메뉴 건너뛰기




Volumn 1850, Issue 1, 2015, Pages 33-42

Advances in mass spectrometry driven O-glycoproteomics

Author keywords

ETD; Glycopeptide; Lectin; Orbitrap; SimpleCell; Site specific

Indexed keywords

GLYCAN; GLYCOPEPTIDE; GLYCOSIDASE; N ACETYLGALACTOSAMINE; PROTEOME; TRANSFERASE; TYROSINE; GLYCOPROTEIN; POLYSACCHARIDE;

EID: 84908277532     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2014.09.026     Document Type: Review
Times cited : (101)

References (93)
  • 2
    • 0042266719 scopus 로고    scopus 로고
    • A genetic approach to mammalian glycan function
    • J.B. Lowe, J.D. Marth, A genetic approach to mammalian glycan function, Annu. Rev. Biochem. 72 (2003) 643-691.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 643-691
    • Lowe, J.B.1    Marth, J.D.2
  • 4
    • 84867426941 scopus 로고    scopus 로고
    • Site-speci fic protein O-glycosylation modulates proprotein processing - deciphering speci fic functions of the large polypeptide GalNAc-transferase gene family
    • K.T. Schjoldager, H. Clausen, Site-speci fic protein O-glycosylation modulates proprotein processing - deciphering speci fic functions of the large polypeptide GalNAc-transferase gene family, Biochim. Biophys. Acta 1820 (2012) 2079-2094.
    • (2012) Biochim. Biophys. Acta , vol.1820 , pp. 2079-2094
    • Schjoldager, K.T.1    Clausen, H.2
  • 5
    • 78449258533 scopus 로고    scopus 로고
    • O-glycosylationmodulates proprotein convertase activation of angiopoietin-like protein 3: Possible role of polypeptide GalNAc-transferase-2 in regulation of concentrations of plasma lipids
    • K.T. Schjoldager, M.B. Vester-Christensen, E.P. Bennett, S.B. Levery, T. Schwientek, W. Yin, O. Blixt, H. Clausen, O-glycosylationmodulates proprotein convertase activation of angiopoietin-like protein 3: possible role of polypeptide GalNAc-transferase-2 in regulation of concentrations of plasma lipids, J. Biol. Chem. 285 (2010) 36293-36303.
    • (2010) J. Biol. Chem. , vol.285 , pp. 36293-36303
    • Schjoldager, K.T.1    Vester-Christensen, M.B.2    Bennett, E.P.3    Levery, S.B.4    Schwientek, T.5    Yin, W.6    Blixt, O.7    Clausen, H.8
  • 8
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • R. Kornfeld, S. Kornfeld, Assembly of asparagine-linked oligosaccharides, Annu. Rev. Biochem. 54 (1985) 631-664.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 9
    • 34247583996 scopus 로고    scopus 로고
    • Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins
    • G.W. Hart, M.P. Housley, C. Slawson, Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins, Nature 446 (2007) 1017-1022.
    • (2007) Nature , vol.446 , pp. 1017-1022
    • Hart, G.W.1    Housley, M.P.2    Slawson, C.3
  • 10
    • 84860365843 scopus 로고    scopus 로고
    • Control of mucin-type O-glycosylation: A classification of the polypeptide GalNAc-transferase gene family
    • E.P. Bennett, U. Mandel, H. Clausen, T.A. Gerken, T.A. Fritz, L.A. Tabak, Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family, Glycobiology 22 (2012) 736-756.
    • (2012) Glycobiology , vol.22 , pp. 736-756
    • Bennett, E.P.1    Mandel, U.2    Clausen, H.3    Gerken, T.A.4    Fritz, T.A.5    Tabak, L.A.6
  • 11
    • 79952106660 scopus 로고    scopus 로고
    • Location, location, location: New insights into O-GalNAc protein glycosylation
    • D.J. Gill, H. Clausen, F. Bard, Location, location, location: new insights into O-GalNAc protein glycosylation, Trends Cell Biol. 21 (2011) 149-158.
    • (2011) Trends Cell Biol. , vol.21 , pp. 149-158
    • Gill, D.J.1    Clausen, H.2    Bard, F.3
  • 12
    • 73649139554 scopus 로고    scopus 로고
    • Mucin-type O-glycosylation-putting the pieces together
    • P.H. Jensen, D. Kolarich, N.H. Packer, Mucin-type O-glycosylation-putting the pieces together, FEBS J. 277 (2010) 81-94.
