메뉴 건너뛰기




Volumn 16, Issue 12, 2015, Pages 29278-29304

Mass spectrometry-based N-glycomics of colorectal cancer

Author keywords

Cancer; Colorectal cancer; Glycome; Glycosylation; N glycomics

Indexed keywords

B RAF KINASE; BETA CATENIN; BEVACIZUMAB; CARCINOEMBRYONIC ANTIGEN RELATED CELL ADHESION MOLECULE 1; EPIDERMAL GROWTH FACTOR RECEPTOR 2; FLUOROURACIL; FOLINIC ACID; GLYCOPROTEIN; GLYCOSIDASE; GLYCOSYLTRANSFERASE; IRINOTECAN; MONOSACCHARIDE; N ACETYLGLUCOSAMINE; OXALIPLATIN; TRANSFORMING GROWTH FACTOR BETA RECEPTOR 2; POLYSACCHARIDE; TUMOR MARKER;

EID: 84949785431     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms161226165     Document Type: Review
Times cited : (22)

References (156)
  • 1
    • 35848961889 scopus 로고    scopus 로고
    • Prevention and early diagnosis of colorectal cancer
    • [PubMed]
    • Bretthauer, M.; Hoff, G. Prevention and early diagnosis of colorectal cancer. Tidsskr. Nor. Laegeforen. 2007, 127, 2688–2691. [PubMed]
    • (2007) Tidsskr. Nor. Laegeforen , vol.127 , pp. 2688-2691
    • Bretthauer, M.1    Hoff, G.2
  • 2
    • 14644396630 scopus 로고    scopus 로고
    • Colorectal cancer screening: Prospects for molecular stool analysis
    • [CrossRef][PubMed]
    • Davies, R.J.; Miller, R.; Coleman, N. Colorectal cancer screening: Prospects for molecular stool analysis. Nat. Rev. Cancer 2005, 5, 199–209. [CrossRef][PubMed]
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 199-209
    • Davies, R.J.1    Miller, R.2    Coleman, N.3
  • 3
    • 34547551323 scopus 로고    scopus 로고
    • Colonoscopy is superior to flexible sigmoidoscopy for colorectal cancer screening: Now beyond a reasonable doubt?
    • [CrossRef][PubMed]
    • Terdiman, J.P. Colonoscopy is superior to flexible sigmoidoscopy for colorectal cancer screening: Now beyond a reasonable doubt? Gastroenterology 2005, 129, 1793–1794. [CrossRef][PubMed]
    • (2005) Gastroenterology , vol.129 , pp. 1793-1794
    • Terdiman, J.P.1
  • 4
    • 0037310758 scopus 로고    scopus 로고
    • Gastrointestinal Consortium Panel. Colorectal cancer screening and surveillance: Clinical guidelines and rationale-Update based on new evidence
    • [CrossRef][PubMed]
    • Winawer, S.; Fletcher, R.; Rex, D.; Bond, J.; Burt, R.; Ferrucci, J.; Ganiats, T.; Levin, T.; Woolf, S.; Johnson, D., et al. Gastrointestinal Consortium Panel. Colorectal cancer screening and surveillance: Clinical guidelines and rationale-Update based on new evidence. Gastroenterology 2003, 124, 544–560. [CrossRef][PubMed]
    • (2003) Gastroenterology , vol.124 , pp. 544-560
    • Winawer, S.1    Fletcher, R.2    Rex, D.3    Bond, J.4    Burt, R.5    Ferrucci, J.6    Ganiats, T.7    Levin, T.8    Woolf, S.9    Johnson, D.10
  • 5
    • 0038662530 scopus 로고    scopus 로고
    • Proteomic applications for the early detection of cancer
    • [CrossRef][PubMed]
    • Wulfkuhle, J.D.; Liotta, L.A.; Petricoin, E.F. Proteomic applications for the early detection of cancer. Nat. Rev. Cancer 2003, 3, 267–275. [CrossRef][PubMed]
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 267-275
    • Wulfkuhle, J.D.1    Liotta, L.A.2    Petricoin, E.F.3
  • 6
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • [CrossRef]
    • Apweiler, R.; Hermjakob, H.; Sharon, N. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim. Biophys. Acta 1999, 1473, 4–8. [CrossRef]
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 7
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • [CrossRef][PubMed]
    • Ohtsubo, K.; Marth, J.D. Glycosylation in cellular mechanisms of health and disease. Cell 2006, 126, 855–867. [CrossRef][PubMed]
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 9
    • 0036677372 scopus 로고    scopus 로고
    • Glycosylation defining cancer malignancy: New winein an old bottle
    • [CrossRef][PubMed]
    • Hakomori, S. Glycosylation defining cancer malignancy: New wine in an old bottle. Proc. Natl. Acad. Sci. USA 2002, 99, 10231–10233. [CrossRef][PubMed]
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10231-10233
    • Hakomori, S.1
  • 11
    • 0024585483 scopus 로고
    • Aberrant glycosylation in tumors and tumor-associated carbohydrate antigens
    • Hakomori, S. Aberrant glycosylation in tumors and tumor-associated carbohydrate antigens. Adv. Cancer Res. 1989, 52, 257–331.
    • (1989) Adv. Cancer Res , vol.52 , pp. 257-331
    • Hakomori, S.1
  • 12
    • 21744431575 scopus 로고    scopus 로고
    • The sweet and sour of cancer: Glycans as novel therapeutic targets
    • [CrossRef][PubMed]
    • Fuster, M.M.; Esko, J.D. The sweet and sour of cancer: Glycans as novel therapeutic targets. Nat. Rev. Cancer 2005, 5, 526–542. [CrossRef][PubMed]
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 526-542
    • Fuster, M.M.1    Esko, J.D.2
  • 15
    • 0027401607 scopus 로고
    • The multistep nature of cancer
    • [CrossRef]
    • Vogelstein, B.; Kinzler, K.W. The multistep nature of cancer. Trends Genet. 1993, 9, 138–141. [CrossRef]
    • (1993) Trends Genet , vol.9 , pp. 138-141
    • Vogelstein, B.1    Kinzler, K.W.2
  • 16
    • 23844507181 scopus 로고    scopus 로고
    • The role of the Wnt signalling pathway in colorectal tumorigenesis
    • [CrossRef][PubMed]
    • Behrens, J. The role of the Wnt signalling pathway in colorectal tumorigenesis. Biochem. Soc. Trans. 2005, 33, 672–675. [CrossRef][PubMed]
    • (2005) Biochem. Soc. Trans , vol.33 , pp. 672-675
    • Behrens, J.1
  • 17
    • 12244301669 scopus 로고    scopus 로고
    • Immunogenic peptides generated by frameshift mutations in DNA mismatch repair-deficient cancer cells
    • [PubMed]
    • Schwitalle, Y.; Linnebacher, M.; Ripberger, E.; Gebert, J.; von Knebel Doeberitz, M. Immunogenic peptides generated by frameshift mutations in DNA mismatch repair-deficient cancer cells. Cancer Immun. 2004, 4, 14. [PubMed]
    • (2004) Cancer Immun , vol.4
    • Schwitalle, Y.1    Linnebacher, M.2    Ripberger, E.3    Gebert, J.4    Von Knebel Doeberitz, M.5
  • 19
    • 0028987249 scopus 로고
    • Regulation of intracellular beta-catenin levels by the adenomatous polyposis coli (APC) tumor-suppressor protein
    • [CrossRef][PubMed]
    • Munemitsu, S.; Albert, I.; Souza, B.; Rubinfeld, B.; Polakis, P. Regulation of intracellular beta-catenin levels by the adenomatous polyposis coli (APC) tumor-suppressor protein. Proc. Natl. Acad. Sci. USA 1995, 92, 3046–3050. [CrossRef][PubMed]
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3046-3050
    • Munemitsu, S.1    Albert, I.2    Souza, B.3    Rubinfeld, B.4    Polakis, P.5
  • 21
    • 0032871491 scopus 로고    scopus 로고
    • How does colorectal cancer present? symptoms, duration, and clues to location
    • [PubMed]
    • Majumdar, S.R.; Fletcher, R.H.; Evans, A.T. How does colorectal cancer present? symptoms, duration, and clues to location. Am. J. Gastroenterol. 1999, 94, 3039–3045. [PubMed]
    • (1999) Am. J. Gastroenterol , vol.94 , pp. 3039-3045
    • Majumdar, S.R.1    Fletcher, R.H.2    Evans, A.T.3
  • 22
    • 79957528016 scopus 로고    scopus 로고
    • The diagnostic value of symptoms for colorectal cancer in primary care: A systematic review
    • [CrossRef][PubMed]
    • Astin, M.; Griffin, T.; Neal, R.D.; Rose, P.; Hamilton, W. The diagnostic value of symptoms for colorectal cancer in primary care: A systematic review. Br. J. Gen. Pract. 2011, 61, e231–e243. [CrossRef][PubMed]
    • (2011) Br. J. Gen. Pract , vol.61 , pp. e231-e243
    • Astin, M.1    Griffin, T.2    Neal, R.D.3    Rose, P.4    Hamilton, W.5
