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Volumn 11, Issue 1, 2014, Pages

O-GlcNAc profiling: From proteins to proteomes

Author keywords

Enrichment; Mass spectrometry; O GlcNAc; O GlcNAcome; O GlcNAcomics; Proteomics; Quantification; Site mapping

Indexed keywords

GLUCOSAMINE DERIVATIVE; LECTIN; O LINKED BETA DEXTRO N ACETYLGLUCOSAMINE; UNCLASSIFIED DRUG;

EID: 84903767444     PISSN: 15426416     EISSN: 15590275     Source Type: Journal    
DOI: 10.1186/1559-0275-11-8     Document Type: Review
Times cited : (224)

References (142)
  • 1
    • 77954142985 scopus 로고    scopus 로고
    • Evolution of glycan diversity
    • 2nd edition. Edited by Varki A, Cummings RD, Esko JD, Freeze HH, Stanley P, Bertozzi CR, Hart GW, Etzler ME. Cold Spring Harbor NY, USA: Cold Spring Harbor Laboratory Press
    • Varki A, Freeze HH, Gagneux P: Evolution of Glycan Diversity. In Essentials of Glycobiology. 2nd edition. Edited by Varki A, Cummings RD, Esko JD, Freeze HH, Stanley P, Bertozzi CR, Hart GW, Etzler ME. Cold Spring Harbor NY, USA: Cold Spring Harbor Laboratory Press; 2009.
    • (2009) Essentials of Glycobiology
    • Varki, A.1    Freeze, H.H.2    Gagneux, P.3
  • 2
    • 79251489778 scopus 로고    scopus 로고
    • Glycomics hits the big time
    • Hart GW, Copeland RJ: Glycomics hits the big time. Cell 2010, 143:672-676.
    • (2010) Cell , vol.143 , pp. 672-676
    • Hart, G.W.1    Copeland, R.J.2
  • 3
    • 0021280147 scopus 로고
    • Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc
    • Torres CR, Hart GW: Topography and polypeptide distribution of terminal N-Acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc. J Biol Chem 1984, 259:3308-3317. (Pubitemid 14130544)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.5 , pp. 3308-3317
    • Torres, C.-R.1    Hart, G.W.2
  • 4
    • 0023037076 scopus 로고
    • The subcellular distribution of terminal N-acetylglucosamine moieties. Localization of a novel protein-saccharidie linkage, O-linked GlcNAc
    • Holt GD, Hart GW: The subcellular distribution of terminal Nacetylglucosamine moieties. Localization of a novel protein-saccharide linkage, O-linked GlcNAc. J Biol Chem 1986, 261:8049-8057. (Pubitemid 17208742)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.17 , pp. 8049-8057
    • Holt, G.D.1    Hart, G.W.2
  • 5
    • 58649095123 scopus 로고    scopus 로고
    • Increased enzymatic O-GlcNAcylation of mitochondrial proteins impairs mitochondrial function in cardiac myocytes exposed to high glucose
    • Hu Y, Suarez J, Fricovsky E, Wang H, Scott BT, Trauger SA, Han W, Hu Y, Oyeleye MO, Dillmann WH: Increased enzymatic O-GlcNAcylation of mitochondrial proteins impairs mitochondrial function in cardiac myocytes exposed to high glucose. J Biol Chem 2009, 284:547-555.
    • (2009) J Biol Chem , vol.284 , pp. 547-555
    • Hu, Y.1    Suarez, J.2    Fricovsky, E.3    Wang, H.4    Scott, B.T.5    Trauger, S.A.6    Han, W.7    Hu, Y.8    Oyeleye, M.O.9    Dillmann, W.H.10
  • 6
    • 0025193520 scopus 로고
    • Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins Identification of a uridine diphospho-nacetylglucosamine: Peptide beta-N-Acetyl-glucosaminyltransferase
    • Haltiwanger RS, Holt GD, Hart GW: Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins. Identification of a uridine diphospho-Nacetylglucosamine: peptide beta-N-Acetyl-glucosaminyltransferase. J Biol Chem 1990, 265:2563-2568.
    • (1990) J Biol Chem , vol.265 , pp. 2563-2568
    • Haltiwanger, R.S.1    Holt, G.D.2    Hart, G.W.3
  • 9
    • 0028085881 scopus 로고
    • Purification and characterization of an O-GlcNAc selective N -Acetyl-ß-d-glucosaminidase from rat spleen cytosol
    • Dong DL, Hart GW: Purification and characterization of an O-GlcNAc selective N-Acetyl-ß-D-glucosaminidase from rat spleen cytosol. J Biol Chem 1994, 269:19321-19330.
    • (1994) J Biol Chem , vol.269 , pp. 19321-19330
    • Dong, D.L.1    Hart, G.W.2
  • 10
    • 77953138098 scopus 로고    scopus 로고
    • Site-specific interplay between O- GlcNAcylation and phosphorylation in cellular regulation
    • Hu P, Shimoji S, Hart GW: Site-specific interplay between O-GlcNAcylation and phosphorylation in cellular regulation. FEBS Lett 2010, 584:2526-2538.
    • (2010) FEBS Lett , vol.584 , pp. 2526-2538
    • Hu, P.1    Shimoji, S.2    Hart, G.W.3
  • 11
    • 77949769388 scopus 로고    scopus 로고
    • O-linked N-Acetylglucosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress
    • Butkinaree C, Park K, Hart GW: O-linked N-Acetylglucosamine (O-GlcNAc): extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress. Biochem Biophys Acta 2010, 2010(1800):96-106.
