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Volumn 1840, Issue 3, 2014, Pages 1105-1116

A straightforward protocol for the preparation of high performance microarray displaying synthetic MUC1 glycopeptides

Author keywords

Autoantibody; Epitope mapping; Microarray; MUC1 glycopeptide; Non specific protein adsorption

Indexed keywords

EPITOPE; GLYCOPEPTIDE; IMINE; IMMUNOGLOBULIN G ANTIBODY; KETONE; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY DF3; MONOCLONAL ANTIBODY KL 6; MONOCLONAL ANTIBODY MA552; MONOCLONAL ANTIBODY MUC1; MONOCLONAL ANTIBODY SM3; MONOCLONAL ANTIBODY VU 11E2; MONOCLONAL ANTIBODY VU 12E1; MONOCLONAL ANTIBODY VU 3C6; MONOCLONAL ANTIBODY VU 3D1; MUCIN 1; PEPTIDE FRAGMENT; PHOSPHORYLCHOLINE; POLYMETHACRYLIC ACID; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG;

EID: 84890834542     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2013.11.009     Document Type: Article
Times cited : (31)

References (102)
  • 1
    • 43549126011 scopus 로고    scopus 로고
    • Structure and function of the cell surface (tethered) mucins
    • DOI 10.1146/annurev.physiol.70.113006.100659
    • C.L. Hattrup, and S.J. Gendler Structure and function of the cell surface (tethered) mucins Annu. Rev. Physiol. 70 2008 431 457 (Pubitemid 351738187)
    • (2008) Annual Review of Physiology , vol.70 , pp. 431-457
    • Hattrup, C.L.1    Gendler, S.J.2
  • 2
    • 77952668655 scopus 로고    scopus 로고
    • Membrane-bound mucins: The mechanistic basis for alterations in the growth and survival of cancer cells
    • S. Bafna, S. Kaur, and S.K. Batra Membrane-bound mucins: the mechanistic basis for alterations in the growth and survival of cancer cells Oncogene 29 2010 2893 2904
    • (2010) Oncogene , vol.29 , pp. 2893-2904
    • Bafna, S.1    Kaur, S.2    Batra, S.K.3
  • 4
    • 40749160803 scopus 로고    scopus 로고
    • Mucin-type O-glycosylation and its potential use in drug and vaccine development
    • DOI 10.1016/j.bbagen.2007.09.010, PII S0304416507002164
    • M.A. Tarp, and H. Clausen Mucin-type O-glycosylation and its potential use in drug and vaccine development Biochim. Biophys. Acta 1780 2008 546 563 (Pubitemid 351381249)
    • (2008) Biochimica et Biophysica Acta - General Subjects , vol.1780 , Issue.3 , pp. 546-563
    • Tarp, M.A.1    Clausen, H.2
  • 5
    • 0347123435 scopus 로고    scopus 로고
    • Mucins in cancer: Protection and control of the cell surface
    • M.A. Hollingsworth, and B.J. Swanson Mucins in cancer: protection and control of the cell surface Nat. Rev. Cancer 4 2004 45 60 (Pubitemid 38082153)
    • (2004) Nature Reviews Cancer , vol.4 , Issue.1 , pp. 45-60
    • Hollingsworth, M.A.1    Swanson, B.J.2
  • 6
    • 77956044379 scopus 로고    scopus 로고
    • PH1-derived bivalent bibodies and trivalent tribodies bind differentially to shed and tumour cell-associated MUC1
    • S. Schoonooghe, I. Burvenich, L. Vervoort, F. De Vos, N. Mertens, and J. Grooten PH1-derived bivalent bibodies and trivalent tribodies bind differentially to shed and tumour cell-associated MUC1 Protein Eng. Des. Sel. 23 2010 721 728
    • (2010) Protein Eng. Des. Sel. , vol.23 , pp. 721-728
    • Schoonooghe, S.1    Burvenich, I.2    Vervoort, L.3    De Vos, F.4    Mertens, N.5    Grooten, J.6
  • 7
    • 0019426220 scopus 로고
    • Monoclonal antibodies to epithelium-specific components of the human milk fat globule membrane: Production and reaction with cells in culture
    • DOI 10.1002/ijc.2910280104
    • J. Taylor-Papadimitriou, J.A. Peterson, J. Arklie, J. Burchell, R.L. Ceriani, and W.F. Bodmer Monoclonal antibodies to epithelium-specific components of the human milk fat globule membrane: production and reaction with cells in culture Int. J. Cancer 28 1981 17 21 (Pubitemid 11070004)