  • 24
    • 0034712536 scopus 로고    scopus 로고
    • Irinotecan combined with fluorouracil compared with fluorouracil alone as first-line treatment for metastatic colorectal cancer: A multicentre randomised trial
    • [CrossRef]
    • Douillard, J.Y.; Cunningham, D.; Roth, A.D.; Navarro, M.; James, R.D.; Karasek, P.; Jandik, P.; Iveson, T.; Carmichael, J.; Alakl, M., et al. Irinotecan combined with fluorouracil compared with fluorouracil alone as first-line treatment for metastatic colorectal cancer: A multicentre randomised trial. Lancet 2000, 355, 1041–1047. [CrossRef]
    • (2000) Lancet , vol.355 , pp. 1041-1047
    • Douillard, J.Y.1    Cunningham, D.2    Roth, A.D.3    Navarro, M.4    James, R.D.5    Karasek, P.6    Jandik, P.7    Iveson, T.8    Carmichael, J.9    Alakl, M.10
  • 26
    • 0026729853 scopus 로고
    • Cytogenetic and molecular investigations of an abnormal Y chromosome: Evidence for a pseudo-dicentric (Yq) isochromosome
    • [PubMed]
    • Savary, J.B.; Vasseur, F.; Flactif, M.; Willatt, L.; Lefebvre, J.; Ferguson-Smith, M.A.; Deminatti, M.M. Cytogenetic and molecular investigations of an abnormal Y chromosome: Evidence for a pseudo-dicentric (Yq) isochromosome. Ann. Genet. 1992, 35, 134–139. [PubMed]
    • (1992) Ann. Genet , vol.35 , pp. 134-139
    • Savary, J.B.1    Vasseur, F.2    Flactif, M.3    Willatt, L.4    Lefebvre, J.5    Ferguson-Smith, M.A.6    Deminatti, M.M.7
  • 27
    • 36749039163 scopus 로고    scopus 로고
    • The multidisciplinary management of gastrointestinal cancer. The integration of cytotoxics and biologicals in the treatment of metastatic colorectal cancer
    • [CrossRef][PubMed]
    • Van Cutsem, E.; Geboes, K. The multidisciplinary management of gastrointestinal cancer. The integration of cytotoxics and biologicals in the treatment of metastatic colorectal cancer. Best Pract. Res. Clin. Gastroenterol. 2007, 21, 1089–1108. [CrossRef][PubMed]
    • (2007) Best Pract. Res. Clin. Gastroenterol , vol.21 , pp. 1089-1108
    • Van Cutsem, E.1    Geboes, K.2
  • 28
    • 6944234851 scopus 로고    scopus 로고
    • New options and old dilemmas in the treatment of patients with advanced colorectal cancer
    • [CrossRef][PubMed]
    • Punt, C. New options and old dilemmas in the treatment of patients with advanced colorectal cancer. Ann. Oncol. 2004, 15, 1453–1459. [CrossRef][PubMed]
    • (2004) Ann. Oncol , vol.15 , pp. 1453-1459
    • Punt, C.1
  • 29
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • [CrossRef][PubMed]
    • Varki, A. Biological roles of oligosaccharides: All of the theories are correct. Glycobiology 1993, 3, 97–130. [CrossRef][PubMed]
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 30
    • 20844437106 scopus 로고    scopus 로고
    • Glycans in cancer and inflammation—Potential for therapeutics and diagnostics
    • [CrossRef][PubMed]
    • Dube, D.H.; Bertozzi, C.R. Glycans in cancer and inflammation—Potential for therapeutics and diagnostics. Nat. Rev. Drug Discov. 2005, 4, 477–488. [CrossRef][PubMed]
    • (2005) Nat. Rev. Drug Discov , vol.4 , pp. 477-488
    • Dube, D.H.1    Bertozzi, C.R.2
  • 31
    • 67649839223 scopus 로고    scopus 로고
    • N-Glycans
    • 2nd ed; Varki, A., Cummings, R.D., Esko, J.D., Freeze, H.H., Stanley, P., Bertozzi, C.R., Hart, G.W., Etzler, M.E., Eds.; Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY, USA
    • Stanley, P.; Schachter, H.; Taniguchi, N. N-Glycans. In Essentials of Glycobiology, 2nd ed.; Varki, A., Cummings, R.D., Esko, J.D., Freeze, H.H., Stanley, P., Bertozzi, C.R., Hart, G.W., Etzler, M.E., Eds.; Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY, USA, 2009.
    • (2009) Essentials of Glycobiology
    • Stanley, P.1    Schachter, H.2    Taniguchi, N.3
  • 32
    • 68249085304 scopus 로고    scopus 로고
    • Paucimannose N-glycans in Caenorhabditis elegans and Drosophila melanogaster
    • [CrossRef][PubMed]
    • Schachter, H. Paucimannose N-glycans in Caenorhabditis elegans and Drosophila melanogaster. Carbohydr. Res. 2009, 344, 1391–1396. [CrossRef][PubMed]
    • (2009) Carbohydr. Res , vol.344 , pp. 1391-1396
    • Schachter, H.1
  • 33
    • 84891793435 scopus 로고    scopus 로고
    • Comparative N-glycan profiling of colorectal cancer cell lines reveals unique bisecting GlcNAc and alpha-2,3-linked sialic acid determinants are associated with membrane proteins of the more metastatic/aggressive cell lines
    • [CrossRef][PubMed]
    • Sethi, M.K.; Thaysen-Andersen, M.; Smith, J.T.; Baker, M.S.; Packer, N.H.; Hancock, W.S.; Fanayan, S. Comparative N-glycan profiling of colorectal cancer cell lines reveals unique bisecting GlcNAc and alpha-2,3-linked sialic acid determinants are associated with membrane proteins of the more metastatic/aggressive cell lines. J. Proteome Res. 2014, 13, 277–288. [CrossRef][PubMed]
    • (2014) J. Proteome Res , vol.13 , pp. 277-288
    • Sethi, M.K.1    Thaysen-Andersen, M.2    Smith, J.T.3    Baker, M.S.4    Packer, N.H.5    Hancock, W.S.6    Fanayan, S.7
  • 34
    • 84868035982 scopus 로고    scopus 로고
    • Comparative structural analysis of the glycosylation of salivary and buccal cell proteins: Innate protection against infection by Candida albicans
    • [CrossRef][PubMed]
    • Everest-Dass, A.V.; Jin, D.; Thaysen-Andersen, M.; Nevalainen, H.; Kolarich, D.; Packer, N.H. Comparative structural analysis of the glycosylation of salivary and buccal cell proteins: Innate protection against infection by Candida albicans. Glycobiology 2012, 22, 1465–1479. [CrossRef][PubMed]
    • (2012) Glycobiology , vol.22 , pp. 1465-1479
    • Everest-Dass, A.V.1    Jin, D.2    Thaysen-Andersen, M.3    Nevalainen, H.4    Kolarich, D.5    Packer, N.H.6
  • 36
    • 84924984955 scopus 로고    scopus 로고
    • Cystic fibrosis and bacterial colonization define the sputum N-glycosylation phenotype
    • [CrossRef][PubMed]
    • Venkatakrishnan, V.; Thaysen-Andersen, M.; Chen, S.C.; Nevalainen, H.; Packer, N.H. Cystic fibrosis and bacterial colonization define the sputum N-glycosylation phenotype. Glycobiology 2015, 25, 88–100. [CrossRef][PubMed]
    • (2015) Glycobiology , vol.25 , pp. 88-100
    • Venkatakrishnan, V.1    Thaysen-Andersen, M.2    Chen, S.C.3    Nevalainen, H.4    Packer, N.H.5
  • 37
    • 84926512718 scopus 로고    scopus 로고
    • Human neutrophils secrete bioactive paucimannosidic proteins from azurophilic granules into pathogen-infected sputum
    • [CrossRef][PubMed]
    • Thaysen-Andersen, M.; Venkatakrishnan, V.; Loke, I.; Laurini, C.; Diestel, S.; Parker, B.L.; Packer, N.H. Human neutrophils secrete bioactive paucimannosidic proteins from azurophilic granules into pathogen-infected sputum. J. Biol. Chem. 2015, 290, 8789–8802. [CrossRef][PubMed]
    • (2015) J. Biol. Chem , vol.290 , pp. 8789-8802
    • Thaysen-Andersen, M.1    Venkatakrishnan, V.2    Loke, I.3    Laurini, C.4    Diestel, S.5    Parker, B.L.6    Packer, N.H.7
  • 38
    • 70449573717 scopus 로고    scopus 로고
    • Biological Roles of Glycans
    • 2nd ed; Varki, A., Cummings, R.D., Esko, J.D., Freeze, H.H., Stanley, P., Bertozzi, C.R., Hart, G.W., Etzler, M.E., Eds.; Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY, USA
    • Varki, A.; Lowe, J.B. Biological Roles of Glycans. In Essentials of Glycobiology, 2nd ed.; Varki, A., Cummings, R.D., Esko, J.D., Freeze, H.H., Stanley, P., Bertozzi, C.R., Hart, G.W., Etzler, M.E., Eds.; Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY, USA, 2009.