    • (2010) Biochem Biophys Acta 2010 , Issue.1800 , pp. 96-106
    • Butkinaree, C.1    Park, K.2    Hart, G.W.3
  • 12
    • 72449187655 scopus 로고    scopus 로고
    • The intersections between O-GlcNAcylation and phosphorylation: Implications for multiple signaling pathways
    • Zeidan Q, Hart GW: The intersections between O-GlcNAcylation and phosphorylation: implications for multiple signaling pathways. J Cell Sci 2010, 123:13-22.
    • (2010) J Cell Sci , vol.123 , pp. 13-22
    • Zeidan, Q.1    Hart, G.W.2
  • 13
    • 79959381299 scopus 로고    scopus 로고
    • Cross talk between GlcNAcylation and phosphorylation: Roles in signaling, transcription, and chronic disease
    • Hart GW, Slawson C, Ramirez-Correa GA, Lagerlof O: Cross talk between GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease. Annu Rev Biochem 2011, 80:825-858.
    • (2011) Annu Rev Biochem , vol.80 , pp. 825-858
    • Hart, G.W.1    Slawson, C.2    Ramirez-Correa, G.A.3    Lagerlof, O.4
  • 14
    • 84880648662 scopus 로고    scopus 로고
    • O-GlcNAc cycling: A link between metabolism and chronic disease
    • Bond MB, Hanover JA: O-GlcNAc Cycling: A link between metabolism and chronic disease. Annu Rev Nutr 2013, 33:131-1325.
    • (2013) Annu Rev Nutr , vol.33 , pp. 131-1325
    • Bond, M.B.1    Hanover, J.A.2
  • 16
    • 84883053156 scopus 로고    scopus 로고
    • Dynamic O-GlcNAcylation and its roles in the cellular stress response and homeostasis
    • Groves JA, Lee A, Yildirir G, Zachara NE: Dynamic O-GlcNAcylation and its roles in the cellular stress response and homeostasis. Cell Stress Chaperone 2013, 18:535-558.
    • (2013) Cell Stress Chaperone , vol.18 , pp. 535-558
    • Groves, J.A.1    Lee, A.2    Yildirir, G.3    Zachara, N.E.4
  • 17
    • 0025855139 scopus 로고
    • Discovery of a metabolic pathway mediating glucose-induced desensitization of the glucose transport system: Role of hexosamine biosynthesis in the induction of insulin resistance
    • Marshall S, Bacote V, Traxinger RR: Discovery of a metabolic pathway mediating glucose-induced desensitization of the glucose transport system. Role of hexosamine biosynthesis in the induction of insulin resistance. J Biol Chem 1991, 266:4706-4712. (Pubitemid 21909414)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.8 , pp. 4706-4712
    • Marshall, S.1    Bacote, V.2    Traxinger, R.R.3
  • 18
    • 78649990012 scopus 로고    scopus 로고
    • O-GlcNAc modification, insulin signaling and diabetic complications
    • Issad T, Masson E, Pagesy P: O-GlcNAc modification, insulin signaling and diabetic complications. Diabetes Metab 2010, 36:423-435.
    • (2010) Diabetes Metab , vol.36 , pp. 423-435
    • Issad, T.1    Masson, E.2    Pagesy, P.3
  • 19
    • 84894029904 scopus 로고    scopus 로고
    • Protein O-GlcNAcylation in diabetes and diabetic complications
    • Ma J, Hart GW: Protein O-GlcNAcylation in diabetes and diabetic complications. Expert Rev Proteomics 2013, 10:365-380.
    • (2013) Expert Rev Proteomics , vol.10 , pp. 365-380
    • Ma, J.1    Hart, G.W.2
  • 20
    • 80052068559 scopus 로고    scopus 로고
    • O-GlcNAc signalling: Implications for cancer cell biology
    • Slawson C, Hart GW: O-GlcNAc signalling: implications for cancer cell biology. Nat Rev Cancer 2011, 11:678-684.
    • (2011) Nat Rev Cancer , vol.11 , pp. 678-684
    • Slawson, C.1    Hart, G.W.2
  • 21
    • 84885315910 scopus 로고    scopus 로고
    • O-GlcNAc in cancer biology
    • doi:10.1007/s00726-013-1543-8
    • Ma Z, Vosseller K: O-GlcNAc in cancer biology. Amino Acids 2013, 45:719- 733. doi:10.1007/s00726-013-1543-8.
    • (2013) Amino Acids , vol.45 , pp. 719-733
    • Ma, Z.1    Vosseller, K.2
  • 22
    • 84884310305 scopus 로고    scopus 로고
    • O-GlcNAcylation: A new cancer hallmark?
    • doi:10.3389/fendo.2013.00099
    • Fardini Y, Dehennaut V, Lefebvre T, et al: O-GlcNAcylation: A new cancer hallmark? Front Endocrinol 2013. doi:10.3389/fendo.2013.00099. http://www.frontiersin.org/Journal/10.3389/fendo.2013.00099/full.