    • (1981) International Journal of Cancer , vol.28 , Issue.1 , pp. 17-21
    • Taylor-Papadimitriou, J.1    Peterson, J.A.2    Arklie, J.3
  • 8
    • 77449106552 scopus 로고    scopus 로고
    • Phase i dose escalation pharmacokinetic assessment of intravenous humanized anti-MUC1 antibody AS1402 in patients with advanced breast cancer
    • M.D. Pegram, V.F. Borges, N. Ibrahim, J. Fulona, C. Perez Shapiro, K. Wang, F.S. Stark, and N.C. Luck Phase I dose escalation pharmacokinetic assessment of intravenous humanized anti-MUC1 antibody AS1402 in patients with advanced breast cancer Breast Cancer Res. 11 2009 R73
    • (2009) Breast Cancer Res. , vol.11 , pp. 73
    • Pegram, M.D.1    Borges, V.F.2    Ibrahim, N.3    Fulona, J.4    Shapiro, C.P.5    Wang, K.6    Stark, F.S.7    Luck, N.C.8
  • 9
    • 77649272126 scopus 로고    scopus 로고
    • Population pharmacokinetics of the humanised monoclonal antibody, HuHMFG1 (AS1402), derived from a phase i study on breast cancer
    • B. Royer, W. Yin, M. Pegram, N. Ibrahim, C. Villanueva, D. Mir, F. Erlandsson, and X. Pivot Population pharmacokinetics of the humanised monoclonal antibody, HuHMFG1 (AS1402), derived from a phase I study on breast cancer Br. J. Cancer 102 2010 827 832
    • (2010) Br. J. Cancer , vol.102 , pp. 827-832
    • Royer, B.1    Yin, W.2    Pegram, M.3    Ibrahim, N.4    Villanueva, C.5    Mir, D.6    Erlandsson, F.7    Pivot, X.8
  • 12
    • 77954349368 scopus 로고    scopus 로고
    • Reactivity of a humanized antibody (hPankoMab) towards a tumor-related MUC1 epitope (TA-MUC1) with various human carcinomas
    • X.N. Fan, U. Karsten, S. Goletz, and Y. Cao Reactivity of a humanized antibody (hPankoMab) towards a tumor-related MUC1 epitope (TA-MUC1) with various human carcinomas Pathol. Res. Pract. 206 2010 585 589
    • (2010) Pathol. Res. Pract. , vol.206 , pp. 585-589
    • Fan, X.N.1    Karsten, U.2    Goletz, S.3    Cao, Y.4
  • 15
    • 0035046084 scopus 로고    scopus 로고
    • Binding patterns of 51 monoclonal antibodies to peptide and carbohydrate epitopes of the epithelial mucin (MUC1) on tissue sections of adenolymphomas of the parotid (Warthin's tumours): Role of epitope masking by glycans
    • Y. Cao, and U. Karsten Binding patterns of 51 monoclonal antibodies to peptide and carbohydrate epitopes of the epithelial mucin (MUC1) on tissue sections of adenolymphomas of the parotid (Warthin's tumours): role of epitope masking by glycans Histochem. Cell Biol. 115 2001 349 356 (Pubitemid 32323892)
    • (2001) Histochemistry and Cell Biology , vol.115 , Issue.4 , pp. 349-356
    • Cao, Y.1    Karsten, U.2
  • 16
    • 0032526177 scopus 로고    scopus 로고
    • Enhanced binding of antibodies to the DTR motif of MUC1 tandem repeat peptide is mediated by site-specific glycosylation
    • U. Karsten, C. Diotel, G. Klich, H. Paulsen, S. Goletz, S. Müller, and F. Hanisch Enhanced binding of antibodies to the DTR motif of MUC1 tandem repeat peptide is mediated by site-specific glycosylation Cancer Res. 58 1998 2541
    • (1998) Cancer Res. , vol.58 , pp. 2541
    • Karsten, U.1    Diotel, C.2    Klich, G.3    Paulsen, H.4    Goletz, S.5    Müller, S.6    Hanisch, F.7
  • 17
    • 4444313524 scopus 로고    scopus 로고
    • Binding patterns of DTR-specific antibodies reveal a glycosylation- conditioned tumor-specific epitope of the epithelial mucin (MUC1)
    • U. Karsten, N. Serttas, H. Paulsen, A. Danielczyk, and S. Goletz Binding patterns of DTR-specific antibodies reveal a glycosylation-conditioned tumor-specific epitope of the epithelial mucin (MUC1) Glycobiology 14 2004 681
    • (2004) Glycobiology , vol.14 , pp. 681
    • Karsten, U.1    Serttas, N.2    Paulsen, H.3    Danielczyk, A.4    Goletz, S.5
  • 18
    • 24644440098 scopus 로고    scopus 로고
    • What makes MUC1 a tumor antigen?