    • (2010) FEBS J. , vol.277 , pp. 81-94
    • Jensen, P.H.1    Kolarich, D.2    Packer, N.H.3
  • 13
    • 84902215375 scopus 로고    scopus 로고
    • Advances in LC-MS/MS-based glycoproteomics: Getting closer to system-wide site-specificmapping of the N- and O-glycoproteome
    • M. Thaysen-Andersen, N.H. Packer, Advances in LC-MS/MS-based glycoproteomics: getting closer to system-wide site-specificmapping of the N- and O-glycoproteome, Biochim. Biophys. Acta 1844 (2014) 1437-1452.
    • (2014) Biochim. Biophys. Acta , vol.1844 , pp. 1437-1452
    • Thaysen-Andersen, M.1    Packer, N.H.2
  • 15
    • 0030066709 scopus 로고    scopus 로고
    • Enzymatic release of oligosaccharides from glycoproteins for chromatographic and electrophoretic analysis
    • R.A. O'Neill, Enzymatic release of oligosaccharides from glycoproteins for chromatographic and electrophoretic analysis, J. Chromatogr. A 720 (1996) 201-215.
    • (1996) J. Chromatogr. A , vol.720 , pp. 201-215
    • O'Neill, R.A.1
  • 16
    • 0035282989 scopus 로고    scopus 로고
    • Glycoprotein identifi cation and localization of O-glycosylation sites by mass spectrometric analysis of deglycosylated/alkylaminylated peptide fragments
    • F.G. Hanisch, M. Jovanovic, J. Peter-Katalinic, Glycoprotein identifi cation and localization of O-glycosylation sites by mass spectrometric analysis of deglycosylated/alkylaminylated peptide fragments, Anal. Biochem. 290 (2001) 47-59.
    • (2001) Anal. Biochem. , vol.290 , pp. 47-59
    • Hanisch, F.G.1    Jovanovic, M.2    Peter-Katalinic, J.3
  • 18
    • 0001607910 scopus 로고    scopus 로고
    • Mapping sites of O-GlcNAc modi fi cation using af fi nity tags for serine and threonine post-translational modi fi cations
    • L. Wells, K. Vosseller, R.N. Cole, J.M. Cronshaw, M.J. Matunis, G.W. Hart, Mapping sites of O-GlcNAc modi fi cation using af fi nity tags for serine and threonine post-translational modi fi cations, Mol. Cell. Proteomics 1 (2002) 791-804.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 791-804
    • Wells, L.1    Vosseller, K.2    Cole, R.N.3    Cronshaw, J.M.4    Matunis, M.J.5    Hart, G.W.6
  • 20
    • 33749041103 scopus 로고    scopus 로고
    • Mass spectrometric analysis of N- and Oglycosylation of tissues and cells
    • S.M. Haslam, S.J. North, A. Dell, Mass spectrometric analysis of N- and Oglycosylation of tissues and cells, Curr. Opin. Struct. Biol. 16 (2006) 584-591.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 584-591
    • Haslam, S.M.1    North, S.J.2    Dell, A.3
  • 21
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • D.F. Zielinska, F. Gnad, J.R.Wisniewski, M. Mann, Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints, Cell 141 (2010) 897-907.
    • (2010) Cell , vol.141 , pp. 897-907
    • Zielinska, D.F.1    Gnad, F.2    Wisniewski, J.R.3    Mann, M.4
  • 23
    • 84859862380 scopus 로고    scopus 로고
    • Human urinary glycoproteomics; attachment site specific analysis of N- and O-linked glycosylations by CID and ECD
    • A. Halim, J. Nilsson, U. Ruetschi, C. Hesse, G. Larson, Human urinary glycoproteomics; attachment site specific analysis of N- and O-linked glycosylations by CID and ECD, Mol. Cell. Proteomics 11 (2012) M111 (013649).
    • (2012) Mol. Cell. Proteomics , vol.11
    • Halim, A.1    Nilsson, J.2    Ruetschi, U.3    Hesse, C.4    Larson, G.5
  • 24
    • 0033214591 scopus 로고    scopus 로고
    • Localization of labile posttranslational modifi cations by electron capture dissociation: The case of gamma-carboxyglutamic acid
    • N.L. Kelleher, R.A. Zubarev, K. Bush, B. Furie, B.C. Furie, F.W. McLafferty, C.T. Walsh, Localization of labile posttranslational modifi cations by electron capture dissociation: the case of gamma-carboxyglutamic acid, Anal. Chem. 71 (1999) 4250-4253.