    • (2013) Front Endocrinol
    • Fardini, Y.1    Dehennaut, V.2    Lefebvre, T.3
  • 23
    • 70349270677 scopus 로고    scopus 로고
    • O-GlcNAc cycling: Implications for neurodegenerative disorders
    • Lazarus BD, Love DC, Hanover JA: O-GlcNAc cycling: implications for Neurodegenerative disorders. Int J Biochem Cell Biol 2009, 41:2134-2146.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 2134-2146
    • Lazarus, B.D.1    Love, D.C.2    Hanover, J.A.3
  • 24
    • 84867903851 scopus 로고    scopus 로고
    • O-GlcNAc cycling modulates neuro degeneration
    • Gong C, Liu F, Iqbal K: O-GlcNAc cycling modulates neurodegeneration. Proc Natl Acad Sci USA 2012, 109:17319-17320.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 17319-17320
    • Gong, C.1    Liu, F.2    Iqbal, K.3
  • 25
    • 33751019949 scopus 로고    scopus 로고
    • Identification of O-GlcNAc Sites on Proteins
    • DOI 10.1016/S0076-6879(06)15008-9, PII S0076687906150089, Glycobiology
    • Whelan SA, Hart GW: Identification of O-GlcNAc sites on proteins. Methods Enzymol 2006, 415:113-133. (Pubitemid 44751094)
    • (2006) Methods in Enzymology , vol.415 , pp. 113-133
    • Whelan, S.A.1    Hart, G.W.2
  • 26
    • 62549123339 scopus 로고    scopus 로고
    • Glycomic approaches to study GlcNAcylation: Protein identification, site-mapping, and site-specific O-GlcNAc quantitation
    • Wang Z, Hart GW: Glycomic approaches to study GlcNAcylation: protein identification, site-mapping, and site-specific O-GlcNAc quantitation. Clin Proteomics 2008, 4:5-13.
    • (2008) Clin Proteomics , vol.4 , pp. 5-13
    • Wang, Z.1    Hart, G.W.2
  • 27
    • 84861325047 scopus 로고    scopus 로고
    • O-GlcNAc proteomics: Mass spectrometric analysis of O-GlcNAc modifications on proteins
    • edited by Julian Whitelegge
    • Chalkley RJ, Wells L, Vosseller K: O-GlcNAc proteomics: mass spectrometric analysis of O-GlcNAc modifications on proteins. In Protein Mass Spectrometry (edited by Julian Whitelegge) 2009, 52:353-374.
    • (2009) Protein Mass Spectrometry , vol.52 , pp. 353-374
    • Chalkley, R.J.1    Wells, L.2    Vosseller, K.3
  • 28
    • 66149128841 scopus 로고    scopus 로고
    • Detecting the " O-GlcNAc-ome "; detection, purification, and analysis of O-GlcNAc modified proteins
    • Zachara NE: Detecting the "O-GlcNAc-ome"; detection, purification, and analysis of O-GlcNAc modified proteins. Methods Mol Biol 2009, 534:251- 279.
    • (2009) Methods Mol Biol , vol.534 , pp. 251-279
    • Zachara, N.E.1
  • 29
    • 84867280662 scopus 로고    scopus 로고
    • Detection and analysis of proteins modified by O-linked N-Acetylglucosamine
    • Zachara NE, Vosseller K, Hart GW: Detection and analysis of proteins modified by O-Linked N-Acetylglucosamine. Curr Protoc Protein Sci 2011, 66:1281-12833. http://onlinelibrary.wiley.com/doi/10.1002/0471140864.ps1208s66/ abstract;jsessionid=1342F2ABD48579AA0ED64C41034F0502.f03t03.
    • (2011) Curr Protoc Protein Sci , vol.66 , pp. 1281-12833
    • Zachara, N.E.1    Vosseller, K.2    Hart, G.W.3
  • 30
    • 84884323220 scopus 로고    scopus 로고
    • O-GlcNAcomics -Revealing roles of OGlcNAcylation in disease mechanisms and development of potential diagnostics
    • doi:10.1002/prca.201300001
    • Copeand RJ, Han G, Hart GW: O-GlcNAcomics-Revealing roles of OGlcNAcylation in disease mechanisms and development of potential diagnostics. Proteomics Clin Appl 2013, 7:597-606. doi:10.1002/prca.201300001.
    • (2013) Proteomics Clin Appl , vol.7 , pp. 597-606
    • Copeand, R.J.1    Han, G.2    Hart, G.W.3
  • 31
    • 0035876021 scopus 로고    scopus 로고
    • Characterization of a mouse monoclonal antibody specific for O-linked N-acetylglucosamine
    • DOI 10.1006/abio.2001.5132
    • Comer FI, Vosseller K, Wells L, Accavitti MA, Hart GW: Characterization of a mouse monoclonl antibody specific for O-linked N-Acetylglucosamine. Anal Biochem 2001, 293:169-177. (Pubitemid 32547901)
    • (2001) Analytical Biochemistry , vol.293 , Issue.2 , pp. 169-177
    • Comer, F.I.1    Vosseller, K.2    Wells, L.3    Accavitti, M.A.4    Hart, G.W.5
  • 32
    • 0023257987 scopus 로고
    • Monoclonal antibodies identify a group of nuclear pore complex glycoproteins
    • DOI 10.1083/jcb.104.5.1143
    • Snow CM, Senior A, Gerace L: Monoclonal antibodies identify a group of nuclear pore complex glycoproteins. J Cell Biol 1987, 104:1143-1156. (Pubitemid 17084472)
    • (1987) Journal of Cell Biology , vol.104 , Issue.5 , pp. 1143-1156
    • Snow, C.M.1    Senior, A.2    Gerace, L.3
  • 33
    • 0023225084 scopus 로고
    • Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine
    • DOI 10.1083/jcb.104.5.1157
    • Holt GD, Snow CM, Senior A, Haltiwanger RS, Gerace L, Hart GW: Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-Acetylglucosamine. J Cell Biol 1987, 104:1157-1164. (Pubitemid 17084473)
    • (1987) Journal of Cell Biology , vol.104 , Issue.5 , pp. 1157-1164
    • Holt, G.D.1    Snow, C.M.2    Senior, A.3
  • 34
    • 0025299405 scopus 로고
    • Cytologic assessment of nuclear and cytoplasmic O-linked N-Acetylglucosamine distribution by using anti-streptococcal monoclonal antibodies
    • Turner JR, Tartakoff AM, Greenspan NS: Cytologic assessment of nuclear and cytoplasmic O-linked N-Acetylglucosamine distribution by using anti-streptococcal monoclonal antibodies. Proc Natl Acad Sci USA 1990, 87:5608-5612.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5608-5612
    • Turner, J.R.1    Tartakoff, A.M.2    Greenspan, N.S.3
  • 36
    • 0036374266 scopus 로고    scopus 로고
    • Identification of ewing's sarcoma gene product as a glycoprotein using a monoclonal antibody that recognizes an immune determinant containing O-linked N-Acetylglucosamine moiety
    • Matsuoka Y, Shibata S, Yasuhara N, Yoneda Y: Identification of Ewing's sarcoma gene product as a glycoprotein using a monoclonal antibody that recognizes an immunodeterminant containing O-linked N-Acetylglucosamine moiety. Hybrid Hybridomics 2002, 21:233-236.