    • DOI 10.1159/000086956
    • U. Karsten, S. von Mensdorff-Pouilly, and S. Goletz What makes MUC1 a tumor antigen Tumor Biol. 26 2005 217 220 (Pubitemid 41379749)
    • (2005) Tumor Biology , vol.26 , Issue.4 , pp. 217-220
    • Karsten, U.1    Von Mensdorff-Pouilly, S.2    Goletz, S.3
  • 22
    • 0033032313 scopus 로고    scopus 로고
    • Specificity analysis of sera from breast cancer patients vaccinated with MUC1-KLH plus QS-21
    • S. Adluri, T. Gilewski, S. Zhang, V. Ramnath, G. Ragupathi, and P. Livingston Specificity analysis of sera from breast cancer patients vaccinated with MUC1-KLH plus QS-21 Br. J. Cancer 79 1999 1806
    • (1999) Br. J. Cancer , vol.79 , pp. 1806
    • Adluri, S.1    Gilewski, T.2    Zhang, S.3    Ramnath, V.4    Ragupathi, G.5    Livingston, P.6
  • 24
    • 0035339389 scopus 로고    scopus 로고
    • Three different vaccines based on the 140-amino acid MUC1 peptide with seven tandemly repeated tumor-specific epitopes elicit distinct immune effector mechanisms in wild-type versus MUC1-transgenic mice with different potential for tumor rejection
    • M. Soares, V. Mehta, and O. Finn Three different vaccines based on the 140-amino acid MUC1 peptide with seven tandemly repeated tumor-specific epitopes elicit distinct immune effector mechanisms in wild-type versus MUC1-transgenic mice with different potential for tumor rejection J. Immunol. 166 2001 6555 6563 (Pubitemid 32467194)
    • (2001) Journal of Immunology , vol.166 , Issue.11 , pp. 6555-6563
    • Soares, M.M.1    Mehta, V.2    Finn, O.J.3
  • 26
    • 0032892187 scopus 로고    scopus 로고
    • Vaccines prepared with sialyl-Tn and sialyl-Tn trimers using the 4-(4- maleimidomethyl)cyclohexane-1-carboxyl hydrazide linker group result in optimal antibody titers against ovine submaxillary mucin and sialyl-Tn- positive tumor cells
    • DOI 10.1007/s002620050542
    • G. Ragupathi, L. Howard, S. Cappello, R.R. Koganty, D. Qiu, B.M. Longenecker, M.A. Reddish, K.O. Lloyd, and P.O. Livingston Vaccines prepared with sialyl-Tn and sialyl-Tn trimers using the 4-(4-maleimidomethyl)cyclohexane- 1-carboxyl hydrazide linker group result in optimal antibody titers against ovine submaxillary mucin and sialyl-Tn-positive tumor cells Cancer Immunol. Immunother. 48 1999 1 8 (Pubitemid 29197237)
    • (1999) Cancer Immunology Immunotherapy , vol.48 , Issue.1 , pp. 1-8
    • Ragupathi, G.1    Howard, L.2    Cappello, S.3    Koganty, R.R.4    Qiu, D.5    Longenecker, B.M.6    Reddish, M.A.7    Lloyd, K.O.8    Livingston, P.O.9
  • 35
    • 70449720923 scopus 로고    scopus 로고
    • Serum autoantibodies as biomarkers for early cancer detection
    • H.T. Tan, J. Low, S.G. Lim, and M.C.M. Chung Serum autoantibodies as biomarkers for early cancer detection FEBS J. 276 2009 6880 6904
    • (2009) FEBS J. , vol.276 , pp. 6880-6904
    • Tan, H.T.1    Low, J.2    Lim, S.G.3    Chung, M.C.M.4
  • 36
    • 0022570617 scopus 로고
    • MAM-6 antigen, a new serum marker for breast cancer monitoring
    • J. Hilkens, V. Kroezen, J.M. Bonfrer, M. De Jong-Bakker, and P.F. Bruning Clinical and epidemiological investigations - Articles: MAM-6 antigen, a new serum marker for breast cancer monitoring Cancer Res. 46 1986 2582 2587 (Pubitemid 16120735)
    • (1986) Cancer Research , vol.46 , Issue.5 , pp. 2582-2587
    • Hilkens, J.1    Kroezen, V.2    Bonfrer, J.M.G.3
  • 37
    • 0030937160 scopus 로고    scopus 로고
    • The effect of circulating antigen on the biodistribution of the engineered human antibody hCTM01 in a nude mice model
    • DOI 10.1007/BF02439555
    • Q. Davies, A.C. Perkins, M. Frier, S. Watson, E.N. Lalani, and E.M. Symonds The effect of circulating antigen on the biodistribution of the engineered human antibody hCTM01 in a nude mice model Eur. J. Nucl. Med. 24 1997 206 209 (Pubitemid 27121102)