    • (1999) Anal. Chem. , vol.71 , pp. 4250-4253
    • Kelleher, N.L.1    Zubarev, R.A.2    Bush, K.3    Furie, B.4    Furie, B.C.5    McLafferty, F.W.6    Walsh, C.T.7
  • 25
    • 0032731855 scopus 로고    scopus 로고
    • Localization of O-glycosylation sites in peptides by electron capture dissociation in a Fourier transform mass spectrometer
    • E. Mirgorodskaya, P. Roepstorff, R.A. Zubarev, Localization of O-glycosylation sites in peptides by electron capture dissociation in a Fourier transform mass spectrometer, Anal. Chem. 71 (1999) 4431-4436.
    • (1999) Anal. Chem. , vol.71 , pp. 4431-4436
    • Mirgorodskaya, E.1    Roepstorff, P.2    Zubarev, R.A.3
  • 27
    • 55849104839 scopus 로고    scopus 로고
    • Application of electron transfer dissociation (ETD) for the analysis of posttranslational modi fications
    • J. Wiesner, T. Premsler, A. Sickmann, Application of electron transfer dissociation (ETD) for the analysis of posttranslational modi fications, Proteomics 8 (2008) 4466-4483.
    • (2008) Proteomics , vol.8 , pp. 4466-4483
    • Wiesner, J.1    Premsler, T.2    Sickmann, A.3
  • 29
    • 84877780038 scopus 로고    scopus 로고
    • Principles of electron capture and transfer dissociation mass spectrometry applied to peptide and protein structure analysis
    • K.O. Zhurov, L. Fornelli, M.D.Wodrich, U.A. Laskay, Y.O. Tsybin, Principles of electron capture and transfer dissociation mass spectrometry applied to peptide and protein structure analysis, Chem. Soc. Rev. 42 (2013) 5014-5030.
    • (2013) Chem. Soc. Rev. , vol.42 , pp. 5014-5030
    • Zhurov, K.O.1    Fornelli, L.2    Wodrich, M.D.3    Laskay, U.A.4    Tsybin, Y.O.5
  • 30
    • 84868123896 scopus 로고    scopus 로고
    • Use of CID/ETD mass spectrometry to analyze glycopeptides
    • Y. Mechref, Use of CID/ETD mass spectrometry to analyze glycopeptides, Curr. Protoc. Protein Sci. 68 (2012) 12.11.1-12.11.11.
    • (2012) Curr. Protoc. Protein Sci. , vol.68 , pp. 12.11.1-12.11.11
    • Mechref, Y.1
  • 32
    • 67049158217 scopus 로고    scopus 로고
    • Identification of protein O-GlcNAcylation sites using electron transfer dissociation mass spectrometry on native peptides
    • R.J. Chalkley, A. Thalhammer, R. Schoepfer, A.L. Burlingame, Identification of protein O-GlcNAcylation sites using electron transfer dissociation mass spectrometry on native peptides, Proc. Natl. Acad. Sci. U. S. A. 106 (2009) 8894-8899.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 8894-8899
    • Chalkley, R.J.1    Thalhammer, A.2    Schoepfer, R.3    Burlingame, A.L.4
  • 34
    • 84867186895 scopus 로고    scopus 로고
    • Discovery of O-GlcNAc-6-phosphate modifi ed proteins in large-scale phosphoproteomics data
    • H. Hahne, B. Kuster, Discovery of O-GlcNAc-6-phosphate modifi ed proteins in large-scale phosphoproteomics data, Mol. Cell. Proteomics 11 (2012) 1063-1069.
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 1063-1069
    • Hahne, H.1    Kuster, B.2
  • 35
    • 72149102185 scopus 로고    scopus 로고
    • Affinity enrichment and characterization of mucin core-1 type glycopeptides from bovine serum
    • Z. Darula, K.F. Medzihradszky, Affinity enrichment and characterization of mucin core-1 type glycopeptides from bovine serum, Mol. Cell. Proteomics 8 (2009) 2515-2526.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2515-2526
    • Darula, Z.1    Medzihradszky, K.F.2
  • 36
    • 56149086397 scopus 로고    scopus 로고
    • Decision tree-driven tandem mass spectrometry for shotgun proteomics
    • D.L. Swaney, G.C.McAlister, J.J. Coon, Decision tree-driven tandem mass spectrometry for shotgun proteomics, Nat. Methods 5 (2008) 959-964.