    • (2002) Hybrid Hybridomics , vol.21 , pp. 233-236
    • Matsuoka, Y.1    Shibata, S.2    Yasuhara, N.3    Yoneda, Y.4
  • 37
    • 79955451720 scopus 로고    scopus 로고
    • O-GlcNAc -specific antibody CTD110.6 cross-reacts with N-GlcNAc2- modified proteins induced under glucose deprivation
    • Isono T: O-GlcNAc-specific antibody CTD110.6 cross-reacts with N-GlcNAc2- modified proteins induced under glucose deprivation. PLoS ONE 2011, 6(4): e18959.
    • (2011) PLoS ONE , vol.6 , Issue.4
    • Isono, T.1
  • 38
    • 0024516198 scopus 로고
    • Glycosylation of chromosomal proteins: Localization of O-linked N-acetylglucosamine in Drosophila chromatin
    • DOI 10.1016/0092-8674(89)90962-8
    • Kelly WG, Hart GW: Glycosylation of chromosomal proteins: localization of O-linked N-Acetylglucosamine in Drosophila chromatin. Cell 1989, 57:243- 251. (Pubitemid 19112364)
    • (1989) Cell , vol.57 , Issue.2 , pp. 243-251
    • Kelly, W.G.1    Hart, G.W.2
  • 39
    • 33750309519 scopus 로고    scopus 로고
    • Comparative analysis by frontal affinity chromatography of oligosaccharide specificity of GlcNAc-binding lectins, Griffonia simplicifolia lectin-II (GSL-II) and Boletopsis leucomelas lectin (BLL)
    • DOI 10.1093/jb/mvj148
    • Nakamura-Tsuruta S, Kominami J, Kamei M, Koyama Y, Suzuki T, Isemura M, Hirabayashi J: Analysis by frontal affinity chromatography of oligosaccharide specificity of GlcNAc-binding lectins, Griffonia simplicifolia lectin-II (GSL-II) and Boletopsis leucomelas lectin (BLL). J Biochem 2006, 140:285-291. (Pubitemid 44618915)
    • (2006) Journal of Biochemistry , vol.140 , Issue.2 , pp. 285-291
    • Nakamura-Tsuruta, S.1    Kominami, J.2    Kamei, M.3    Koyama, Y.4    Suzuki, T.5    Isemura, M.6    Hirabayashi, J.7
  • 40
    • 0033644367 scopus 로고    scopus 로고
    • Identification of glycosylation sites in mucin peptides by edman degradation
    • Zachara NE, Gooley AA: Identification of glycosylation sites in mucin peptides by Edman degradation. Methods Mol Biol 2000, 125:121-128.
    • (2000) Methods Mol Biol , vol.125 , pp. 121-128
    • Zachara, N.E.1    Gooley, A.A.2
  • 42
    • 0027289130 scopus 로고
    • RNA polymerase II is a glycoprotein. Modification of the COOH-terminal domain by O-GlcNAc
    • Kelly WG, Dahmus ME, Hart GW: RNA polymerase II is a glycoprotein. Modification of the COOH-Terminal domain by O-GlcNAc. J Biol Chem 1993, 268:10416-10424. (Pubitemid 23150226)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.14 , pp. 10416-10424
    • Kelly, W.G.1    Dahmus, M.E.2    Hart, G.W.3
  • 44
    • 33749750735 scopus 로고
    • Fast atom bombardment of solids (F.A.B.): A new ion source for mass spectrometry
    • Barber M, Bordoli RS, Sedgewick RD, Tyler AN: Fast atom bombardment of solids (F.A.B.): A new ion source for mass spectrometry. J Chem Soc Chem Commun 1981, 7:325-327.
    • (1981) J Chem Soc Chem Commun , vol.7 , pp. 325-327
    • Barber, M.1    Bordoli, R.S.2    Sedgewick, R.D.3    Tyler, A.N.4
  • 46
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn JB, Mann M, Meng CK, Wong SF, Whitehouse CM: Electrospray ionization for mass spectrometry of large biomolecules. Science 1989, 246:64-71. (Pubitemid 19252085)
    • (1989) Science , vol.246 , Issue.4926 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 47
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10, 000 daltons
    • Karas M, Hillenkamp F: Laser desorption ionization of proteins with molecular masses exceeding 10, 000 daltons. Anal Chem 1988, 60:2299- 2301.
