoblastoid cells after treatment with herceptin and herceptin/Lipoplex. J. Proteome. Res. 9, 1533-1540
    • (2010) J. Proteome. Res. , vol.9 , pp. 1533-1540
    • Lattová, E.1    Tomanek, B.2    Bartusik, D.3    Perreault, H.4
  • 61
    • 84984066625 scopus 로고
    • An equation to describe dose-responses where there is stimulation of growth at low doses
    • Brain, P., and Cousens, R. (1989) An equation to describe dose-responses where there is stimulation of growth at low doses. Weed Res. 29, 93-96
    • (1989) Weed Res. , vol.29 , pp. 93-96
    • Brain, P.1    Cousens, R.2


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