메뉴 건너뛰기




Volumn 33, Issue 3, 2016, Pages 405-415

Comparison of analytical methods for profiling N- and O-linked glycans from cultured cell lines: HUPO Human Disease Glycomics/Proteome Initiative multi-institutional study

(31)  Ito, Hiromi a,n   Kaji, Hiroyuki a   Togayachi, Akira a   Azadi, Parastoo b   Ishihara, Mayumi b   Geyer, Rudolf c   Galuska, Christina c   Geyer, Hildegard c   Kakehi, Kazuaki d   Kinoshita, Mitsuhiro d   Karlsson, Niclas G e   Jin, Chunsheng e   Kato, Koichi f   Yagi, Hirokazu f   Kondo, Sachiko f   Kawasaki, Nana g,o   Hashii, Noritaka g   Kolarich, Daniel h   Stavenhagen, Kathrin h,p   Packer, Nicolle H i   more..


Author keywords

Glycoproteomics; Human disease glycomics proteome initiative (HGPI); Human proteome organization (HUPO)

Indexed keywords

ALDITOL; FUCOSE; GLYCOPEPTIDE; GLYCOPROTEIN; IMMUNOGLOBULIN G; N LINKED GLYCAN; O LINKED GLYCAN; SIALIC ACID; SIALYL LEWIS X ANTIGEN; TRANSFERRIN; UNCLASSIFIED DRUG; BIOLOGICAL MARKER; POLYSACCHARIDE;

EID: 84975780471     PISSN: 02820080     EISSN: 15734986     Source Type: Journal    
DOI: 10.1007/s10719-015-9625-3     Document Type: Article
Times cited : (24)