    • (1988) Anal Chem , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 48
    • 34548336772 scopus 로고    scopus 로고
    • Higher-energy C-trap dissociation for peptide modification analysis
    • DOI 10.1038/nmeth1060, PII NMETH1060
    • Olsen JV, Macek B, Lange O, Makarov A, Horning S, Mann M: Higher-energy C-Trap dissociation for peptide modification analysis. Nat Methods 2007, 4:709-712. (Pubitemid 47338163)
    • (2007) Nature Methods , vol.4 , Issue.9 , pp. 709-712
    • Olsen, J.V.1    Macek, B.2    Lange, O.3    Makarov, A.4    Horning, S.5    Mann, M.6
  • 50
    • 0035567107 scopus 로고    scopus 로고
    • Identification of GlcNAcylation sites of peptides and α-crystallin using Q-TOF mass spectrometry
    • DOI 10.1016/S1044-0305(01)00295-1, PII S1044030501002951
    • Chalkley RJ, Burlingame AL: Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry. J Am Soc Mass Spectrom 2001, 12:1106-1113. (Pubitemid 34552656)
    • (2001) Journal of the American Society for Mass Spectrometry , vol.12 , Issue.10 , pp. 1106-1113
    • Chalkley, R.J.1    Burlingame, A.L.2
  • 51
    • 0344870025 scopus 로고    scopus 로고
    • Identification of novel sites of O-NAcetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry
    • Chalkley RJ, Burlingame AL: Identification of novel sites of O-NAcetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry. Mol Cell Proteomics 2003, 2:182-190.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 182-190
    • Chalkley, R.J.1    Burlingame, A.L.2
  • 52
    • 79954437580 scopus 로고    scopus 로고
    • Mapping O-GlcNAc modification sites on tau and generation of a sitespecific O-GlcNAc tau antibody
    • Yuzwa SA, Yadav AK, Skorobogatko Y, Clark T, Vosseller K, Vocadlo DJ: Mapping O-GlcNAc modification sites on Tau and generation of a sitespecific O-GlcNAc Tau antibody. Amino Acids 2011, 40:857-868.
    • (2011) Amino Acids , vol.40 , pp. 857-868
    • Yuzwa, S.A.1    Yadav, A.K.2    Skorobogatko, Y.3    Clark, T.4    Vosseller, K.5    Vocadlo, D.J.6
  • 53
    • 80052472260 scopus 로고    scopus 로고
    • Combining high-energy c-Trap dissociation and electron transfer dissociation for protein O-GlcNAc modification site assignment
    • Zhao P, Viner R, Teo CF, Boons GJ, Horn D, Wells L: Combining high-energy C-Trap dissociation and electron transfer dissociation for protein O-GlcNAc modification site assignment. J Proteome Res 2011, 10:4088-4104.
    • (2011) J Proteome Res , vol.10 , pp. 4088-4104
    • Zhao, P.1    Viner, R.2    Teo, C.F.3    Boons, G.J.4    Horn, D.5    Wells, L.6
  • 54
    • 0030025149 scopus 로고    scopus 로고
    • Selective detection and site-analysis of O-GlcNAc-modified glycopeptides by β-elimination and tandem electrospray mass spectrometry
    • DOI 10.1006/abio.1996.0047
    • Greis KD, Hayes BK, Comer FI, Kirk M, Barnes S, Lowary TL, Hart GW: Selective detection and site-Analysis of O-GlcNAc-modified glycopeptides by beta-elimination and tandem electrospray mass spectrometry. Anal Biochem 1996, 234:38-49. (Pubitemid 26045751)
    • (1996) Analytical Biochemistry , vol.234 , Issue.1 , pp. 38-49
    • Greis, K.D.1    Hayes, B.K.2    Comer, F.I.3    Kirk, M.4    Barnes, S.5    Lowary, T.L.6    Hart, G.W.7
  • 55
    • 0001607910 scopus 로고    scopus 로고
    • Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-Translational modifications
    • Wells L, Vosseller K, Cole RN, Cronshaw JM, Matunis MJ, Hart GW: Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-Translational modifications. Mol Cell Proteomics 2002, 1:791-804.
    • (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
  • 57
    • 72449170135 scopus 로고    scopus 로고
    • O-linked N-Acetylglucosamine modification of insulin receptor substrate-1 occurs in close proximity to multiple SH2 domain binding motifs
    • Klein AL, Berkaw MN, Buse MG, Ball LE: O-linked N-Acetylglucosamine modification of insulin receptor substrate-1 occurs in close proximity to multiple SH2 domain binding motifs. Mol Cell Proteomics 2009, 8:2733- 2745.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2733-2745
    • Klein, A.L.1    Berkaw, M.N.2    Buse, M.G.3    Ball, L.E.4
  • 58
    • 84874989980 scopus 로고    scopus 로고
    • Electron transfer dissociation (ETD): The mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-A study of the O-GlcNAcylated protein host cell factor C1
    • Myers SA, Daou S, Affarel B, Burlingame A: Electron transfer dissociation (ETD): The mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-A study of the O-GlcNAcylated protein host cell factor C1. Proteomics 2013, 13:982-991.
    • (2013) Proteomics , vol.13 , pp. 982-991
    • Myers, S.A.1    Daou, S.2    Affarel, B.3    Burlingame, A.4
  • 59
    • 84886896817 scopus 로고    scopus 로고
    • O-GlcNAc regulates emerin binding to BAF in a chromatin- And lamin b-enriched 'niche'
    • doi:10.1074/jbc. M113.503060
    • Berk JM, Maitra S, Dawdy AW, Shabanowitz J, Hunt DF, Wilson KL: O-GlcNAc regulates emerin binding to BAF in a chromatin- And lamin B-enriched 'niche'. J Biol Chem 2013, 288:30192-30209. doi:10.1074/jbc. M113.503060.