    • (2009) Essentials of Glycobiology
    • Varki, A.1    Lowe, J.B.2
  • 39
    • 0021832294 scopus 로고
    • Host-mediated selection of influenza virus receptor variants. Sialic acid-alpha 2,6Gal-specific clones of A/duck/Ukraine/1/63 revert to sialic acid-alpha 2,3Gal-specific wild type in ovo
    • [PubMed]
    • Rogers, G.N.; Daniels, R.S.; Skehel, J.J.; Wiley, D.C.; Wang, X.F.; Higa, H.H.; Paulson, J.C. Host-mediated selection of influenza virus receptor variants. Sialic acid-alpha 2,6Gal-specific clones of A/duck/Ukraine/1/63 revert to sialic acid-alpha 2,3Gal-specific wild type in ovo. J. Biol. Chem. 1985, 260, 7362–7367. [PubMed]
    • (1985) J. Biol. Chem , vol.260 , pp. 7362-7367
    • Rogers, G.N.1    Daniels, R.S.2    Skehel, J.J.3    Wiley, D.C.4    Wang, X.F.5    Higa, H.H.6    Paulson, J.C.7
  • 40
    • 0029858031 scopus 로고    scopus 로고
    • Selectins and their ligands: Current concepts and controversies
    • [PubMed]
    • Kansas, G.S. Selectins and their ligands: Current concepts and controversies. Blood 1996, 88, 3259–3287. [PubMed]
    • (1996) Blood , vol.88 , pp. 3259-3287
    • Kansas, G.S.1
  • 41
    • 0028198111 scopus 로고
    • How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum
    • [CrossRef][PubMed]
    • Helenius, A. How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol. Biol. Cell 1994, 5, 253–265. [CrossRef][PubMed]
    • (1994) Mol. Biol. Cell , vol.5 , pp. 253-265
    • Helenius, A.1
  • 42
    • 0022458022 scopus 로고
    • Lysosomal enzyme trafficking in mannose 6-phosphate receptor-positive mouse L-cells: Demonstration of a steady state accumulation of phosphorylated acid hydrolases
    • [CrossRef][PubMed]
    • Gabel, C.A.; Foster, S.A. Lysosomal enzyme trafficking in mannose 6-phosphate receptor-positive mouse L-cells: Demonstration of a steady state accumulation of phosphorylated acid hydrolases. J. Cell Biol. 1986, 102, 943–950. [CrossRef][PubMed]
    • (1986) J. Cell Biol , vol.102 , pp. 943-950
    • Gabel, C.A.1    Foster, S.A.2
  • 43
    • 0023305010 scopus 로고
    • Thyroglobulin, the major and obligatory exportable protein of thyroid follicle cells, carries the lysosomal recognition marker mannose-6-phosphate
    • [PubMed]
    • Herzog, V.; Neumuller, W.; Holzmann, B. Thyroglobulin, the major and obligatory exportable protein of thyroid follicle cells, carries the lysosomal recognition marker mannose-6-phosphate. EMBO J. 1987, 6, 555–560. [PubMed]
    • (1987) EMBO J , vol.6 , pp. 555-560
    • Herzog, V.1    Neumuller, W.2    Holzmann, B.3
  • 44
    • 44449153943 scopus 로고    scopus 로고
    • Functional roles of N-glycans in cell signaling and cell adhesion in cancer
    • [CrossRef][PubMed]
    • Zhao, Y.Y.; Takahashi, M.; Gu, J.G.; Miyoshi, E.; Matsumoto, A.; Kitazume, S.; Taniguchi, N. Functional roles of N-glycans in cell signaling and cell adhesion in cancer. Cancer Sci. 2008, 99, 1304–1310. [CrossRef][PubMed]
    • (2008) Cancer Sci , vol.99 , pp. 1304-1310
    • Zhao, Y.Y.1    Takahashi, M.2    Gu, J.G.3    Miyoshi, E.4    Matsumoto, A.5    Kitazume, S.6    Taniguchi, N.7
  • 45
    • 0029053448 scopus 로고
    • The role of N-glycans in the secretory pathway
    • [CrossRef]
    • Fiedler, K.; Simons, K. The role of N-glycans in the secretory pathway. Cell 1995, 81, 309–312. [CrossRef]
    • (1995) Cell , vol.81 , pp. 309-312
    • Fiedler, K.1    Simons, K.2
  • 46
    • 84923313064 scopus 로고    scopus 로고
    • Glycosylation characteristics of colorectal cancer
    • [PubMed]
    • Holst, S.; Wuhrer, M.; Rombouts, Y. Glycosylation characteristics of colorectal cancer. Adv. Cancer Res. 2015, 126, 203–256. [PubMed]
    • (2015) Adv. Cancer Res , vol.126 , pp. 203-256
    • Holst, S.1    Wuhrer, M.2    Rombouts, Y.3
  • 47
    • 84860239658 scopus 로고    scopus 로고
    • Aberrant glycosylation associated with enzymes as cancer biomarkers
    • [CrossRef][PubMed]
    • Meany, D.L.; Chan, D.W. Aberrant glycosylation associated with enzymes as cancer biomarkers. Clin. Proteom. 2011, 8, 7. [CrossRef][PubMed]
    • (2011) Clin. Proteom , vol.8
    • Meany, D.L.1    Chan, D.W.2
  • 48
    • 84858138360 scopus 로고    scopus 로고
    • Loss and recovery of Mgat3 and GnT-III Mediated E-cadherin N-glycosylation is a mechanism involved in epithelial-mesenchymal-epithelial transitions
    • [CrossRef][PubMed]
    • Pinho, S.S.; Oliveira, P.; Cabral, J.; Carvalho, S.; Huntsman, D.; Gartner, F.; Seruca, R.; Reis, C.A.; Oliveira, C. Loss and recovery of Mgat3 and GnT-III Mediated E-cadherin N-glycosylation is a mechanism involved in epithelial-mesenchymal-epithelial transitions. PLoS ONE 2012, 7, e33191. [CrossRef][PubMed]
    • (2012) Plos ONE , vol.7
    • Pinho, S.S.1    Oliveira, P.2    Cabral, J.3    Carvalho, S.4    Huntsman, D.5    Gartner, F.6    Seruca, R.7    Reis, C.A.8    Oliveira, C.9
  • 49
    • 84857692860 scopus 로고    scopus 로고
    • Branched N-glycans and their implications for cell adhesion, signaling and clinical applications for cancer biomarkers and in therapeutics
    • [CrossRef][PubMed]
    • Taniguchi, N.; Korekane, H. Branched N-glycans and their implications for cell adhesion, signaling and clinical applications for cancer biomarkers and in therapeutics. BMB Rep. 2011, 44, 772–781. [CrossRef][PubMed]
    • (2011) BMB Rep , vol.44 , pp. 772-781
    • Taniguchi, N.1    Korekane, H.2
  • 50
    • 0028169250 scopus 로고
    • Cytochemical staining for beta 1,6 branching of asparagine-linked oligosaccharides in variants of metastatic human colon carcinoma cells
    • [PubMed]
    • Li, W.P.; Zuber, C.; Heitz, P.U.; Roth, J. Cytochemical staining for beta 1,6 branching of asparagine-linked oligosaccharides in variants of metastatic human colon carcinoma cells. Am. J. Pathol. 1994, 145, 470–480. [PubMed]
    • (1994) Am. J. Pathol , vol.145 , pp. 470-480
    • Li, W.P.1    Zuber, C.2    Heitz, P.U.3    Roth, J.4
  • 52
    • 0023255440 scopus 로고
    • Beta 1–6 branching of Asn-linked oligosaccharides is directly associated with metastasis
    • [CrossRef][PubMed]
    • Dennis, J.W.; Laferte, S.; Waghorne, C.; Breitman, M.L.; Kerbel, R.S. Beta 1–6 branching of Asn-linked oligosaccharides is directly associated with metastasis. Science 1987, 236, 582–585. [CrossRef][PubMed]
    • (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
  • 53
    • 0035526267 scopus 로고    scopus 로고
    • Sialyltransferases in cancer
    • [CrossRef]
    • Dall’Olio, F.; Chiricolo, M. Sialyltransferases in cancer. Glycoconjug. J. 2001, 18, 841–850. [CrossRef]
    • (2001) Glycoconjug. J , vol.18 , pp. 841-850
    • Dall’Olio, F.1    Chiricolo, M.2
  • 55
    • 0024448635 scopus 로고
    • Increased CMP-NeuAc:Gal beta 1,4GlcNAc-R alpha 2,6 sialyltransferase activity in human colorectal cancer tissues
    • [PubMed]
    • Dall’Olio, F.; Malagolini, N.; di Stefano, G.; Minni, F.; Marrano, D.; Serafini-Cessi, F. Increased CMP-NeuAc:Gal beta 1,4GlcNAc-R alpha 2,6 sialyltransferase activity in human colorectal cancer tissues. Int. J. Cancer 1989, 44, 434–439. [PubMed]
    • (1989) Int. J. Cancer , vol.44 , pp. 434-439
    • Dall’Olio, F.1    Malagolini, N.2    Di Stefano, G.3    Minni, F.4    Marrano, D.5    Serafini-Cessi, F.6
  • 56
    • 0027723424 scopus 로고
    • Enhanced activity of CMP-neuAc:Gal beta 1,4GlcNAc:Alpha 2,6-sialyltransferase in metastasizing human colorectal tumor tissue and serum of tumor patients
    • [CrossRef]
    • Gessner, P.; Riedl, S.; Quentmaier, A.; Kemmner, W. Enhanced activity of CMP-neuAc:Gal beta 1,4GlcNAc:alpha 2,6-sialyltransferase in metastasizing human colorectal tumor tissue and serum of tumor patients. Cancer Lett. 1993, 75, 143–149. [CrossRef]
    • (1993) Cancer Lett , vol.75 , pp. 143-149
    • Gessner, P.1    Riedl, S.2    Quentmaier, A.3    Kemmner, W.4
  • 57
    • 84943593972 scopus 로고    scopus 로고
    • In-depth N-glycome profiling of paired colorectal cancer and non-tumorigenic tissues reveals cancer-, stage- and EGFR-specific protein N-glycosylation
    • [CrossRef][PubMed]
    • Sethi, M.K.; Kim, H.; Park, C.K.; Baker, M.S.; Paik, Y.K.; Packer, N.H.; Hancock, W.S.; Fanayan, S.; Thaysen-Andersen, M. In-depth N-glycome profiling of paired colorectal cancer and non-tumorigenic tissues reveals cancer-, stage- and EGFR-specific protein N-glycosylation. Glycobiology 2015, 25, 1064–1078. [CrossRef][PubMed]