    • (2008) Nat. Methods , vol.5 , pp. 959-964
    • Swaney, D.L.1    McAlister, G.C.2    Coon, J.J.3
  • 38
    • 0015239274 scopus 로고
    • Studies on the chemical and enzymatic modification of glycoproteins. A general method for the tritiation of sialic acid-containing glycoproteins
    • L. Van Lenten, G. Ashwell, Studies on the chemical and enzymatic modification of glycoproteins. A general method for the tritiation of sialic acid-containing glycoproteins, J. Biol. Chem. 246 (1971) 1889-1894.
    • (1971) J. Biol. Chem. , vol.246 , pp. 1889-1894
    • Van Lenten, L.1    Ashwell, G.2
  • 39
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • H. Zhang, X.J. Li, D.B. Martin, R. Aebersold, Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry, Nat. Biotechnol. 21 (2003) 660-666.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 660-666
    • Zhang, H.1    Li, X.J.2    Martin, D.B.3    Aebersold, R.4
  • 40
    • 0026698693 scopus 로고
    • A method for determination of N-glycosylation sites in glycoproteins by collision-induced dissociation analysis in fast atom bombardment mass spectrometry: Identification of the positions of carbohydrate-linked asparagine in recombinant alpha-amylase by treatment with peptide-N-glycosidase F in 18O-labeled water
    • J. Gonzalez, T. Takao, H. Hori, V. Besada, R. Rodriguez, G. Padron, Y. Shimonishi, A method for determination of N-glycosylation sites in glycoproteins by collision-induced dissociation analysis in fast atom bombardment mass spectrometry: identification of the positions of carbohydrate-linked asparagine in recombinant alpha-amylase by treatment with peptide-N-glycosidase F in 18O-labeled water, Anal. Biochem. 205 (1992) 151-158.
    • (1992) Anal. Biochem. , vol.205 , pp. 151-158
    • Gonzalez, J.1    Takao, T.2    Hori, H.3    Besada, V.4    Rodriguez, R.5    Padron, G.6    Shimonishi, Y.7
  • 41
    • 84857873715 scopus 로고    scopus 로고
    • Chemical deamidation: A common pitfall in large-scale N-linked glycoproteomic mass spectrometry-based analyses
    • G. Palmisano, M.N. Melo-Braga, K. Engholm-Keller, B.L. Parker, M.R. Larsen, Chemical deamidation: a common pitfall in large-scale N-linked glycoproteomic mass spectrometry-based analyses, J. Proteome Res. 11 (2012) 1949-1957.
    • (2012) J. Proteome Res. , vol.11 , pp. 1949-1957
    • Palmisano, G.1    Melo-Braga, M.N.2    Engholm-Keller, K.3    Parker, B.L.4    Larsen, M.R.5
  • 43
    • 84864629154 scopus 로고    scopus 로고
    • Determination of deamidation artifacts introduced by sample preparation using 18O-labeling and tandem mass spectrometry analysis
    • Y. Du, F. Wang, K. May, W. Xu, H. Liu, Determination of deamidation artifacts introduced by sample preparation using 18O-labeling and tandem mass spectrometry analysis, Anal. Chem. 84 (2012) 6355-6360.
    • (2012) Anal. Chem. , vol.84 , pp. 6355-6360
    • Du, Y.1    Wang, F.2    May, K.3    Xu, W.4    Liu, H.5
  • 44
    • 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
    • V. Tretter, F. Altmann, L. Marz, 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. 199 (1991) 647-652.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 647-652
    • Tretter, V.1    Altmann, F.2    Marz, L.3
  • 45
    • 9344265921 scopus 로고
    • Removal of sialic acid from serum gonadotropin by acidic and enzymic hydrolysis
    • M.E. Rafelson Jr., H. Clauser, J. Legault-Demare, Removal of sialic acid from serum gonadotropin by acidic and enzymic hydrolysis, Biochim. Biophys. Acta 47 (1961) 406-407.