    • (2013) J Biol Chem , vol.288 , pp. 30192-30209
    • Berk, J.M.1    Maitra, S.2    Dawdy, A.W.3    Shabanowitz, J.4    Hunt, D.F.5    Wilson, K.L.6
  • 60
    • 84865737357 scopus 로고    scopus 로고
    • Peptide identification by tandem mass spectrometry with alternate fragmentation modes
    • Guthals A, Bandeira N: Peptide identification by tandem mass spectrometry with alternate fragmentation modes. Mol Cell Proteomics 2012, 11:550-557.
    • (2012) Mol Cell Proteomics , vol.11 , pp. 550-557
    • Guthals, A.1    Bandeira, N.2
  • 61
    • 79955747622 scopus 로고    scopus 로고
    • A novel two-stage tandem mass spectrometry approach and scoring scheme for the identification of O-GlcNAc modified peptides
    • Hahne H, Kuster B: A novel two-stage tandem mass spectrometry approach and scoring scheme for the identification of O-GlcNAc modified peptides. J Am Soc Mass Spectrom 2011, 22:931-942.
    • (2011) J Am Soc Mass Spectrom , vol.22 , pp. 931-942
    • Hahne, H.1    Kuster, B.2
  • 62
    • 0036091929 scopus 로고    scopus 로고
    • Production of O-GlcNAc modified recombinant proteins in Escherichia coli
    • Lim KH, Ha CH, Chang HI: Production of O-GlcNAc modified recombinant proteins in Escherichia coli. J Microbiol Biotech 2002, 12:306-311. (Pubitemid 34520978)
    • (2002) Journal of Microbiology and Biotechnology , vol.12 , Issue.2 , pp. 306-311
    • Lim, K.H.1    Ha, C.H.2    Chang, H.I.3
  • 63
    • 84885634003 scopus 로고    scopus 로고
    • Chemical derivatization of peptide carboxyl groups for highly efficient electron transfer dissociation
    • doi:10.1007/s13361-013-0701-2
    • Frey BL, Ladror DT, Sondalle SB, Krusemark CJ, Jue AL, Coon JJ, Smith LM: Chemical derivatization of peptide carboxyl groups for highly efficient electron transfer dissociation. J Am Soc Mass Spectrom 2013, 24:1710-1721. doi:10.1007/s13361-013-0701-2.
    • (2013) J Am Soc Mass Spectrom , vol.24 , pp. 1710-1721
    • Frey, B.L.1    Ladror, D.T.2    Sondalle, S.B.3    Krusemark, C.J.4    Jue, A.L.5    Coon, J.J.6    Smith, L.M.7
  • 64
    • 84858726212 scopus 로고    scopus 로고
    • Proteomic databases and tools to decipher post-Translational modifications
    • Kamath KS, Vasavada MS, Srivastava S: Proteomic databases and tools to decipher post-Translational modifications. J Proteomics 2011, 75:127-44.
    • (2011) J Proteomics , vol.75 , pp. 127-144
    • Kamath, K.S.1    Vasavada, M.S.2    Srivastava, S.3
  • 65
    • 79953652899 scopus 로고    scopus 로고
    • DBOGAP -An integrated bioinformatics resource for protein O-GlcNAcylation
    • Wang J, Torii M, Liu H, Hart GW, Hu ZZ: dbOGAP-An integrated bioinformatics resource for protein O-GlcNAcylation. BMC Bioinforma 2011, 12:91.
    • (2011) BMC Bioinforma , vol.12 , pp. 91
    • Wang, J.1    Torii, M.2    Liu, H.3    Hart, G.W.4    Hu, Z.Z.5
  • 66
    • 0036370537 scopus 로고    scopus 로고
    • Prediction of glycosylation across the human proteome and the correlation to protein function
    • Gupta R, Brunak S: Prediction of glycosylation across the human proteome and the correlation to protein function. Pac Symp Biocomput 2002, 7:310-322.
    • (2002) Pac Symp Biocomput , vol.7 , pp. 310-322
    • Gupta, R.1    Brunak, S.2
  • 67
    • 84885164309 scopus 로고    scopus 로고
    • O-GlcNAcPRED: A sensitive predictor to capture protein O-GlcNAcylation sites
    • doi:10.1039/C3MB-70326F
    • Jia C, Liu T, Wang Z: O-GlcNAcPRED: A sensitive predictor to capture protein O-GlcNAcylation sites. Mol BioSyst 2013, 9:2909-2913. doi:10.1039/C3MB-70326F.
    • (2013) Mol BioSyst , vol.9 , pp. 2909-2913
    • Jia, C.1    Liu, T.2    Wang, Z.3
  • 71
    • 84884139186 scopus 로고    scopus 로고
    • Activation of the transcriptional function of the NF-kB protein c-Rel by oglcnac glycosylation
    • Ramakrishnan P, Clark PM, Mason DE, Peters EC, Hsieh-Wilson LC, Baltimore D: Activation of the transcriptional function of the NF-kB Protein c-Rel by OGlcNAc Glycosylation. Sci Signal 2013, 6:ra75. http://stke.sciencemag.org/cgi/ content/abstract/sigtrans;6/290/ra75.