    • (1997) European Journal of Nuclear Medicine , vol.24 , Issue.2 , pp. 206-209
    • Davies, Q.1    Perkins, A.C.2    Frier, M.3    Watson, S.4    Lalani, E.-N.5    Symonds, E.M.6
  • 38
    • 0028452913 scopus 로고
    • Exploiting altered glycosylation patterns in cancer: Progress and challenges in diagnosis and therapy
    • DOI 10.1016/0167-7799(94)90121-X
    • J. Taylor-Papadimitriou, and A.A. Epenetos Exploiting altered glycosylation patterns in cancer: progress and challenges in diagnosis and therapy Trends Biotechnol. 12 1994 227 233 (Pubitemid 24190550)
    • (1994) Trends in Biotechnology , vol.12 , Issue.6 , pp. 227-233
    • Taylor-Papadimitriou, J.1    Epenetos, A.A.2
  • 41
    • 0024523057 scopus 로고
    • Circulating CA 15-3 antigen levels in non-mammary malignancies
    • R. Colomer, A. Ruibal, Salvador Genolla, and L. Circulating CA 15-3 antigen levels in non-mammary malignancies Br. J. Cancer 59 1989 283 286 (Pubitemid 19072734)
    • (1989) British Journal of Cancer , vol.59 , Issue.2 , pp. 283-286
    • Colomer, R.1    Ruibal, A.2    Genolla, J.3    Salvador, L.4
  • 44
    • 0021740104 scopus 로고
    • Differential reactivity of a novel monoclonal antibody (DF3) with human malignant versus benign breast tumors
    • D. Kufe, G. Inghirami, M. Abe, D. Hayes, H. Justi-Wheeler, and J. Schlom Differential reactivity of a novel monoclonal antibody (DF3) with human malignant versus benign breast tumors Hybridoma 3 1984 223 232 (Pubitemid 15184701)
    • (1984) Hybridoma , vol.3 , Issue.3 , pp. 223-232
    • Kufe, D.1    Inghirami, G.2    Abe, M.3
  • 45
    • 0021132973 scopus 로고
    • Monoclonal antibodies against human milk-fat globule membranes detecting differentiation antigens of the mammary gland and its tumors
    • J. Hilkens, F. Buijs, J. Hilgers, P. Hageman, J. Calafat, A. Sonnenberg, and M. van der Valk Monoclonal antibodies against human milk-fat globule membranes detecting differentiation antigens of the mammary gland and its tumors Int. J. Cancer 34 1984 197 206 (Pubitemid 14053141)
    • (1984) International Journal of Cancer , vol.34 , Issue.2 , pp. 197-206
    • Hilkens, J.1    Buijs, F.2    Hilgers, J.3
  • 46
    • 0026659195 scopus 로고
    • Tumor selective reactivity of a monoclonal antibody prepared against a recombinant peptide derived from the DF3 human breast carcinoma-associated antigen
    • L. Perey, D.F. Hayes, P. Maimonis, M. Abe, C. O'Hara, and D.W. Kufe Tumor selective reactivity of a monoclonal antibody prepared against a recombinant peptide derived from the DF3 human breast carcinoma-associated antigen Cancer Res. 52 1992 2563 2568
    • (1992) Cancer Res. , vol.52 , pp. 2563-2568
    • Perey, L.1    Hayes, D.F.2    Maimonis, P.3    Abe, M.4    O'Hara, C.5    Kufe, D.W.6
  • 47
    • 0024077916 scopus 로고
    • Detection of soluble tumor-associated antigens in sera and effusions using novel monoclonal antibodies, KL-3 and KL-6, against lung adenocarcinoma
    • N. Kohno, M. Akiyama, S. Kyoizumi, M. Hakoda, K. Kobuke, and M. Yamakido Detection of soluble tumor-associated antigens in sera and effusions using novel monoclonal antibodies, KL-3 and KL-6, against lung adenocarcinoma Jpn. J. Clin. Oncol. 18 1988 203 216
    • (1988) Jpn. J. Clin. Oncol. , vol.18 , pp. 203-216
    • Kohno, N.1    Akiyama, M.2    Kyoizumi, S.3    Hakoda, M.4    Kobuke, K.5    Yamakido, M.6
  • 48
    • 0033071977 scopus 로고    scopus 로고
    • Lung epithelium-specific proteins - Characteristics and potential applications as markers
    • C. Hermans, and A. Bernard Lung epithelium-specific proteins - characteristics and potential applications as markers Am. J. Respir. Crit. Care Med. 159 1999 646 678
    • (1999) Am. J. Respir. Crit. Care Med. , vol.159 , pp. 646-678