    • (1961) Biochim. Biophys. Acta , vol.47 , pp. 406-407
    • Rafelson, M.E.1    Clauser, H.2    Legault-Demare, J.3
  • 47
    • 0015859264 scopus 로고
    • External labeling of cell surface galactose and galactosamine in glycolipid and glycoprotein of human erythrocytes
    • C.G. Gahmberg, S.I. Hakomori, External labeling of cell surface galactose and galactosamine in glycolipid and glycoprotein of human erythrocytes, J. Biol. Chem. 248 (1973) 4311-4317.
    • (1973) J. Biol. Chem. , vol.248 , pp. 4311-4317
    • Gahmberg, C.G.1    Hakomori, S.I.2
  • 48
    • 84871954135 scopus 로고    scopus 로고
    • Glycoproteomics enabled by tagging sialic acid- or galactose-terminated glycans
    • T.N. Ramya, E. Weerapana, B.F. Cravatt, J.C. Paulson, Glycoproteomics enabled by tagging sialic acid- or galactose-terminated glycans, Glycobiology 23 (2013) 211-221.
    • (2013) Glycobiology , vol.23 , pp. 211-221
    • Ramya, T.N.1    Weerapana, E.2    Cravatt, B.F.3    Paulson, J.C.4
  • 50
    • 0345598906 scopus 로고    scopus 로고
    • A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation
    • H.C. Hang, C. Yu, D.L. Kato, C.R. Bertozzi, A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation, Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 14846-14851.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 14846-14851
    • Hang, H.C.1    Yu, C.2    Kato, D.L.3    Bertozzi, C.R.4
  • 52
    • 0345868573 scopus 로고    scopus 로고
    • Probing glycosyltransferase activities with the Staudinger ligation
    • H.C. Hang, C. Yu, M.R. Pratt, C.R. Bertozzi, Probing glycosyltransferase activities with the Staudinger ligation, J. Am. Chem. Soc. 126 (2004) 6-7.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 6-7
    • Hang, H.C.1    Yu, C.2    Pratt, M.R.3    Bertozzi, C.R.4
  • 55
    • 35649011957 scopus 로고    scopus 로고
    • Exploring the sialiome using titanium dioxide chromatography and mass spectrometry
    • M.R. Larsen, S.S. Jensen, L.A. Jakobsen, N.H. Heegaard, Exploring the sialiome using titanium dioxide chromatography and mass spectrometry, Mol. Cell. Proteomics 6 (2007) 1778-1787.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1778-1787
    • Larsen, M.R.1    Jensen, S.S.2    Jakobsen, L.A.3    Heegaard, N.H.4
  • 56
    • 78649961364 scopus 로고    scopus 로고
    • Selective enrichment of sialic acid-containing glycopeptides using titanium dioxide chromatography with analysis by HILIC and mass spectrometry
    • G. Palmisano, S.E. Lendal, K. Engholm-Keller, R. Leth-Larsen, B.L. Parker, M.R. Larsen, Selective enrichment of sialic acid-containing glycopeptides using titanium dioxide chromatography with analysis by HILIC and mass spectrometry, Nat. Protoc. 5 (2010) 1974-1982.
    • (2010) Nat. Protoc. , vol.5 , pp. 1974-1982
    • Palmisano, G.1    Lendal, S.E.2    Engholm-Keller, K.3    Leth-Larsen, R.4    Parker, B.L.5    Larsen, M.R.6
  • 58
    • 84863789621 scopus 로고    scopus 로고
    • How to dig deeper? Improved enrichment methods for mucin core-1 type glycopeptides
    • Z. Darula, J. Sherman, K.F. Medzihradszky, How to dig deeper? Improved enrichment methods for mucin core-1 type glycopeptides, Mol. Cell. Proteomics 11 (2012) O111 (016774).
    • (2012) Mol. Cell. Proteomics , vol.11
    • Darula, Z.1    Sherman, J.2    Medzihradszky, K.F.3
  • 59
    • 84867280662 scopus 로고    scopus 로고
    • Detection and analysis of proteins modified by O-linked N-acetylglucosamine
    • 95: II: 17.6: 17.6.1-17.6.33
    • N.E. Zachara, K. Vosseller, G.W. Hart, Detection and analysis of proteins modified by O-linked N-acetylglucosamine, Curr. Protoc. Protein Sci. (2011) (95: II: 17.6: 17.6.1-17.6.33).
    • (2011) Curr. Protoc. Protein Sci.