    • (2013) Sci Signal , vol.6
    • Ramakrishnan, P.1    Clark, P.M.2    Mason, D.E.3    Peters, E.C.4    Hsieh-Wilson, L.C.5    Baltimore, D.6
  • 72
    • 67651173106 scopus 로고    scopus 로고
    • Proteomics by mass spectrometry: Approaches, advances, and applications
    • Yates JR, Ruse CI, Nakorchevsky A: Proteomics by mass spectrometry: Approaches, advances, and applications. Annu Rev Biomed Eng 2009, 11:49-79.
    • (2009) Annu Rev Biomed Eng , vol.11 , pp. 49-79
    • Yates, J.R.1    Ruse, C.I.2    Nakorchevsky, A.3
  • 73
    • 79959424627 scopus 로고    scopus 로고
    • Quantitative, high-resolution proteomics for data-driven systems biology
    • Cox J, Mann M: Quantitative, high-resolution proteomics for data-driven systems biology. Annu Rev Biochem 2011, 80:273-299.
    • (2011) Annu Rev Biochem , vol.80 , pp. 273-299
    • Cox, J.1    Mann, M.2
  • 74
    • 84861897793 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics and network biology
    • Bensimon A, Heck AJ, Aebersold R: Mass spectrometry-based proteomics and network biology. Annu Rev Biochem 2012, 81:379-405.
    • (2012) Annu Rev Biochem , vol.81 , pp. 379-405
    • Bensimon, A.1    Heck, A.J.2    Aebersold, R.3
  • 75
    • 36949020624 scopus 로고    scopus 로고
    • Proteomic analysis of O-GlcNAc modifications derived from streptozotocin and glucosamine induced β-cell apoptosis
    • Park J, Kwon H, Kang Y, Kim Y: Proteomic analysis of O-GlcNAc modifications derived from streptozotocin and glucosamine induced beta-cell apoptosis. J Biochem Mol Biol 2007, 40:1058-1068. (Pubitemid 350242294)
    • (2007) Journal of Biochemistry and Molecular Biology , vol.40 , Issue.6 , pp. 1058-1068
    • Park, J.1    Kwon, H.2    Kang, Y.3    Kim, Y.4
  • 76
    • 58749095861 scopus 로고    scopus 로고
    • Two-dimensional gel-based approaches for the assessment of N-linked and O-GlcNAc glycosylation in human and simian immunodeficiency viruses
    • Graham DR, Mitsak MJ, Elliott ST, Chen D, Whelan SA, Hart GW, Van Eyk JE: Two-dimensional gel-based approaches for the assessment of N-Linked and O-GlcNAc glycosylation in human and simian immunodeficiency viruses. Proteomics 2008, 8:4919-4930.
    • (2008) Proteomics , vol.8 , pp. 4919-4930
    • Graham, D.R.1    Mitsak, M.J.2    Elliott, S.T.3    Chen, D.4    Whelan, S.A.5    Hart, G.W.6    Van Eyk, J.E.7
  • 79
    • 77957220211 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis in proteomics: Past, present and future
    • Rabilloud T, Chevallet M, Luche S, Lelong C: Two-dimensional gel electrophoresis in proteomics: past, present and future. J Proteomics 2010, 73:2064-2077.
    • (2010) J Proteomics , vol.73 , pp. 2064-2077
    • Rabilloud, T.1    Chevallet, M.2    Luche, S.3    Lelong, C.4
  • 80
    • 84867167595 scopus 로고    scopus 로고
    • Discovery of O-GlcNAc -modified proteins in published large-scale proteome data
    • Hahne H, Moghaddas-Gholami A, Kuster B: Discovery of O-GlcNAc-modified proteins in published large-scale proteome data. Mol Cell Proteomics 2012, 11:843-850.
    • (2012) Mol Cell Proteomics , vol.11 , pp. 843-850
    • Hahne, H.1    Moghaddas-Gholami, A.2    Kuster, B.3
  • 81
    • 34548438595 scopus 로고    scopus 로고
    • Dynamic interplay between O-linked N-acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation
    • DOI 10.1074/mcp.M600453-MCP200
    • Wang Z, Pandey A, Hart GW: Dynamic interplay between O-linked N-Acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation. Mol Cell Proteomics 2007, 6:1365-1379. (Pubitemid 47365435)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.8 , pp. 1365-1379
    • Wang, Z.1    Pandey, A.2    Hart, G.W.3
  • 82
    • 79954434103 scopus 로고    scopus 로고
    • The dynamic stressinduced " O-GlcNAc -ome" highlights functions for O-GlcNAc in regulating DNA damage/repair and other cellular pathways
    • Zachara NE, Molina H, Wong KY, Pandey A, Hart GW: The dynamic stressinduced "O-GlcNAc-ome" highlights functions for O-GlcNAc in regulating DNA damage/repair and other cellular pathways. Amino Acids 2011, 40:793-808.
    • (2011) Amino Acids , vol.40 , pp. 793-808
    • Zachara, N.E.1    Molina, H.2    Wong, K.Y.3    Pandey, A.4    Hart, G.W.5
  • 83
    • 5444254250 scopus 로고    scopus 로고
    • Lectin-based structural glycomics: Glycoproteomics and glycan profiling
    • DOI 10.1023/B:GLYC.0000043745.18988.a1, Ist Symposium of Japanese Consortium for Glycobiology and Glycotechnology
    • Hirabayashi J: Lectin-based structural glycomics: Glycoproteomics and glycan profiling. Glycoconjugate J 2004, 21:35-40. (Pubitemid 39360738)
    • (2004) Glycoconjugate Journal , vol.21 , Issue.1-2 , pp. 35-40
    • Hirabayashi, J.1
  • 84
    • 0026716436 scopus 로고
    • Crystal structure of a wheat germ agglutinin/glycophorinsialoglycopeptide receptor complex Structural basis for cooper-Ative lectin-cell binding
    • Wright CS: Crystal structure of a wheat germ agglutinin/ glycophorinsialoglycopeptide receptor complex. Structural basis for cooper-Ative lectin-cell binding. J Biol Chem 1992, 267:14345-14352.