    • (2015) Glycobiology , vol.25 , pp. 1064-1078
    • Sethi, M.K.1    Kim, H.2    Park, C.K.3    Baker, M.S.4    Paik, Y.K.5    Packer, N.H.6    Hancock, W.S.7    Fanayan, S.8    Thaysen-Andersen, M.9
  • 58
    • 0026695634 scopus 로고
    • Sialyltransferase activity and hepatic tumor growth in a nude mouse model of colorectal cancer metastases
    • [PubMed]
    • Harvey, B.E.; Toth, C.A.; Wagner, H.E.; Steele, G.D., Jr.; Thomas, P. Sialyltransferase activity and hepatic tumor growth in a nude mouse model of colorectal cancer metastases. Cancer Res. 1992, 52, 1775–1779. [PubMed]
    • (1992) Cancer Res , vol.52 , pp. 1775-1779
    • Harvey, B.E.1    Toth, C.A.2    Wagner, H.E.3    Steele, G.D.4    Thomas, P.5
  • 59
    • 84888586398 scopus 로고    scopus 로고
    • Increasing the alpha 2, 6 sialylation of glycoproteins may contribute to metastatic spread and therapeutic resistance in colorectal cancer
    • [CrossRef][PubMed]
    • Park, J.J.; Lee, M. Increasing the alpha 2, 6 sialylation of glycoproteins may contribute to metastatic spread and therapeutic resistance in colorectal cancer. Gut Liver 2013, 7, 629–641. [CrossRef][PubMed]
    • (2013) Gut Liver , vol.7 , pp. 629-641
    • Park, J.J.1    Lee, M.2
  • 61
    • 0025048023 scopus 로고
    • Sialosyl-Tn. A novel mucin antigen associated with prognosis in colorectal cancer patients
    • [CrossRef]
    • Itzkowitz, S.H.; Bloom, E.J.; Kokal, W.A.; Modin, G.; Hakomori, S.; Kim, Y.S. Sialosyl-Tn. A novel mucin antigen associated with prognosis in colorectal cancer patients. Cancer 1990, 66, 1960–1966. [CrossRef]
    • (1990) Cancer , vol.66 , pp. 1960-1966
    • Itzkowitz, S.H.1    Bloom, E.J.2    Kokal, W.A.3    Modin, G.4    Hakomori, S.5    Kim, Y.S.6
  • 63
    • 0028041301 scopus 로고
    • Selectin ligands
    • [CrossRef][PubMed]
    • Varki, A. Selectin ligands. Proc. Natl. Acad. Sci. USA 1994, 91, 7390–7397. [CrossRef][PubMed]
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7390-7397
    • Varki, A.1
  • 64
    • 0032482987 scopus 로고    scopus 로고
    • P-selectin deficiency attenuates tumor growth and metastasis
    • [CrossRef][PubMed]
    • Kim, Y.J.; Borsig, L.; Varki, N.M.; Varki, A. P-selectin deficiency attenuates tumor growth and metastasis. Proc. Natl. Acad. Sci. USA 1998, 95, 9325–9330. [CrossRef][PubMed]
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9325-9330
    • Kim, Y.J.1    Borsig, L.2    Varki, N.M.3    Varki, A.4
  • 65
    • 0037133173 scopus 로고    scopus 로고
    • Synergistic effects of L- and P-selectin in facilitating tumor metastasis can involve non-mucin ligands and implicate leukocytes as enhancers of metastasis
    • [CrossRef][PubMed]
    • Borsig, L.; Wong, R.; Hynes, R.O.; Varki, N.M.; Varki, A. Synergistic effects of L- and P-selectin in facilitating tumor metastasis can involve non-mucin ligands and implicate leukocytes as enhancers of metastasis. Proc. Natl. Acad. Sci. USA 2002, 99, 2193–2198. [CrossRef][PubMed]
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2193-2198
    • Borsig, L.1    Wong, R.2    Hynes, R.O.3    Varki, N.M.4    Varki, A.5
  • 66
    • 84879200371 scopus 로고    scopus 로고
    • Alpha2,3-Sialyltransferase ST3Gal IV promotes migration and metastasis in pancreatic adenocarcinoma cells and tends to be highly expressed in pancreatic adenocarcinoma tissues
    • [CrossRef][PubMed]
    • Perez-Garay, M.; Arteta, B.; Llop, E.; Cobler, L.; Pages, L.; Ortiz, R.; Ferri, M.J.; de Bolo, C.; Figueras, J.; de Llorens, R., et al. alpha2,3-Sialyltransferase ST3Gal IV promotes migration and metastasis in pancreatic adenocarcinoma cells and tends to be highly expressed in pancreatic adenocarcinoma tissues. Int. J. Biochem. Cell Biol. 2013, 45, 1748–1757. [CrossRef][PubMed]
    • (2013) Int. J. Biochem. Cell Biol. , vol.45 , pp. 1748-1757
    • Perez-Garay, M.1    Arteta, B.2    Llop, E.3    Cobler, L.4    Pages, L.5    Ortiz, R.6    Ferri, M.J.7    De Bolo, C.8    Figueras, J.9    De Llorens, R.10
  • 68
  • 69
    • 0035361603 scopus 로고    scopus 로고
    • Increased expression of UDP-galactose transporter messenger RNA in human colon cancer tissues and its implication in synthesis of Thomsen-Friedenreich antigen and sialyl Lewis A/X determinants
    • [PubMed]
    • Kumamoto, K.; Goto, Y.; Sekikawa, K.; Takenoshita, S.; Ishida, N.; Kawakita, M.; Kannagi, R. Increased expression of UDP-galactose transporter messenger RNA in human colon cancer tissues and its implication in synthesis of Thomsen-Friedenreich antigen and sialyl Lewis A/X determinants. Cancer Res. 2001, 61, 4620–4627. [PubMed]
    • (2001) Cancer Res , vol.61 , pp. 4620-4627
    • Kumamoto, K.1    Goto, Y.2    Sekikawa, K.3    Takenoshita, S.4    Ishida, N.5    Kawakita, M.6    Kannagi, R.7
  • 70
    • 77952836494 scopus 로고    scopus 로고
    • Epigenetic silencing of the sulfate transporter gene DTDST induces sialyl Lewisx expression and accelerates proliferation of colon cancer cells
    • [CrossRef][PubMed]
    • Yusa, A.; Miyazaki, K.; Kimura, N.; Izawa, M.; Kannagi, R. Epigenetic silencing of the sulfate transporter gene DTDST induces sialyl Lewisx expression and accelerates proliferation of colon cancer cells. Cancer Res. 2010, 70, 4064–4073. [CrossRef][PubMed]
    • (2010) Cancer Res , vol.70 , pp. 4064-4073
    • Yusa, A.1    Miyazaki, K.2    Kimura, N.3    Izawa, M.4    Kannagi, R.5
  • 71
    • 0037014655 scopus 로고    scopus 로고
    • The action of N-acetylglucosaminyltransferase-V is prevented by the bisecting GlcNAc residue at the catalytic step
    • [CrossRef]
    • Sasai, K.; Ikeda, Y.; Eguchi, H.; Tsuda, T.; Honke, K.; Taniguchi, N. The action of N-acetylglucosaminyltransferase-V is prevented by the bisecting GlcNAc residue at the catalytic step. FEBS Lett. 2002, 522, 151–155. [CrossRef]
    • (2002) FEBS Lett , vol.522 , pp. 151-155
    • Sasai, K.1    Ikeda, Y.2    Eguchi, H.3    Tsuda, T.4    Honke, K.5    Taniguchi, N.6
  • 72
    • 33845961737 scopus 로고    scopus 로고
    • N-acetylglucosaminyltransferase III antagonizes the effect of N-acetylglucosaminyltransferase V on alpha3beta1 integrin-mediated cell migration
    • [CrossRef][PubMed]
    • Zhao, Y.; Nakagawa, T.; Itoh, S.; Inamori, K.; Isaji, T.; Kariya, Y.; Kondo, A.; Miyoshi, E.; Miyazaki, K.; Kawasaki, N., et al. N-acetylglucosaminyltransferase III antagonizes the effect of N-acetylglucosaminyltransferase V on alpha3beta1 integrin-mediated cell migration. J. Biol. Chem. 2006, 281, 32122–32130. [CrossRef][PubMed]
    • (2006) J. Biol. Chem. , vol.281 , pp. 32122-32130
    • Zhao, Y.1    Nakagawa, T.2    Itoh, S.3    Inamori, K.4    Isaji, T.5    Kariya, Y.6    Kondo, A.7    Miyoshi, E.8    Miyazaki, K.9    Kawasaki, N.10
  • 73
    • 0035815609 scopus 로고    scopus 로고
    • The relative activities of the C2GnT1 and ST3Gal-I glycosyltransferases determine O-glycan structure and expression of a tumor-associated epitope on MUC1
    • [CrossRef][PubMed]
    • Dalziel, M.; Whitehouse, C.; McFarlane, I.; Brockhausen, I.; Gschmeissner, S.; Schwientek, T.; Clausen, H.; Burchell, J.M.; Taylor-Papadimitriou, J. The relative activities of the C2GnT1 and ST3Gal-I glycosyltransferases determine O-glycan structure and expression of a tumor-associated epitope on MUC1. J. Biol. Chem. 2001, 276, 11007–11015. [CrossRef][PubMed]
    • (2001) J. Biol. Chem , vol.276 , pp. 11007-11015
    • Dalziel, M.1    Whitehouse, C.2    McFarlane, I.3    Brockhausen, I.4    Gschmeissner, S.5    Schwientek, T.6    Clausen, H.7    Burchell, J.M.8    Taylor-Papadimitriou, J.9
  • 74
    • 0035361378 scopus 로고    scopus 로고
    • Overexpression of sialyltransferase CMP-sialic acid:Galbeta1,3GalNAc-R alpha6-Sialyltransferase is related to poor patient survival in human colorectal carcinomas
    • [PubMed]
    • Schneider, F.; Kemmner, W.; Haensch, W.; Franke, G.; Gretschel, S.; Karsten, U.; Schlag, P.M. Overexpression of sialyltransferase CMP-sialic acid:Galbeta1,3GalNAc-R alpha6-Sialyltransferase is related to poor patient survival in human colorectal carcinomas. Cancer Res. 2001, 61, 4605–4611. [PubMed]
    • (2001) Cancer Res , vol.61 , pp. 4605-4611