    • Zachara, N.E.1    Vosseller, K.2    Hart, G.W.3
  • 64
    • 84878653784 scopus 로고    scopus 로고
    • Glycoengineering of human cell lines using zinc finger nuclease gene targeting: SimpleCells with homogeneous GalNAc O-glycosylation allow isolation of the O-glycoproteome by one-step lectin affinity chromatography
    • C. Steentoft, E.P. Bennett, H. Clausen, Glycoengineering of human cell lines using zinc finger nuclease gene targeting: SimpleCells with homogeneous GalNAc O-glycosylation allow isolation of the O-glycoproteome by one-step lectin affinity chromatography, Methods Mol. Biol. 1022 (2013) 387-402.
    • (2013) Methods Mol. Biol. , vol.1022 , pp. 387-402
    • Steentoft, C.1    Bennett, E.P.2    Clausen, H.3
  • 69
    • 79954612783 scopus 로고    scopus 로고
    • Emerging paradigms for the initiation of mucin-type protein O-glycosylation by the polypeptide GalNAc transferase family of glycosyltransferases
    • T.A. Gerken, O. Jamison, C.L. Perrine, J.C. Collette, H.Moinova, L. Ravi, S.D. Markowitz, W. Shen, H. Patel, L.A. Tabak, Emerging paradigms for the initiation of mucin-type protein O-glycosylation by the polypeptide GalNAc transferase family of glycosyltransferases, J. Biol. Chem. 286 (2011) 14493-14507.
    • (2011) J. Biol. Chem. , vol.286 , pp. 14493-14507
    • Gerken, T.A.1    Jamison, O.2    Perrine, C.L.3    Collette, J.C.4    Moinova, H.5    Ravi, L.6    Markowitz, S.D.7    Shen, W.8    Patel, H.9    Tabak, L.A.10
  • 72
    • 66649090939 scopus 로고    scopus 로고
    • Ablation of the Galnt3 gene leads to low-circulating intact fibroblast growth factor 23 (Fgf23) concentrations and hyperphosphatemia despite increased Fgf23 expression
    • S. Ichikawa, A.H. Sorenson, A.M. Austin, D.S. Mackenzie, T.A. Fritz, A. Moh, S.L. Hui, M.J. Econs, Ablation of the Galnt3 gene leads to low-circulating intact fibroblast growth factor 23 (Fgf23) concentrations and hyperphosphatemia despite increased Fgf23 expression, Endocrinology 150 (2009) 2543-2550.
    • (2009) Endocrinology , vol.150 , pp. 2543-2550
    • Ichikawa, S.1    Sorenson, A.H.2    Austin, A.M.3    Mackenzie, D.S.4    Fritz, T.A.5    Moh, A.6    Hui, S.L.7    Econs, M.J.8
  • 73
    • 77955279149 scopus 로고    scopus 로고
    • The role of mucin-type O-glycans in eukaryotic development
    • L.A. Tabak, The role of mucin-type O-glycans in eukaryotic development, Semin. Cell Dev. Biol. 21 (2010) 616-621.
    • (2010) Semin. Cell Dev. Biol. , vol.21 , pp. 616-621
    • Tabak, L.A.1
  • 76
    • 84901036287 scopus 로고    scopus 로고
    • Mammalian O-mannosylation pathway: Glycan structures, enzymes, and protein substrates
    • J.L. Praissman, L. Wells, Mammalian O-mannosylation pathway: glycan structures, enzymes, and protein substrates, Biochemistry 53 (2014) 3066-3078.
    • (2014) Biochemistry , vol.53 , pp. 3066-3078
    • Praissman, J.L.1    Wells, L.2
  • 77
    • 0018801488 scopus 로고
    • Novel mannitol-containing oligosaccharides obtained by mild alkaline borohydride treatment of a chondroitin sulfate proteoglycan from brain
    • J. Finne, T. Krusius, R.K. Margolis, R.U.Margolis, Novel mannitol-containing oligosaccharides obtained by mild alkaline borohydride treatment of a chondroitin sulfate proteoglycan from brain, J. Biol. Chem. 254 (1979) 10295-10300.