    • Hermans, C.1    Bernard, A.2
  • 52
    • 42549154345 scopus 로고    scopus 로고
    • Usefulness of monitoring the circulating Krebs von den Lungen-6 levels to predict the clinical outcome of patients with advanced nonsmall cell lung cancer treated with epidermal growth factor receptor tyrosine kinase inhibitors
    • DOI 10.1002/ijc.23411
    • N. Ishikawa, N. Hattori, A. Yokoyama, S. Tanaka, R. Nishino, K. Yoshikawa, S. Ohshimo, K. Fujitaka, H. Ohnishi, H. Hamada, K. Arihiro, and N. Kohno Usefulness of monitoring the circulating Krebs von den Lungen-6 levels to predict the clinical outcome of patients with advanced nonsmall cell lung cancer treated with epidermal growth factor receptor tyrosine kinase inhibitors Int. J. Cancer 122 2008 2612 2620 (Pubitemid 351590499)
    • (2008) International Journal of Cancer , vol.122 , Issue.11 , pp. 2612-2620
    • Ishikawa, N.1    Hattori, N.2    Yokoyama, A.3    Tanaka, S.4    Nishino, R.5    Yoshioka, K.6    Ohshimo, S.7    Fujitaka, K.8    Ohnishi, H.9    Hamada, H.10    Arihiro, K.11    Kohno, N.12
  • 54
    • 58149350380 scopus 로고    scopus 로고
    • Positive KL-6 mucin expression combined with decreased membranous B-catenin expression indicates worse prognosis in colorectal carcinoma
    • W. Zhang, W. Tang, Y. Inagaki, M. Qiu, H. Lixu, X. Li, Y. Sugawara, H. Sagawa, M. Nakata, and N. Kokudo Positive KL-6 mucin expression combined with decreased membranous B-catenin expression indicates worse prognosis in colorectal carcinoma Oncol. Rep. 20 2008 1013 1019
    • (2008) Oncol. Rep. , vol.20 , pp. 1013-1019
    • Zhang, W.1    Tang, W.2    Inagaki, Y.3    Qiu, M.4    Lixu, H.5    Li, X.6    Sugawara, Y.7    Sagawa, H.8    Nakata, M.9    Kokudo, N.10
  • 55
    • 79959464070 scopus 로고    scopus 로고
    • Glycan microarrays for decoding the glycome
    • C.D. Rillahan, and J.C. Paulson Glycan microarrays for decoding the glycome Annu. Rev. Biochem. 80 2011 797 823
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 797-823
    • Rillahan, C.D.1    Paulson, J.C.2
  • 58
    • 67650351512 scopus 로고    scopus 로고
    • Microarrays with varying carbohydrate density reveal distinct subpopulations of serum antibodies
    • O. Oyelaran, L.M. MeShane, D. Farnsworth, and J.C. Gildersleeve Microarrays with varying carbohydrate density reveal distinct subpopulations of serum antibodies J. Proteome Res. 8 2009 3529 3538
    • (2009) J. Proteome Res. , vol.8 , pp. 3529-3538
    • Oyelaran, O.1    Meshane, L.M.2    Farnsworth, D.3    Gildersleeve, J.C.4
  • 59
    • 70349286700 scopus 로고    scopus 로고
    • Profiling human serum antibodies with a carbohydrate antigen microarray
    • O. Oyelaran, L.M. MeShane, L. Dodd, and J.C. Gildersleeve Profiling human serum antibodies with a carbohydrate antigen microarray J. Proteome Res. 8 2009 4301 4310
    • (2009) J. Proteome Res. , vol.8 , pp. 4301-4310
    • Oyelaran, O.1    Meshane, L.M.2    Dodd, L.3    Gildersleeve, J.C.4
  • 63
    • 33645781487 scopus 로고    scopus 로고
    • Construction of highly glycosylated mucin-type glycopeptides based on microwave-assisted solid-phase syntheses and enzymatic modifications
    • T. Matsushita, H. Hinou, M. Fumoto, M. Kurogochi, N. Fujitani, H. Shimizu, and S.-I. Nishimura Construction of highly glycosylated mucin-type glycopeptides based on microwave-assisted solid-phase syntheses and enzymatic modifications J. Org. Chem. 71 2006 3051 3063
    • (2006) J. Org. Chem. , vol.71 , pp. 3051-3063
    • Matsushita, T.1    Hinou, H.2    Fumoto, M.3    Kurogochi, M.4    Fujitani, N.5    Shimizu, H.6    Nishimura, S.-I.7
  • 64
    • 33845956872 scopus 로고    scopus 로고
    • Construction and structural characterization of versatile lactosaminoglycan-related compound library for the synthesis of complex glycopeptides and glycosphingolipids