    • Schneider, F.1    Kemmner, W.2    Haensch, W.3    Franke, G.4    Gretschel, S.5    Karsten, U.6    Schlag, P.M.7
  • 76
    • 0035877279 scopus 로고    scopus 로고
    • Overexpression of lysosomal-type sialidase leads to suppression of metastasis associated with reversion of malignant phenotype in murine B16 melanoma cells
    • [CrossRef][PubMed]
    • Kato, T.; Wang, Y.; Yamaguchi, K.; Milner, C.M.; Shineha, R.; Satomi, S.; Miyagi, T. Overexpression of lysosomal-type sialidase leads to suppression of metastasis associated with reversion of malignant phenotype in murine B16 melanoma cells. Int. J. Cancer 2001, 92, 797–804. [CrossRef][PubMed]
    • (2001) Int. J. Cancer , vol.92 , pp. 797-804
    • Kato, T.1    Wang, Y.2    Yamaguchi, K.3    Milner, C.M.4    Shineha, R.5    Satomi, S.6    Miyagi, T.7
  • 77
    • 0037049967 scopus 로고    scopus 로고
    • Reduced sialidase expression in highly metastatic variants of mouse colon adenocarcinoma 26 and retardation of their metastatic ability by sialidase overexpression
    • [CrossRef][PubMed]
    • Sawada, M.; Moriya, S.; Saito, S.; Shineha, R.; Satomi, S.; Yamori, T.; Tsuruo, T.; Kannagi, R.; Miyagi, T. Reduced sialidase expression in highly metastatic variants of mouse colon adenocarcinoma 26 and retardation of their metastatic ability by sialidase overexpression. Int. J. Cancer 2002, 97, 180–185. [CrossRef][PubMed]
    • (2002) Int. J. Cancer , vol.97 , pp. 180-185
    • Sawada, M.1    Moriya, S.2    Saito, S.3    Shineha, R.4    Satomi, S.5    Yamori, T.6    Tsuruo, T.7    Kannagi, R.8    Miyagi, T.9
  • 78
    • 77950410995 scopus 로고    scopus 로고
    • Alterations in glycosylation as biomarkers for cancer detection
    • [CrossRef][PubMed]
    • Reis, C.A.; Osorio, H.; Silva, L.; Gomes, C.; David, L. Alterations in glycosylation as biomarkers for cancer detection. J. Clin. Pathol. 2010, 63, 322–329. [CrossRef][PubMed]
    • (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
  • 80
    • 34250217743 scopus 로고    scopus 로고
    • Multiplexed analysis of glycan variation on native proteins captured by antibody microarrays
    • [CrossRef][PubMed]
    • Chen, S.; LaRoche, T.; Hamelinck, D.; Bergsma, D.; Brenner, D.; Simeone, D.; Brand, R.E.; Haab, B.B. Multiplexed analysis of glycan variation on native proteins captured by antibody microarrays. Nat. Methods 2007, 4, 437–444. [CrossRef][PubMed]
    • (2007) Nat. Methods , vol.4 , pp. 437-444
    • Chen, S.1    Laroche, T.2    Hamelinck, D.3    Bergsma, D.4    Brenner, D.5    Simeone, D.6    Brand, R.E.7    Haab, B.B.8
  • 81
    • 0025043537 scopus 로고
    • Studies on relationship between histology, tumor markers (Prostatic acid phosphatase.Prostate specific antigen. Gamma-seminoprotein.Leu-7) and clinical course in prostate cancer
    • [CrossRef]
    • Tanahashi, T.; Namba, K.; Murao, T. Studies on relationship between histology, tumor markers (prostatic acid phosphatase.prostate specific antigen.gamma-seminoprotein.leu-7) and clinical course in prostate cancer. Jpn. J. Urol. 1990, 81, 680–685. [CrossRef]
    • (1990) Jpn. J. Urol. , vol.81 , pp. 680-685
    • Tanahashi, T.1    Namba, K.2    Murao, T.3
  • 82
    • 58149397996 scopus 로고    scopus 로고
    • Altered glycosylation in tumours focused to cancer diagnosis
    • [CrossRef][PubMed]
    • Peracaula, R.; Barrabés, S.; Sarrats, A.; Rudd, P.M.; de Llorens, R. Altered glycosylation in tumours focused to cancer diagnosis. Dis. Markers 2008, 25, 207–218. [CrossRef][PubMed]
    • (2008) Dis. Markers , vol.25 , pp. 207-218
    • Peracaula, R.1    Barrabés, S.2    Sarrats, A.3    Rudd, P.M.4    De Llorens, R.5
  • 83
    • 77649115961 scopus 로고    scopus 로고
    • Differential protein expression on the cell surface of colorectal cancer cells associated to tumor metastasis
    • [PubMed]
    • Luque-Garcia, J.L.; Martinez-Torrecuadrada, J.L.; Epifano, C.; Canamero, M.; Babel, I.; Casal, J.I. Differential protein expression on the cell surface of colorectal cancer cells associated to tumor metastasis. Proteomics 2010, 10, 940–952. [PubMed]
    • (2010) Proteomics , vol.10 , pp. 940-952
    • Luque-Garcia, J.L.1    Martinez-Torrecuadrada, J.L.2    Epifano, C.3    Canamero, M.4    Babel, I.5    Casal, J.I.6
  • 84
    • 84875931748 scopus 로고    scopus 로고
    • Proteogenomic analysis of human colon carcinoma cell lines LIM1215, LIM1899, and LIM2405
    • [CrossRef][PubMed]
    • Fanayan, S.; Smith, J.T.; Lee, L.Y.; Yan, F.; Snyder, M.; Hancock, W.S.; Nice, E. Proteogenomic analysis of human colon carcinoma cell lines LIM1215, LIM1899, and LIM2405. J. Proteome Res. 2013, 12, 1732–1742. [CrossRef][PubMed]
    • (2013) J. Proteome Res. , vol.12 , pp. 1732-1742
    • Fanayan, S.1    Smith, J.T.2    Lee, L.Y.3    Yan, F.4    Snyder, M.5    Hancock, W.S.6    Nice, E.7
  • 85
    • 84899696230 scopus 로고    scopus 로고
    • Proteomic analysis reveals novel proteins associated with progression and differentiation of colorectal carcinoma
    • [PubMed]
    • Gan, Y.; Chen, D.; Li, X. Proteomic analysis reveals novel proteins associated with progression and differentiation of colorectal carcinoma. J. Cancer Res. Ther. 2014, 10, 89–96. [PubMed]
    • (2014) J. Cancer Res. Ther , vol.10 , pp. 89-96
    • Gan, Y.1    Chen, D.2    Li, X.3
  • 86
    • 84930965675 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of paired colorectal cancer and non-tumorigenic tissues reveals signature proteins and perturbed pathways involved in CRC progression and metastasis
    • [CrossRef][PubMed]
    • Sethi, M.K.; Thaysen-Andersen, M.; Kim, H.; Park, C.K.; Baker, M.S.; Packer, N.H.; Paik, Y.K.; Hancock, W.S.; Fanayan, S. Quantitative proteomic analysis of paired colorectal cancer and non-tumorigenic tissues reveals signature proteins and perturbed pathways involved in CRC progression and metastasis. J. Proteom. 2015, 126, 54–67. [CrossRef][PubMed]
    • (2015) J. Proteom , vol.126 , pp. 54-67
    • Sethi, M.K.1    Thaysen-Andersen, M.2    Kim, H.3    Park, C.K.4    Baker, M.S.5    Packer, N.H.6    Paik, Y.K.7    Hancock, W.S.8    Fanayan, S.9
  • 87
    • 84902215375 scopus 로고    scopus 로고
    • Advances in LC-MS/MS-based glycoproteomics: Getting closer to system-wide site-specific mapping of the N- and O-glycoproteome
    • [CrossRef][PubMed]
    • Thaysen-Andersen, M.; Packer, N.H. Advances in LC-MS/MS-based glycoproteomics: Getting closer to system-wide site-specific mapping of the N- and O-glycoproteome. Biochim. Biophys. Acta 2014, 1844, 1437–1452. [CrossRef][PubMed]
    • (2014) Biochim. Biophys. Acta , vol.1844 , pp. 1437-1452
    • Thaysen-Andersen, M.1    Packer, N.H.2
  • 88
    • 84862168794 scopus 로고    scopus 로고
    • Structural analysis of N- and O-glycans released from glycoproteins
    • [CrossRef][PubMed]
    • Jensen, P.H.; Karlsson, N.G.; Kolarich, D.; Packer, N.H. Structural analysis of N- and O-glycans released from glycoproteins. Nat. Protoc. 2012, 7, 1299–1310. [CrossRef][PubMed]
    • (2012) Nat. Protoc , vol.7 , pp. 1299-1310
    • Jensen, P.H.1    Karlsson, N.G.2    Kolarich, D.3    Packer, N.H.4
  • 89
    • 84903592013 scopus 로고    scopus 로고
    • Recent advances in mass spectrometry-based glycoproteomics
    • [PubMed]
    • Frost, D.C.; Li, L. Recent advances in mass spectrometry-based glycoproteomics. Adv. Protein Chem. Struct. Biol. 2014, 95, 71–123. [PubMed]
    • (2014) Adv. Protein Chem. Struct. Biol , vol.95 , pp. 71-123
    • Frost, D.C.1    Li, L.2
  • 90
    • 0026657798 scopus 로고
    • Differential glycosylation and cell surface expression of lysosomal membrane glycoproteins in sublines of a human colon cancer exhibiting distinct metastatic potentials
    • [PubMed]
    • Saitoh, O.; Wang, W.C.; Lotan, R.; Fukud, M. Differential glycosylation and cell surface expression of lysosomal membrane glycoproteins in sublines of a human colon cancer exhibiting distinct metastatic potentials. J. Biol. Chem. 1992, 267, 5700–5711. [PubMed]
    • (1992) J. Biol. Chem , vol.267 , pp. 5700-5711
    • Saitoh, O.1    Wang, W.C.2    Lotan, R.3    Fukud, M.4
  • 91
    • 0028990810 scopus 로고
    • Quantitative lectin-histochemical and immunohistochemical studies on the occurrence of alpha(2,3)- and alpha(2,6)-linked sialic acid residues in colorectal carcinomas. Relation to clinicopathologic features