    • (1979) J. Biol. Chem. , vol.254 , pp. 10295-10300
    • Finne, J.1    Krusius, T.2    Margolis, R.K.3    Margolis, R.U.4
  • 78
    • 0031026624 scopus 로고    scopus 로고
    • Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve alpha-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of alpha-dystroglycan with laminin
    • A. Chiba, K. Matsumura, H. Yamada, T. Inazu, T. Shimizu, S. Kusunoki, I. Kanazawa, A. Kobata, T. Endo, Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve alpha-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of alpha-dystroglycan with laminin, J. Biol. Chem. 272 (1997) 2156-2162.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2156-2162
    • Chiba, A.1    Matsumura, K.2    Yamada, H.3    Inazu, T.4    Shimizu, T.5    Kusunoki, S.6    Kanazawa, I.7    Kobata, A.8    Endo, T.9
  • 80
    • 77955440095 scopus 로고    scopus 로고
    • Characterization of site-specific O-glycan structures within the mucin-like domain of alpha-dystroglycan from human skeletal muscle
    • J. Nilsson, J. Nilsson, G. Larson, A. Grahn, Characterization of site-specific O-glycan structures within the mucin-like domain of alpha-dystroglycan from human skeletal muscle, Glycobiology 20 (2010) 1160-1169.
    • (2010) Glycobiology , vol.20 , pp. 1160-1169
    • Nilsson, J.1    Nilsson, J.2    Larson, G.3    Grahn, A.4
  • 83
    • 34250639054 scopus 로고    scopus 로고
    • Characterization of a novel modification on IgG2 light chain. Evidence for the presence of O-linked mannosylation
    • T. Martinez, D. Pace, L. Brady, M. Gerhart, A. Balland, Characterization of a novel modification on IgG2 light chain. Evidence for the presence of O-linked mannosylation, J. Chromatogr. A 1156 (2007) 183-187.
    • (2007) J. Chromatogr. A , vol.1156 , pp. 183-187
    • Martinez, T.1    Pace, D.2    Brady, L.3    Gerhart, M.4    Balland, A.5
  • 84
    • 57749114758 scopus 로고    scopus 로고
    • Receptor tyrosine phosphatase beta (RPTPbeta) activity and signaling are attenuated by glycosylation and subsequent cell surface galectin-1 binding
    • K.L. Abbott, R.T. Matthews, M. Pierce, Receptor tyrosine phosphatase beta (RPTPbeta) activity and signaling are attenuated by glycosylation and subsequent cell surface galectin-1 binding, J. Biol. Chem. 283 (2008) 33026-33035.
    • (2008) J. Biol. Chem. , vol.283 , pp. 33026-33035
    • Abbott, K.L.1    Matthews, R.T.2    Pierce, M.3
  • 86
    • 84864578742 scopus 로고    scopus 로고
    • Neurofascin 186 is O-mannosylated within and outside of the mucin domain
    • S. Pacharra, F.G. Hanisch, I. Breloy, Neurofascin 186 is O-mannosylated within and outside of the mucin domain, J. Proteome Res. 11 (2012) 3955-3964.
    • (2012) J. Proteome Res. , vol.11 , pp. 3955-3964
    • Pacharra, S.1    Hanisch, F.G.2    Breloy, I.3
  • 90
    • 32244440192 scopus 로고    scopus 로고
    • Dystroglycan: Frombiosynthesis to pathogenesis of human disease
    • R. Barresi, K.P. Campbell, Dystroglycan: frombiosynthesis to pathogenesis of human disease, J. Cell Sci. 119 (2006) 199-207.
    • (2006) J. Cell Sci. , vol.119 , pp. 199-207
    • Barresi, R.1    Campbell, K.P.2
  • 91
    • 84855515852 scopus 로고    scopus 로고
    • Dystroglycan function requires xylosyl- and glucuronyltransferase activities of LARGE
    • K. Inamori, T. Yoshida-Moriguchi, Y. Hara, M.E. Anderson, L. Yu, K.P. Campbell, Dystroglycan function requires xylosyl- and glucuronyltransferase activities of LARGE, Science 335 (2012) 93-96.
    • (2012) Science , vol.335 , pp. 93-96
    • Inamori, K.1    Yoshida-Moriguchi, T.2    Hara, Y.3    Anderson, M.E.4    Yu, L.5    Campbell, K.P.6
  • 92
    • 84874883376 scopus 로고    scopus 로고
    • The o-mannosylation pathway: Glycosyltransferases and proteins implicated in congenital muscular dystrophy
    • L.Wells, The o-mannosylation pathway: glycosyltransferases and proteins implicated in congenital muscular dystrophy, J. Biol. Chem. 288 (2013) 6930-6935.
    • (2013) J. Biol. Chem. , vol.288 , pp. 6930-6935
    • Wells, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.