    • DOI 10.1021/jo0617161
    • K. Naruchi, T. Hamamoto, M. Kurogochi, H. Hinou, H. Shimizu, T. Matsushita, N. Fujitani, H. Kondo, and S.-I. Nishimura Construction and structural characterization of versatile lactosaminoglycan-related compound library for the synthesis of complex glycopeptides and glycosphingolipids J. Org. Chem. 71 2006 9609 9621 (Pubitemid 46032625)
    • (2006) Journal of Organic Chemistry , vol.71 , Issue.26 , pp. 9609-9621
    • Naruchi, K.1    Hamamoto, T.2    Kurogochi, M.3    Hinou, H.4    Shimizu, H.5    Matsushita, T.6    Fujitani, N.7    Kondo, H.8    Nishimura, S.-I.9
  • 70
    • 0037135998 scopus 로고    scopus 로고
    • Developing site-specific immobilization strategies of peptides in a microarray
    • DOI 10.1016/S0960-894X(02)00379-7, PII S0960894X02003797
    • M.-L. Lesaicherre, M. Uttamchandani, G.Y.J. Chen, and S.Q. Yao Developing site-specific immobilization strategies of peptides in a microarray Bioorg. Med. Chem. Lett. 12 2002 2079 2083 (Pubitemid 34804370)
    • (2002) Bioorganic and Medicinal Chemistry Letters , vol.12 , Issue.16 , pp. 2079-2083
    • Lesaicherre, M.-L.1    Uttamchandani, M.2    Chen, G.Y.J.3    Yao, S.Q.4
  • 73
    • 1442324446 scopus 로고    scopus 로고
    • Characterization of A Polymeric Adsorbed Coating for DNA Microarray Glass Slides
    • DOI 10.1021/ac0352629
    • G. Pirri, F. Damin, M. Chiari, E. Bontempi, and L.E. Depero Characterization of a polymeric adsorbed coating for DNA microarray glass slides Anal. Chem. 76 2004 1352 1358 (Pubitemid 38280483)
    • (2004) Analytical Chemistry , vol.76 , Issue.5 , pp. 1352-1358
    • Pirri, G.1    Damin, F.2    Chiari, M.3    Bontempi, E.4    Depero, L.E.5
  • 74
    • 18044391505 scopus 로고    scopus 로고
    • Molecular transporter between polymer platforms: Highly efficient chemoenzymatic glycopeptide synthesis by the combined use of solid-phase and water-soluble polymer supports
    • DOI 10.1002/anie.200463065
    • M. Fumoto, H. Hinou, T. Matsushita, M. Kurogochi, T. Ohta, T. Ito, K. Yamada, A. Takimoto, H. Kondo, T. Inazu, and S.-I. Nishimura Molecular transporter between polymer platforms: highly efficient chemoenzymatic glycopeptide synthesis by the combined use of solid-phase and water-soluble polymer supports Angew. Chem. Int. Ed. Engl. 44 2005 2534 2537 (Pubitemid 40600323)
    • (2005) Angewandte Chemie - International Edition , vol.44 , Issue.17 , pp. 2534-2537
    • Fumoto, M.1    Hinou, H.2    Matsushita, T.3    Kurogochi, M.4    Ohta, T.5    Ito, T.6    Yamada, K.7    Takimoto, A.8    Kondo, H.9    Inazu, T.10    Nishimura, S.-I.11
  • 76
    • 59249099294 scopus 로고    scopus 로고
    • Structural and functional glycosphingolipidomics by glycoblotting with an aminooxy-functionalized gold nanoparticle
    • N. Nagahori, M. Abe, and S.-I. Nishimura Structural and functional glycosphingolipidomics by glycoblotting with an aminooxy-functionalized gold nanoparticle Biochemistry 48 2009 583 594
    • (2009) Biochemistry , vol.48 , pp. 583-594
    • Nagahori, N.1    Abe, M.2    Nishimura, S.-I.3
  • 77
    • 84871475298 scopus 로고    scopus 로고
    • Effect of ganglioside GM3 synthase gene knockout on the glycoprotein N-glycan profile of mouse embryonic fibroblast
    • N. Nagahori, T. Yamashita, M. Amano, and S.-I. Nishimura Effect of ganglioside GM3 synthase gene knockout on the glycoprotein N-glycan profile of mouse embryonic fibroblast Chembiochem 14 2013 73 82
    • (2013) Chembiochem , vol.14 , pp. 73-82
    • Nagahori, N.1    Yamashita, T.2    Amano, M.3    Nishimura, S.-I.4
  • 79
    • 0035353388 scopus 로고    scopus 로고
    • Zwitterionic SAMs that resist nonspecific adsorption of protein from aqueous buffer