    • [CrossRef]
    • Vierbuchen, M.J.; Fruechtnicht, W.; Brackrock, S.; Krause, K.T.; Zienkiewicz, T.J. Quantitative lectin-histochemical and immunohistochemical studies on the occurrence of alpha(2,3)- and alpha(2,6)-linked sialic acid residues in colorectal carcinomas. Relation to clinicopathologic features. Cancer 1995, 76, 727–735. [CrossRef]
    • (1995) Cancer , vol.76 , pp. 727-735
    • Vierbuchen, M.J.1    Fruechtnicht, W.2    Brackrock, S.3    Krause, K.T.4    Zienkiewicz, T.J.5
  • 94
    • 50449090546 scopus 로고    scopus 로고
    • Glycoproteomics and glycomics investigation of membrane N-glycosylproteins from human colon carcinoma cells
    • [CrossRef][PubMed]
    • Vercoutter-Edouart, A.S.; Slomianny, M.C.; Dekeyzer-Beseme, O.; Haeuw, J.F.; Michalsk, J.C. Glycoproteomics and glycomics investigation of membrane N-glycosylproteins from human colon carcinoma cells. Proteomics 2008, 8, 3236–3256. [CrossRef][PubMed]
    • (2008) Proteomics , vol.8 , pp. 3236-3256
    • Vercoutter-Edouart, A.S.1    Slomianny, M.C.2    Dekeyzer-Beseme, O.3    Haeuw, J.F.4    Michalsk, J.C.5
  • 95
    • 45549091249 scopus 로고    scopus 로고
    • Plasma glycoprotein profiling for colorectal cancer biomarker identification by lectin glycoarray and lectin blot
    • [CrossRef][PubMed]
    • Qiu, Y.; Patwa, T.H.; Xu, L.; Shedden, K.; Misek, D.E.; Tuck, M.; Jin, G.; Ruffin, M.T.; Turgeon, D.K.; Synal, S., et al. Plasma glycoprotein profiling for colorectal cancer biomarker identification by lectin glycoarray and lectin blot. J. Proteome Res. 2008, 7, 1693–1703. [CrossRef][PubMed]
    • (2008) J. Proteome Res , vol.7 , pp. 1693-1703
    • Qiu, Y.1    Patwa, T.H.2    Xu, L.3    Shedden, K.4    Misek, D.E.5    Tuck, M.6    Jin, G.7    Ruffin, M.T.8    Turgeon, D.K.9    Synal, S.10
  • 96
    • 84856218833 scopus 로고    scopus 로고
    • Identification and assessment of new biomarkers for colorectal cancer with serum N-glycan profiling
    • [CrossRef][PubMed]
    • Zhao, Y.P.; Ruan, C.P.; Wang, H.; Hu, Z.Q.; Fang, M.; Gu, X.; Ji, J.; Zhao, J.Y.; Gao, C.F. Identification and assessment of new biomarkers for colorectal cancer with serum N-glycan profiling. Cancer 2012, 118, 639–650. [CrossRef][PubMed]
    • (2012) Cancer , vol.118 , pp. 639-650
    • Zhao, Y.P.1    Ruan, C.P.2    Wang, H.3    Hu, Z.Q.4    Fang, M.5    Gu, X.6    Ji, J.7    Zhao, J.Y.8    Gao, C.F.9
  • 97
    • 84878520352 scopus 로고    scopus 로고
    • Associated expression of alpha2,3sialylated type 2 chain structures with lymph node metastasis in distal colorectal cancer
    • [CrossRef][PubMed]
    • Fukasawa, T.; Asao, T.; Yamauchi, H.; Ide, M.; Tabe, Y.; Fujii, T.; Yamaguchi, S.; Tsutsumi, S.; Yazawa, S.; Kuwano, H. Associated expression of alpha2,3sialylated type 2 chain structures with lymph node metastasis in distal colorectal cancer. Surg. Today 2013, 43, 155–162. [CrossRef][PubMed]
    • (2013) Surg. Today , vol.43 , pp. 155-162
    • Fukasawa, T.1    Asao, T.2    Yamauchi, H.3    Ide, M.4    Tabe, Y.5    Fujii, T.6    Yamaguchi, S.7    Tsutsumi, S.8    Yazawa, S.9    Kuwano, H.10
  • 98
    • 84901976686 scopus 로고    scopus 로고
    • Comprehensive glycomics comparison between colon cancer cell cultures and tumours: Implications for biomarker studies
    • [CrossRef][PubMed]
    • Chik, J.H.; Zhou, J.; Moh, E.S.; Christopherson, R.; Clarke, S.J.; Molloy, M.P.; Packer, N.H. Comprehensive glycomics comparison between colon cancer cell cultures and tumours: Implications for biomarker studies. J. Proteom. 2014, 108, 146–162. [CrossRef][PubMed]
    • (2014) J. Proteom , vol.108 , pp. 146-162
    • Chik, J.H.1    Zhou, J.2    Moh, E.S.3    Christopherson, R.4    Clarke, S.J.5    Molloy, M.P.6    Packer, N.H.7
  • 100
    • 0024336222 scopus 로고
    • Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases
    • [CrossRef]
    • Maley, F.; Trimble, R.B.; Tarentino, A.L.; Plummer, T.H., Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases. Anal. Biochem. 1989, 180, 195–204. [CrossRef]
    • (1989) Anal. Biochem , vol.180 , pp. 195-204
    • Maley, F.1    Trimble, R.B.2    Tarentino, A.L.3    Plummer, T.H.4
  • 101
    • 0025923253 scopus 로고
    • Peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F cannot release glycans with fucose attached alpha 1–3 to the asparagine-linked N-acetylglucosamine residue
    • [CrossRef][PubMed]
    • Tretter, V.; Altmann, F.; Marz, L. Peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F cannot release glycans with fucose attached alpha 1–3 to the asparagine-linked N-acetylglucosamine residue. Eur. J. Biochem. 1991, 199, 647–652. [CrossRef][PubMed]
    • (1991) Eur. J. Biochem , vol.199 , pp. 647-652
    • Tretter, V.1    Altmann, F.2    Marz, L.3
  • 102
    • 0030066709 scopus 로고    scopus 로고
    • Enzymatic release of oligosaccharides from glycoproteins for chromatographic and electrophoretic analysis
    • [CrossRef]
    • O’Neill, R.A. Enzymatic release of oligosaccharides from glycoproteins for chromatographic and electrophoretic analysis. J. Chromatogr. A 1996, 720, 201–215. [CrossRef]
    • (1996) J. Chromatogr. A , vol.720 , pp. 201-215
    • O’Neill, R.A.1
  • 103
    • 0036462597 scopus 로고    scopus 로고
    • Structural investigations of glycoconjugates at high sensitivity
    • [CrossRef][PubMed]
    • Mechref, Y.; Novotny, M.V. Structural investigations of glycoconjugates at high sensitivity. Chem. Rev. 2002, 102, 321–369. [CrossRef][PubMed]
    • (2002) Chem. Rev , vol.102 , pp. 321-369
    • Mechref, Y.1    Novotny, M.V.2
  • 104
    • 33845417633 scopus 로고    scopus 로고
    • Strategies for analysis of glycoprotein glycosylation
    • [CrossRef][PubMed]
    • Geyer, H.; Geyer, R. Strategies for analysis of glycoprotein glycosylation. Biochim. Biophys. Acta 2006, 1764, 1853–1869. [CrossRef][PubMed]
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 1853-1869
    • Geyer, H.1    Geyer, R.2
  • 105
    • 77956062358 scopus 로고    scopus 로고
    • Glycan labeling strategies and their use in identification and quantification
    • [CrossRef][PubMed]
    • Ruhaak, L.R.; Zauner, G.; Huhn, C.; Bruggink, C.; Deelder, A.M.; Wuhrer, M. Glycan labeling strategies and their use in identification and quantification. Anal. Bioanal. Chem. 2010, 397, 3457–3481. [CrossRef][PubMed]
    • (2010) Anal. Bioanal. Chem , vol.397 , pp. 3457-3481
    • Ruhaak, L.R.1    Zauner, G.2    Huhn, C.3    Bruggink, C.4    Deelder, A.M.5    Wuhrer, M.6
  • 106
    • 84907200792 scopus 로고    scopus 로고
    • Specific glycosylation of membrane proteins in epithelial ovarian cancer cell lines: Glycan structures reflect gene expression and DNA methylation status
    • [CrossRef][PubMed]
    • Anugraham, M.; Jacob, F.; Nixdorf, S.; Everest-Dass, A.V.; Heinzelmann-Schwarz, V.; Packer, N.H. Specific glycosylation of membrane proteins in epithelial ovarian cancer cell lines: Glycan structures reflect gene expression and DNA methylation status. Mol. Cell. Proteom. 2014, 13, 2213–2232. [CrossRef][PubMed]
    • (2014) Mol. Cell. Proteom , vol.13 , pp. 2213-2232
    • Anugraham, M.1    Jacob, F.2    Nixdorf, S.3    Everest-Dass, A.V.4    Heinzelmann-Schwarz, V.5    Packer, N.H.6
  • 107
    • 84908873236 scopus 로고    scopus 로고
    • Comprehensive N-glycome profiling of cultured human epithelial breast cells identifies unique secretome N-glycosylation signatures enabling tumorigenic subtype classification
    • [CrossRef][PubMed]
    • Lee, L.Y.; Thaysen-Andersen, M.; Baker, M.S.; Packer, N.H.; Hancock, W.S.; Fanayan, S. Comprehensive N-glycome profiling of cultured human epithelial breast cells identifies unique secretome N-glycosylation signatures enabling tumorigenic subtype classification. J. Proteome Res. 2014, 13, 4783–4795. [CrossRef][PubMed]
    • (2014) J. Proteome Res , vol.13 , pp. 4783-4795
    • Lee, L.Y.1    Thaysen-Andersen, M.2    Baker, M.S.3    Packer, N.H.4    Hancock, W.S.5    Fanayan, S.6
  • 109
    • 34447312516 scopus 로고    scopus 로고
    • Tools for glycomics: Relative quantitation of glycans by isotopic permethylation using 13CH3I
    • [CrossRef][PubMed]