References (26)
  • 1
    • 84975742483 scopus 로고    scopus 로고
    • D., Policy issues for the development and use of biomarkers in health
    • Development, O. for E.C. and, Co-operation, O.E., Oecd, D.: Policy issues for the development and use of biomarkers in health. (2011)
    • (2011) for E.C. and, Co-operation, O.E., Oecd
    • Development, O.1
  • 2
    • 0030745147 scopus 로고    scopus 로고
    • Perspectives on the significance of altered glycosylation of glycoproteins in cancer
    • COI: 1:CAS:528:DyaK2sXlslOhtbg%3D, PID: 9298689
    • Kim, Y.J., Varki, A.: Perspectives on the significance of altered glycosylation of glycoproteins in cancer. Glycoconj. J. 14, 569–576 (1997)
    • (1997) Glycoconj. J. , vol.14 , pp. 569-576
    • Kim, Y.J.1    Varki, A.2
  • 3
    • 84901004695 scopus 로고    scopus 로고
    • Sweet and sour: the impact of differential glycosylation in cancer cells undergoing epithelial-mesenchymal transition
    • PID: 24724053
    • Freire-de-Lima, L.: Sweet and sour: the impact of differential glycosylation in cancer cells undergoing epithelial-mesenchymal transition. Front. Oncol. 4, 59 (2014)
    • (2014) Front. Oncol. , vol.4 , pp. 59
    • Freire-de-Lima, L.1
  • 4
    • 84860222212 scopus 로고    scopus 로고
    • Golgi pH, its regulation and roles in human disease
    • COI: 1:CAS:528:DC%2BC38Xht1yht7bF, PID: 21585247
    • Rivinoja, A., Pujol, F.M., Hassinen, A., Kellokumpu, S.: Golgi pH, its regulation and roles in human disease. Ann. Med. 44, 542–554 (2012)
    • (2012) Ann. Med. , vol.44 , pp. 542-554
    • Rivinoja, A.1    Pujol, F.M.2    Hassinen, A.3    Kellokumpu, S.4
  • 8
    • 84864108807 scopus 로고    scopus 로고
    • Transcriptional regulation of the protocadherin beta cluster during Her-2 protein-induced mammary tumorigenesis results from altered N-glycan branching
    • COI: 1:CAS:528:DC%2BC38XhtVGnt73K, PID: 22665489
    • Guo, H., Nairn, A., dela Rosa, M., Nagy, T., Zhao, S., Moremen, K., Pierce, M.: Transcriptional regulation of the protocadherin beta cluster during Her-2 protein-induced mammary tumorigenesis results from altered N-glycan branching. J. Biol. Chem 287, 24941–24954 (2012)
    • (2012) J. Biol. Chem , vol.287 , pp. 24941-24954
    • Guo, H.1    Nairn, A.2    dela Rosa, M.3    Nagy, T.4    Zhao, S.5    Moremen, K.6    Pierce, M.7
  • 9
    • 84864106579 scopus 로고    scopus 로고
    • Proteomic identification of glycosylphosphatidylinositol anchor-dependent membrane proteins elevated in breast carcinoma
    • COI: 1:CAS:528:DC%2BC38XhtVGnt7jM, PID: 22654114
    • Zhao, P., Nairn, A.V., Hester, S., Moremen, K.W., O’Regan, R.M., Oprea, G., Wells, L., Pierce, M., Abbott, K.L.: Proteomic identification of glycosylphosphatidylinositol anchor-dependent membrane proteins elevated in breast carcinoma. J. Biol. Chem. 287, 25230–25240 (2012)
    • (2012) J. Biol. Chem. , vol.287 , pp. 25230-25240
    • Zhao, P.1    Nairn, A.V.2    Hester, S.3    Moremen, K.W.4    O’Regan, R.M.5    Oprea, G.6    Wells, L.7    Pierce, M.8    Abbott, K.L.9
  • 12
    • 85016373908 scopus 로고    scopus 로고
    • Development and application of multidimensional HPLC mapping method for O-linked oligosaccharides
    • COI: 1:CAS:528:DC%2BC38Xlt1Chsrc%3D, PID: 24970123
    • Yagi, H., Ohno, E., Kondo, S., Yoshida, A., Kato, K.: Development and application of multidimensional HPLC mapping method for O-linked oligosaccharides. Biomolecules. 1, 48–62 (2011)
    • (2011) Biomolecules. , vol.1 , pp. 48-62
    • Yagi, H.1    Ohno, E.2    Kondo, S.3    Yoshida, A.4    Kato, K.5
  • 13
    • 0142134975 scopus 로고    scopus 로고
    • GALAXY (Glycoanalysis by the Three Axes of MS and Chromatography): a web application that assists structural analyses of N-Glycans
    • COI: 1:CAS:528:DC%2BD3sXosF2mtLg%3D
    • Takahashi, N., Kato, K.: GALAXY (Glycoanalysis by the Three Axes of MS and Chromatography): a web application that assists structural analyses of N-Glycans. Trends. Glycosci. Glycotechnol. 15, 235–251 (2003)
    • (2003) Trends. Glycosci. Glycotechnol. , vol.15 , pp. 235-251
    • Takahashi, N.1    Kato, K.2
  • 14
    • 34447343820 scopus 로고    scopus 로고
    • Mass + retention time = structure: a strategy for the analysis of N-glycans by carbon LC-ESI-MS and its application to fibrin N-glycans
    • COI: 1:CAS:528:DC%2BD2sXlvFSnsb8%3D, PID: 17539604
    • Pabst, M., Bondili, J.S., Stadlmann, J., Mach, L., Altmann, F.: Mass + retention time = structure: a strategy for the analysis of N-glycans by carbon LC-ESI-MS and its application to fibrin N-glycans. Anal. Chem. 79, 5051–5057 (2007)