    • R.E. Holmlin, X. Chen, R.G. Chapman, S. Takayama, and G.M. Whitesides Zwitterionic SAMs that resist nonspecific adsorption of protein from aqueous buffer Langmuir 17 2001 2841 2850 (Pubitemid 35330542)
    • (2001) Langmuir , vol.17 , Issue.9 , pp. 2841-2850
    • Holmlin, R.E.1    Chen, X.2    Chapman, R.G.3    Takayama, S.4    Whitesides, G.M.5
  • 80
    • 26844460799 scopus 로고    scopus 로고
    • Strong resistance of phosphorylcholine self-assembled monolayers to protein adsorption: Insights into nonfouling properties of zwitterionic materials
    • DOI 10.1021/ja054169u
    • S. Chen, J. Zheng, L. Li, and S. Jiang Strong resistance of phosphorylcholine self-assembled monolayers to protein adsorption: insights into nonfouling properties of zwitterionic materials J. Am. Chem. Soc. 127 2005 14473 14478 (Pubitemid 41457607)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.41 , pp. 14473-14478
    • Chen, S.1    Zheng, J.2    Li, L.3    Jiang, S.4
  • 82
    • 84857067090 scopus 로고    scopus 로고
    • Phosphorylcholine self-assembled monolayers-coated quantum dots: Real-time imaging of live animals by cell surface mimetic glyco-nanoparticles
    • S.-I. Nishimura Phosphorylcholine self-assembled monolayers-coated quantum dots: real-time imaging of live animals by cell surface mimetic glyco-nanoparticles Clin. Lab. Med. 132 2012 73 87
    • (2012) Clin. Lab. Med. , vol.132 , pp. 73-87
    • Nishimura, S.-I.1
  • 85
    • 84894794252 scopus 로고    scopus 로고
    • Serum glycan as a prognostic marker in patients with advanced hepatocellular carcinoma treated with sorafenib
    • 10.1002/hep.26531 (in press)
    • K. Miyahara, K. Nouso, Y. Miyake, S. Nakamura, S. Obi, M. Amano, K. Hirose, S.-I. Nishimura, and K. Yamamoto Serum glycan as a prognostic marker in patients with advanced hepatocellular carcinoma treated with sorafenib Hepatology 2013 10.1002/hep.26531 (in press)
    • (2013) Hepatology
    • Miyahara, K.1    Nouso, K.2    Miyake, Y.3    Nakamura, S.4    Obi, S.5    Amano, M.6    Hirose, K.7    Nishimura, S.-I.8    Yamamoto, K.9
  • 86
    • 33846496361 scopus 로고    scopus 로고
    • Identification of a novel cancer-specific immunodominant glycopeptide epitope in the MUC1 tandem repeat
    • DOI 10.1093/glycob/cwl061
    • M.A. Tarp, A.L. Sorensen, U. Mandel, H. Paulsen, J. Burchell, J. Taylor-Papadimitriou, and H. Clausen Identification of a novel cancer-specific immunodominant glycopeptide epitope in the MUC1 tandem repeat Glycobiology 17 2007 197 209 (Pubitemid 46152536)
    • (2007) Glycobiology , vol.17 , Issue.2 , pp. 197-209
    • Tarp, M.A.1    Sorensen, A.L.2    Mandel, U.3    Paulsen, H.4    Burchell, J.5    Taylor-Papadimitriou, J.6    Clausen, H.7
  • 91
    • 84872546499 scopus 로고    scopus 로고
    • Site-specific conformational alteration induced by sialylation of MUC1 tandem repeating glycopeptides at an epitope region for the anti-KL-6 monoclonal antibody
    • T. Matsushita, N. Ohyabu, N. Fujitani, K. Naruchi, H. Shimizu, H. Hinou, and S.-I. Nishimura Site-specific conformational alteration induced by sialylation of MUC1 tandem repeating glycopeptides at an epitope region for the anti-KL-6 monoclonal antibody Biochemistry 52 2013 402 414
    • (2013) Biochemistry , vol.52 , pp. 402-414
    • Matsushita, T.1    Ohyabu, N.2    Fujitani, N.3    Naruchi, K.4    Shimizu, H.5    Hinou, H.6    Nishimura, S.-I.7
  • 92
    • 33745686511 scopus 로고    scopus 로고
    • Synthesis and structural model of an α(2,6)-sialyl-T glycosylated MUC1 eicosapeptide under physiological conditions
    • DOI 10.1002/chem.200600144
    • S. Dziadek, C. Griesinger, H. Kunz, and U.M. Reinsheid Synthesis and structural model of an α(2,6)-sialyl-T glycosylated MUC1 eicosapeptide under physiological conditions Chem. Eur. J. 12 2006 4981 4993 (Pubitemid 43999118)