    • Alvarez-Manilla, G.; Warren, N.L.; Abney, T.; Atwood, J., III; Azadi, P.; York, W.S.; Pierce, M.; Orlando, R. Tools for glycomics: Relative quantitation of glycans by isotopic permethylation using 13CH3I. Glycobiology 2007, 17, 677–687. [CrossRef][PubMed]
    • (2007) Glycobiology , vol.17 , pp. 677-687
    • Alvarez-Manilla, G.1    Warren, N.L.2    Abney, T.3    Atwood, J.4    Azadi, P.5    York, W.S.6    Pierce, M.7    Orlando, R.8
  • 110
    • 0029164230 scopus 로고
    • Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid
    • [CrossRef][PubMed]
    • Bigge, J.C.; Patel, T.P.; Bruce, J.A.; Goulding, P.N.; Charles, S.M.; Parekh, R.B. Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid. Anal. Biochem. 1995, 230, 229–238. [CrossRef][PubMed]
    • (1995) Anal. Biochem , vol.230 , pp. 229-238
    • Bigge, J.C.1    Patel, T.P.2    Bruce, J.A.3    Goulding, P.N.4    Charles, S.M.5    Parekh, R.B.6
  • 113
    • 26444476996 scopus 로고    scopus 로고
    • Protein glycosylation analysis by liquid chromatography-mass spectrometry
    • [CrossRef][PubMed]
    • Wuhrer, M.; Deelder, A.M.; Hokke, C.H. Protein glycosylation analysis by liquid chromatography-mass spectrometry. J. Chromatogr. B Anal. Technol. Biomed. Life Sci. 2005, 825, 124–133. [CrossRef][PubMed]
    • (2005) J. Chromatogr. B Anal. Technol. Biomed. Life Sci , vol.825 , pp. 124-133
    • Wuhrer, M.1    Deelder, A.M.2    Hokke, C.H.3
  • 114
    • 34748837881 scopus 로고    scopus 로고
    • Analysis of N-glycans from recombinant immunoglobulin G by on-line reversed-phase high-performance liquid chromatography/mass spectrometry
    • [CrossRef][PubMed]
    • Chen, X.; Flynn, G.C. Analysis of N-glycans from recombinant immunoglobulin G by on-line reversed-phase high-performance liquid chromatography/mass spectrometry. Anal. Biochem. 2007, 370, 147–161. [CrossRef][PubMed]
    • (2007) Anal. Biochem , vol.370 , pp. 147-161
    • Chen, X.1    Flynn, G.C.2
  • 115
    • 66149125257 scopus 로고    scopus 로고
    • Two-dimensional HPLC separation with reverse-phase-nano-LC-MS/MS for the characterization of glycan pools after labeling with 2-aminobenzamide
    • [PubMed]
    • Wuhrer, M.; Koeleman, C.A.; Deelder, A.M. Two-dimensional HPLC separation with reverse-phase-nano-LC-MS/MS for the characterization of glycan pools after labeling with 2-aminobenzamide. Methods Mol. Biol. 2009, 534, 79–91. [PubMed]
    • (2009) Methods Mol. Biol , vol.534 , pp. 79-91
    • Wuhrer, M.1    Koeleman, C.A.2    Deelder, A.M.3
  • 116
    • 0035100927 scopus 로고    scopus 로고
    • Liquid chromatography ion trap mass spectrometric analysis of oligosaccharides using permethylated derivatives
    • [CrossRef][PubMed]
    • Delaney, J.; Vouros, P. Liquid chromatography ion trap mass spectrometric analysis of oligosaccharides using permethylated derivatives. Rapid Commun. Mass Spectrom. 2001, 15, 325–334. [CrossRef][PubMed]
    • (2001) Rapid Commun. Mass Spectrom , vol.15 , pp. 325-334
    • Delaney, J.1    Vouros, P.2
  • 117
    • 33748471966 scopus 로고    scopus 로고
    • Hydrophilic interaction chromatography
    • [CrossRef][PubMed]
    • Hemstrom, P.; Irgum, K. Hydrophilic interaction chromatography. J. Sep. Sci. 2006, 29, 1784–1821. [CrossRef][PubMed]
    • (2006) J. Sep. Sci , vol.29 , pp. 1784-1821
    • Hemstrom, P.1    Irgum, K.2
  • 118
    • 53849145298 scopus 로고    scopus 로고
    • Mass spectrometry for proteomics
    • [CrossRef][PubMed]
    • Han, X.; Aslanian, A.; Yates, J.R., Mass spectrometry for proteomics. Curr. Opin. Chem. Biol. 2008, 12, 483–490. [CrossRef][PubMed]
    • (2008) Curr. Opin. Chem. Biol , vol.12 , pp. 483-490
    • Han, X.1    Aslanian, A.2    Yates, J.R.3
  • 119
    • 45949091084 scopus 로고    scopus 로고
    • Impact of column temperature and mobile phase components on selectivity of hydrophilic interaction chromatography (HILIC)
    • [CrossRef][PubMed]
    • Hao, Z.; Xiao, B.; Weng, N. Impact of column temperature and mobile phase components on selectivity of hydrophilic interaction chromatography (HILIC). J. Sep. Sci. 2008, 31, 1449–1464. [CrossRef][PubMed]
    • (2008) J. Sep. Sci. , vol.31 , pp. 1449-1464
    • Hao, Z.1    Xiao, B.2    Weng, N.3
  • 120
    • 84880292105 scopus 로고    scopus 로고
    • High-performance anion-exchange chromatography with pulsed amperometric detection for carbohydrate analysis of glycoproteins
    • [CrossRef][PubMed]
    • Rohrer, J.S.; Basumallick, L.; Hurum, D. High-performance anion-exchange chromatography with pulsed amperometric detection for carbohydrate analysis of glycoproteins. Biochemistry 2013, 78, 697–709. [CrossRef][PubMed]
    • (2013) Biochemistry , vol.78 , pp. 697-709
    • Rohrer, J.S.1    Basumallick, L.2    Hurum, D.3
  • 122
    • 0002953457 scopus 로고
    • Structure and performance of porous graphitic carbon in liquid chromatography
    • [CrossRef]
    • Knox, J.H.; Kaur, B.; Millward, G. Structure and performance of porous graphitic carbon in liquid chromatography. J. Chromatogr. A 1986, 352, 3–25. [CrossRef]
    • (1986) J. Chromatogr. A , vol.352 , pp. 3-25
    • Knox, J.H.1    Kaur, B.2    Millward, G.3
  • 123
    • 84925481642 scopus 로고    scopus 로고
    • Clinical Glycomics Employing Graphitized Carbon Liquid Chromatography—Mass Spectrometry
    • [CrossRef][PubMed]
    • Stavenhagen, K.; Kolarich, D.; Wuhrer, M. Clinical Glycomics Employing Graphitized Carbon Liquid Chromatography—Mass Spectrometry. Chromatographia 2014, 78, 307–320. [CrossRef][PubMed]
    • (2014) Chromatographia , vol.78 , pp. 307-320
    • Stavenhagen, K.1    Kolarich, D.2    Wuhrer, M.3
  • 124
    • 84856269227 scopus 로고    scopus 로고
    • Isomeric analysis of oligomannosidic N-glycans and their dolichol-linked precursors
    • [CrossRef][PubMed]
    • Pabst, M.; Grass, J.; Toegel, S.; Liebminger, E.; Strasser, R.; Altmann, F. Isomeric analysis of oligomannosidic N-glycans and their dolichol-linked precursors. Glycobiology 2012, 22, 389–399. [CrossRef][PubMed]
    • (2012) Glycobiology , vol.22 , pp. 389-399
    • Pabst, M.1    Grass, J.2    Toegel, S.3    Liebminger, E.4    Strasser, R.5    Altmann, F.6
  • 126
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • [CrossRef][PubMed]
    • Fenn, J.B.; Mann, M.; Meng, C.K.; Wong, S.F.; Whitehouse, C.M. Electrospray ionization for mass spectrometry of large biomolecules. Science 1989, 246, 64–71. [CrossRef][PubMed]
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 127
    • 24644477568 scopus 로고
    • Matrix-assisted ultraviolet laser desorption of non-volatile compounds
    • [CrossRef]
    • Karas, M.; Bachmann, D.; Bahr, U.; Hillenkamp, F. Matrix-assisted ultraviolet laser desorption of non-volatile compounds. Int. J. Mass Spectrom. Ion Process. 1987, 78, 53–68. [CrossRef]
    • (1987) Int. J. Mass Spectrom. Ion Process , vol.78 , pp. 53-68
    • Karas, M.1    Bachmann, D.2    Bahr, U.3    Hillenkamp, F.4
  • 128
    • 84984042980 scopus 로고
    • Protein and polymer analyses up to m/z 100 000 by laser ionization time-of-flight mass spectrometry
    • [CrossRef]
    • Tanaka, K.; Waki, H.; Ido, Y.; Akita, S.; Yoshida, Y.; Yoshida, T.; Matsuo, T. Protein and polymer analyses up to m/z 100 000 by laser ionization time-of-flight mass spectrometry. Rapid Commun. Mass Spectrom. 1988, 2, 151–153. [CrossRef]
    • (1988) Rapid Commun. Mass Spectrom , vol.2 , pp. 151-153
    • Tanaka, K.1    Waki, H.2    Ido, Y.3    Akita, S.4    Yoshida, Y.5    Yoshida, T.6    Matsuo, T.7
  • 129
    • 0000178042 scopus 로고
    • Micro-electrospray mass spectrometry: Ultra-high-sensitivity analysis of peptides and proteins
    • [CrossRef]
    • Emmett, M.R.; Caprioli, R.M. Micro-electrospray mass spectrometry: Ultra-high-sensitivity analysis of peptides and proteins. J. Am. Soc. Mass Spectrom. 1994, 5, 605–613. [CrossRef]
    • (1994) J. Am. Soc. Mass Spectrom , vol.5 , pp. 605-613
    • Emmett, M.R.1    Caprioli, R.M.2
  • 130
    • 0031962612 scopus 로고    scopus 로고
    • Mass spectrometry and the age of the proteome
    • [CrossRef]
    • Yates, J.R. Mass spectrometry and the age of the proteome. J. Mass Spectrom. 1998, 33, 1–19. [CrossRef]
    • (1998) J. Mass Spectrom , vol.33 , pp. 1-19
    • Yates, J.R.1
  • 131
    • 0025088325 scopus 로고
    • High-accuracy molecular mass determination of proteins using matrix-assisted laser desorption mass spectrometry
    • [CrossRef][PubMed]