    • (2007) Anal. Chem. , vol.79 , pp. 5051-5057
    • Pabst, M.1    Bondili, J.S.2    Stadlmann, J.3    Mach, L.4    Altmann, F.5
  • 15
    • 84862168794 scopus 로고    scopus 로고
    • Structural analysis of N- and O-glycans released from glycoproteins
    • COI: 1:CAS:528:DC%2BC38Xot1CgtLk%3D, PID: 22678433
    • Jensen, P.H., Karlsson, N.G., Kolarich, D., Packer, N.H.: Structural analysis of N- and O-glycans released from glycoproteins. Nat. Protoc. 7, 1299–1310 (2012)
    • (2012) Nat. Protoc. , vol.7 , pp. 1299-1310
    • Jensen, P.H.1    Karlsson, N.G.2    Kolarich, D.3    Packer, N.H.4
  • 17
    • 54749113731 scopus 로고    scopus 로고
    • Influence of electrosorption, solvent, temperature, and ion polarity on the performance of LC-ESI-MS using graphitic carbon for acidic oligosaccharides
    • COI: 1:CAS:528:DC%2BD1cXhtVOqt7vF, PID: 18778038
    • Pabst, M., Altmann, F.: Influence of electrosorption, solvent, temperature, and ion polarity on the performance of LC-ESI-MS using graphitic carbon for acidic oligosaccharides. Anal. Chem. 80, 7534–7542 (2008)
    • (2008) Anal. Chem. , vol.80 , pp. 7534-7542
    • Pabst, M.1    Altmann, F.2
  • 18
    • 0037051978 scopus 로고    scopus 로고
    • Abnormal glycosylation and altered Golgi structure in colorectal cancer: dependence on intra-Golgi pH
    • COI: 1:CAS:528:DC%2BD38XivVaitbw%3D, PID: 11959136
    • Kellokumpu, S., Sormunen, R., Kellokumpu, I.: Abnormal glycosylation and altered Golgi structure in colorectal cancer: dependence on intra-Golgi pH. FEBS Lett. 516, 217–224 (2002)
    • (2002) FEBS Lett. , vol.516 , pp. 217-224
    • Kellokumpu, S.1    Sormunen, R.2    Kellokumpu, I.3
  • 20
    • 84876005928 scopus 로고    scopus 로고
    • The minimum information required for a glycomics experiment (MIRAGE) project: improving the standards for reporting mass-spectrometry-based glycoanalytic data
    • COI: 1:CAS:528:DC%2BC3sXmt12ntrs%3D, PID: 23378518
    • Kolarich, D., Rapp, E., Struwe, W.B., Haslam, S.M., Zaia, J., McBride, R., Agravat, S., Campbell, M.P., Kato, M., Ranzinger, R., Kettner, C., York, W.S.: The minimum information required for a glycomics experiment (MIRAGE) project: improving the standards for reporting mass-spectrometry-based glycoanalytic data. Mol. Cell. Proteomics 12, 991–995 (2013)
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 991-995
    • Kolarich, D.1    Rapp, E.2    Struwe, W.B.3    Haslam, S.M.4    Zaia, J.5    McBride, R.6    Agravat, S.7    Campbell, M.P.8    Kato, M.9    Ranzinger, R.10    Kettner, C.11    York, W.S.12
  • 23
    • 84983656017 scopus 로고    scopus 로고
    • Comparison of methods for the analysis of therapeutic immunoglobulin G Fc-glycosylation profiles-Part 2: mass spectrometric methods
    • COI: 1:CAS:528:DC%2BC28XmvFyrurc%3D, PID: 25996192
    • Reusch, D., Haberger, M., Falck, D., Peter, B., Maier, B., Gassner, J., Hook, M., Wagner, K., Bonnington, L., Bulau, P., Wuhrer, M.: Comparison of methods for the analysis of therapeutic immunoglobulin G Fc-glycosylation profiles-Part 2: mass spectrometric methods. MAbs 7, 732–742 (2015)
    • (2015) MAbs , vol.7 , pp. 732-742
    • Reusch, D.1    Haberger, M.2    Falck, D.3    Peter, B.4    Maier, B.5    Gassner, J.6    Hook, M.7    Wagner, K.8    Bonnington, L.9    Bulau, P.10    Wuhrer, M.11
  • 24
    • 55149085231 scopus 로고    scopus 로고
    • Comparison of LC and LC/MS methods for quantifying N-glycosylation in recombinant IgGs
    • COI: 1:CAS:528:DC%2BD1cXhtlOhtLfE, PID: 18707900
    • Sinha, S., Pipes, G., Topp, E.M., Bondarenko, P.V., Treuheit, M.J., Gadgil, H.S.: Comparison of LC and LC/MS methods for quantifying N-glycosylation in recombinant IgGs. J. Am. Soc. Mass Spectrom. 19, 1643–1654 (2008)
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 1643-1654
    • Sinha, S.1    Pipes, G.2    Topp, E.M.3    Bondarenko, P.V.4    Treuheit, M.J.5    Gadgil, H.S.6
  • 25
    • 77956931053 scopus 로고    scopus 로고
    • A systematic approach to protein glycosylation analysis: a path through the maze
    • PID: 20852609
    • Mariño, K., Bones, J., Kattla, J.J., Rudd, P.M.: A systematic approach to protein glycosylation analysis: a path through the maze. Nat. Chem. Biol. 6, 713–723 (2010)
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 713-723
    • Mariño, K.1    Bones, J.2    Kattla, J.J.3    Rudd, P.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.