    • (2006) Chemistry - A European Journal , vol.12 , Issue.19 , pp. 4981-4993
    • Dziadek, S.1    Griesinger, C.2    Kunz, H.3    Reinscheid, U.M.4
  • 94
    • 0036852241 scopus 로고    scopus 로고
    • Cancer immunoediting: From immunosurveillance to tumor escape
    • DOI 10.1038/ni1102-991
    • G.P. Dunn, A.T. Bruce, H. Ikeda, L.J. Old, and R.D. Schreiber Cancer immunoediting: from immunosurveillance to tumor escape Nat. Immunol. 3 2002 991 998 (Pubitemid 35363648)
    • (2002) Nature Immunology , vol.3 , Issue.11 , pp. 991-998
    • Dunn, G.P.1    Bruce, A.T.2    Ikeda, H.3    Old, L.J.4    Schreiber, R.D.5
  • 95
    • 2542430341 scopus 로고    scopus 로고
    • The three Es of cancer immunoediting
    • DOI 10.1146/annurev.immunol.22.012703.104803
    • G.P. Dunn, L.J. Old, and R.D. Screiber The three Es of cancer immunoediting Annu. Rev. Immunol. 22 2004 329 360 (Pubitemid 38680426)
    • (2004) Annual Review of Immunology , vol.22 , pp. 329-360
    • Dunn, G.P.1    Old, L.J.2    Schreiber, R.D.3
  • 96
    • 33748987908 scopus 로고    scopus 로고
    • Cancer despite immunosurveillance: Immunoselection and immunosubversion
    • DOI 10.1038/nri1936, PII NRI1936
    • L. Zitvogel, A. Tesniere, and G. Kroemer Cancer despite immunosurveillance: immunoselection and immunosubversion Nat. Rev. Immunol. 6 2006 715 727 (Pubitemid 44453458)
    • (2006) Nature Reviews Immunology , vol.6 , Issue.10 , pp. 715-727
    • Zitvogel, L.1    Tesniere, A.2    Kroemer, G.3
  • 97
    • 0036561908 scopus 로고    scopus 로고
    • Modelling the molecular circuitry of cancer
    • W.C. Hahn, and R.A. Weinberg Modelling the molecular circuitry of cancer Nat. Rev. Cancer 2 2002 331 341 (Pubitemid 37328946)
    • (2002) Nature Reviews Cancer , vol.2 , Issue.5 , pp. 331-341
    • Hahn, W.C.1    Weinberg, R.A.2
  • 100
    • 0030830164 scopus 로고    scopus 로고
    • Localization of O-glycosylation sites on glycopeptide fragments from lactation-associated MUC1. All putative sites within the tandem repeat are glycosylation targets in vivo
    • DOI 10.1074/jbc.272.40.24780
    • S. Müller, S. Goletz, N. Packer, A. Gooley, A.M. Lawson, and F.-G. Hanisch Localization of O-glycosylation sites on glycopeptide fragments from lactation-associated MUC1: all putative sites within the tandem repeat are glycosylation targets in vivo J. Biol. Chem. 272 1997 24780 24793 (Pubitemid 27415647)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.40 , pp. 24780-24793
    • Muller, S.1    Goletz, S.2    Packer, N.3    Gooley, A.4    Lawson, A.M.5    Hanisch, F.-G.6
  • 101
    • 0037135544 scopus 로고    scopus 로고
    • Recombinant MUC1 probe authentically reflects cell-specific O-glycosylation profiles of endogenous breast cancer mucin. High density and prevalent core 2-based glycosylation
    • DOI 10.1074/jbc.M202921200
    • S. Müller, and F.-G. Hanisch Recombinant MUC1 probe authentically reflects cell-specific O-glycosylation profiles of endogenous breast cancer mucin: high density and prevalent core 2-based glycosylation J. Biol. Chem. 277 2002 26103 26112 (Pubitemid 34967094)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.29 , pp. 26103-26112
    • Muller, S.1    Hanisch, F.-G.2
  • 102
    • 34547759863 scopus 로고    scopus 로고
    • High-throughput carbohydrate microarray profiling of 27 antibodies demonstrates widespread specificity problems
    • DOI 10.1093/glycob/cwm047
    • J.C. Manimala, T.A. Roach, Z. Li, and J.C. Gildersleeve High-throughput carbohydrate microarray profiling of 27 antibodies demonstrates widespread specificity problems Glycobiology 17 2007 17C 23C (Pubitemid 47241816)
    • (2007) Glycobiology , vol.17 , Issue.8
    • Manimala, J.C.1    Roach, T.A.2    Li, Z.3    Gildersleeve, J.C.4


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