    • Beavis, R.C.; Chait, B.T. High-accuracy molecular mass determination of proteins using matrix-assisted laser desorption mass spectrometry. Anal. Chem. 1990, 62, 1836–1840. [CrossRef][PubMed]
    • (1990) Anal. Chem , vol.62 , pp. 1836-1840
    • Beavis, R.C.1    Chait, B.T.2
  • 132
    • 44649169019 scopus 로고    scopus 로고
    • Improved repeatability and matrix-assisted desorption/ionization—Time of flight mass spectrometry compatibility in capillary isoelectric focusing
    • [CrossRef][PubMed]
    • Silvertand, L.H.; Torano, J.S.; de Jong, G.J.; van Bennekom, W.P. Improved repeatability and matrix-assisted desorption/ionization—Time of flight mass spectrometry compatibility in capillary isoelectric focusing. Electrophoresis 2008, 29, 1985–1996. [CrossRef][PubMed]
    • (2008) Electrophoresis , vol.29 , pp. 1985-1996
    • Silvertand, L.H.1    Torano, J.S.2    De Jong, G.J.3    Van Bennekom, W.P.4
  • 133
    • 26844536197 scopus 로고    scopus 로고
    • Simple and robust two-layer matrix/sample preparation method for MALDI MS/MS analysis of peptides
    • [CrossRef][PubMed]
    • Zheng, J.; Li, N.; Ridyard, M.; Dai, H.; Robbins, S.M.; Li, L. Simple and robust two-layer matrix/sample preparation method for MALDI MS/MS analysis of peptides. J. Proteome Res. 2005, 4, 1709–1716. [CrossRef][PubMed]
    • (2005) J. Proteome Res , vol.4 , pp. 1709-1716
    • Zheng, J.1    Li, N.2    Ridyard, M.3    Dai, H.4    Robbins, S.M.5    Li, L.6
  • 134
    • 51649085326 scopus 로고    scopus 로고
    • Mass spectrometry and the emerging field of glycomics
    • [CrossRef][PubMed]
    • Zaia, J. Mass spectrometry and the emerging field of glycomics. Chem. Biol. 2008, 15, 881–892. [CrossRef][PubMed]
    • (2008) Chem. Biol , vol.15 , pp. 881-892
    • Zaia, J.1
  • 135
    • 84880311546 scopus 로고    scopus 로고
    • Mass spectrometry of glycans
    • [CrossRef][PubMed]
    • Han, L.; Costello, C.E. Mass spectrometry of glycans. Biochemistry 2013, 78, 710–720. [CrossRef][PubMed]
    • (2013) Biochemistry , vol.78 , pp. 710-720
    • Han, L.1    Costello, C.E.2
  • 136
    • 0024206786 scopus 로고
    • A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates
    • [CrossRef]
    • Domon, B.; Costello, C.E. A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates. Glycoconjug. J. 1988, 5, 397–409. [CrossRef]
    • (1988) Glycoconjug. J , vol.5 , pp. 397-409
    • Domon, B.1    Costello, C.E.2
  • 137
    • 84859396316 scopus 로고    scopus 로고
    • Effective use of mass spectrometry for glycan and glycopeptide structural analysis
    • [CrossRef][PubMed]
    • Leymarie, N.; Zaia, J. Effective use of mass spectrometry for glycan and glycopeptide structural analysis. Anal. Chem. 2012, 84, 3040–3048. [CrossRef][PubMed]
    • (2012) Anal. Chem. , vol.84 , pp. 3040-3048
    • Leymarie, N.1    Zaia, J.2
  • 138
    • 34548681626 scopus 로고    scopus 로고
    • A glycomics platform for the analysis of permethylated oligosaccharide alditols
    • [CrossRef][PubMed]
    • Costello, C.E.; Contado-Miller, J.M.; Cipollo, J.F. A glycomics platform for the analysis of permethylated oligosaccharide alditols. J. Am. Soc. Mass Spectrom. 2007, 18, 1799–1812. [CrossRef][PubMed]
    • (2007) J. Am. Soc. Mass Spectrom , vol.18 , pp. 1799-1812
    • Costello, C.E.1    Contado-Miller, J.M.2    Cipollo, J.F.3
  • 139
    • 66149089569 scopus 로고    scopus 로고
    • Solid-phase permethylation for glycomic analysis
    • [PubMed]
    • Mechref, Y.; Kang, P.; Novotny, M.V. Solid-phase permethylation for glycomic analysis. Methods Mol. Biol. 2009, 534, 53–64. [PubMed]
    • (2009) Methods Mol. Biol , vol.534 , pp. 53-64
    • Mechref, Y.1    Kang, P.2    Novotny, M.V.3
  • 140
    • 14344254313 scopus 로고    scopus 로고
    • Fragmentation of negative ions from carbohydrates: Part 3. Fragmentation of hybrid and complex N-linked glycans
    • [CrossRef][PubMed]
    • Harvey, D.J. Fragmentation of negative ions from carbohydrates: part 3. fragmentation of hybrid and complex N-linked glycans. J. Am. Soc. Mass Spectrom. 2005, 16, 631–646. [CrossRef][PubMed]
    • (2005) J. Am. Soc. Mass Spectrom , vol.16 , pp. 631-646
    • Harvey, D.J.1
  • 141
    • 74049114658 scopus 로고    scopus 로고
    • Quantitative glycomics
    • Springer: Berlin, Germany
    • Orlando, R. Quantitative glycomics. In Functional Glycomics; Springer: Berlin, Germany, 2010; pp. 31–49.
    • (2010) Functional Glycomics , pp. 31-49
    • Orlando, R.1
  • 143
    • 84928032463 scopus 로고    scopus 로고
    • Relative vs absolute quantitation in disease glycomics
    • [CrossRef][PubMed]
    • Moh, E.S.; Thaysen-Andersen, M.; Packer, N.H. Relative vs absolute quantitation in disease glycomics. Proteom. Clin. Appl. 2015, 9, 368–382. [CrossRef][PubMed]
    • (2015) Proteom. Clin. Appl , vol.9 , pp. 368-382
    • Moh, E.S.1    Thaysen-Andersen, M.2    Packer, N.H.3
  • 144
    • 16344380985 scopus 로고    scopus 로고
    • Automatic annotation of matrix-assisted laser desorption/ionization N-glycan spectra
    • [CrossRef][PubMed]
    • Goldberg, D.; Sutton-Smith, M.; Paulson, J.; Dell, A. Automatic annotation of matrix-assisted laser desorption/ionization N-glycan spectra. Proteomics 2005, 5, 865–875. [CrossRef][PubMed]
    • (2005) Proteomics , vol.5 , pp. 865-875
    • Goldberg, D.1    Sutton-Smith, M.2    Paulson, J.3    Dell, A.4
  • 145
    • 84949839586 scopus 로고    scopus 로고
    • GlycoWorkbench
    • GlycoWorkbench. Available online: http://www.eurocarbdb.org/applications/ms-tools (accessed on 15 August 2015).
  • 146
    • 45549094069 scopus 로고    scopus 로고
    • GlycoWorkbench: A tool for the computer-assisted annotation of mass spectra of glycans
    • [CrossRef][PubMed]
    • Ceroni, A.; Maass, K.; Geyer, H.; Geyer, R.; Dell, A.; Haslam, S.M. GlycoWorkbench: A tool for the computer-assisted annotation of mass spectra of glycans. J. Proteome Res. 2008, 7, 1650–1659. [CrossRef][PubMed]
    • (2008) J. Proteome Res , vol.7 , pp. 1650-1659
    • Ceroni, A.1    Maass, K.2    Geyer, H.3    Geyer, R.4    Dell, A.5    Haslam, S.M.6
  • 147
    • 84949839587 scopus 로고    scopus 로고
    • GlycoMod
    • GlycoMod. Available online: http://www.expasy.ch/tools/glycomod (accessed on 20 May 2015).
  • 148
    • 0035261661 scopus 로고    scopus 로고
    • GlycoMod—A software tool for determining glycosylation compositions from mass spectrometric data
    • [CrossRef]
    • Cooper, C.A.; Gasteiger, E.; Packer, N.H. GlycoMod—A software tool for determining glycosylation compositions from mass spectrometric data. Proteomics 2001, 1, 340–349. [CrossRef]
    • (2001) Proteomics , vol.1 , pp. 340-349
    • Cooper, C.A.1    Gasteiger, E.2    Packer, N.H.3
  • 149
    • 84949839588 scopus 로고    scopus 로고
    • UnicarbKB, accessed on 4 April 2015
    • UnicarbKB. Available online: http://www.unicarbkb.org/ (accessed on 4 April 2015).
  • 150
    • 84949839589 scopus 로고    scopus 로고
    • UnicarbDB, accessed on 4 April2015
    • UnicarbDB. Available online: http://www.unicarb-db.org (accessed on 4 April2015).
  • 154
    • 62549156308 scopus 로고    scopus 로고
    • The Potentials of Glycomics in Biomarker Discovery
    • [CrossRef]
    • Kam, R.K.; Poon, T.C. The Potentials of Glycomics in Biomarker Discovery. Clin. Proteom. 2008, 4, 67–79. [CrossRef]
    • (2008) Clin. Proteom , vol.4 , pp. 67-79
    • Kam, R.K.1    Poon, T.C.2
  • 155
    • 84946415785 scopus 로고    scopus 로고
    • Sugars Interfere or Glycomics in the Field of Cancer Biomarkers
    • [CrossRef]
    • Zahradnikova, M.; Vojtesek, B.; Hernychova, L. Sugars Interfere or Glycomics in the Field of Cancer Biomarkers. Klin. Onkol. 2015, 28, S20–S25. [CrossRef]
    • (2015) Klin. Onkol , vol.28 , pp. S20-S25
    • Zahradnikova, M.1    Vojtesek, B.2    Hernychova, L.3
  • 156
    • 84922011987 scopus 로고    scopus 로고
    • Neutrophil extracellular traps in cancer progression
    • [CrossRef][PubMed]
    • Cools-Lartigue, J.; Spicer, J.; Najmeh, S.; Ferri, L. Neutrophil extracellular traps in cancer progression. Cell. Mol. Life Sci. 2014, 71, 4179–4194. [CrossRef][PubMed]
    • (2014) Cell. Mol. Life Sci , vol.71 , pp. 4179-4194
    • Cools-Lartigue, J.1    Spicer, J.2    Najmeh, S.3    Ferri, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.