    • (1992) J Biol Chem , vol.267 , pp. 14345-14352
    • Wright, C.S.1
  • 85
    • 0031281693 scopus 로고    scopus 로고
    • Bioaffinity chromatography in the 10 mM range of Kd
    • Leickt L, Bergstrom M, Zopf D, Ohlson S: Bioaffinity chromatography in the 10 mM range of Kd. Anal Biochem 1997, 253:135-136.
    • (1997) Anal Biochem , vol.253 , pp. 135-136
    • Leickt, L.1    Bergstrom, M.2    Zopf, D.3    Ohlson, S.4
  • 87
    • 67049158217 scopus 로고    scopus 로고
    • Identification of protein O-GlcNAcylation sites using electron transfer dissociation mass spectrometry on native peptides
    • Chalkley RJ, Thalhammer A, Schoepfer R, Burlingame AL: Identification of protein O-GlcNAcylation sites using electron transfer dissociation mass spectrometry on native peptides. Proc Natl Acad Sci USA 2009, 106:8894-8899.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 8894-8899
    • Chalkley, R.J.1    Thalhammer, A.2    Schoepfer, R.3    Burlingame, A.L.4
  • 88
    • 79959334683 scopus 로고    scopus 로고
    • Polycomb repressive complex 2 is necessary for the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells
    • Myers SA, Panning B, Burlingame AL: Polycomb repressive complex 2 is necessary for the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells. Proc Natl Acad Sci USA 2011, 108:9490-9495.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 9490-9495
    • Myers, S.A.1    Panning, B.2    Burlingame, A.L.3
  • 90
    • 84876004511 scopus 로고    scopus 로고
    • Identification of O-linked N-Acetylglucosamine (O-GlcNAc)-modified osteoblast proteins by electron transfer dissociation tandem mass spectrometry reveals proteins critical for bone formation
    • Nagel AK, Schilling M, Comte-Walters S, Berkaw MN, Ball LE: Identification of O-linked N-Acetylglucosamine (O-GlcNAc)-modified osteoblast proteins by electron transfer dissociation tandem mass spectrometry reveals proteins critical for bone formation. Mol Cell Proteomics 2013, 12:945-55.
    • (2013) Mol Cell Proteomics , vol.12 , pp. 945-955
    • Nagel, A.K.1    Schilling, M.2    Comte-Walters, S.3    Berkaw, M.N.4    Ball, L.E.5
  • 91
    • 0029031553 scopus 로고
    • Specific isolation of O-linked N-Acetylglucosamine glycopeptides from complex mixtures
    • Hayes BK, Greis KD, Hart GW: Specific isolation of O-linked N-Acetylglucosamine glycopeptides from complex mixtures. Anal Biochem 1995, 228:115-122.
    • (1995) Anal Biochem , vol.228 , pp. 115-122
    • Hayes, B.K.1    Greis, K.D.2    Hart, G.W.3
  • 92
    • 0034329621 scopus 로고    scopus 로고
    • Simultaneous detection and identification of O-GlcNAc -modified glycoproteins using liquid chromatography-Tandem mass spectrometry
    • Haynes PA, Aebersold R: Simultaneous detection and identification of O-GlcNAc-modified glycoproteins using liquid chromatography-Tandem mass spectrometry. Anal Chem 2000, 72:5402-5410.
    • (2000) Anal Chem , vol.72 , pp. 5402-5410
    • Haynes, P.A.1    Aebersold, R.2
  • 93
    • 79954437842 scopus 로고    scopus 로고
    • O-GlcNAcylation of the plum pox virus capsid protein catalyzed by SECRET AGENT: Characterization of O-GlcNAc sites by electron transfer dissociation mass spectrometry
    • Kim YC, Udeshi ND, Balsbaugh JL, Shabanowitz J, Hunt DF, Olszewski NE: O-GlcNAcylation of the Plum pox virus capsid protein catalyzed by SECRET AGENT: characterization of O-GlcNAc sites by electron transfer dissociation mass spectrometry. Amino Acid 2011, 40:869-876.
    • (2011) Amino Acid , vol.40 , pp. 869-876
    • Kim, Y.C.1    Udeshi, N.D.2    Balsbaugh, J.L.3    Shabanowitz, J.4    Hunt, D.F.5    Olszewski, N.E.6
  • 94
    • 77952034762 scopus 로고    scopus 로고
    • Enrichment of O-GlcNAc modified proteins by the periodate oxidation-hydrazide resin capture approach
    • Klement E, Lipinszki Z, Kupihár Z, Udvardy A, Medzihradszky KF: Enrichment of O-GlcNAc modified proteins by the periodate oxidation-hydrazide resin capture approach. J Proteome Res 2010, 9:2200-2206.
    • (2010) J Proteome Res , vol.9 , pp. 2200-2206
    • Klement, E.1    Lipinszki, Z.2    Kupihár, Z.3    Udvardy, A.4    Medzihradszky, K.F.5
  • 95
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • DOI 10.1038/nbt827
    • Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol 2003, 21:660-666. (Pubitemid 36638093)
    • (2003) Nature Biotechnology , vol.21 , Issue.6 , pp. 660-666
    • Zhang, H.1    Li, X.-J.2    Martin, D.B.3    Aebersold, R.4
  • 96
    • 13844313887 scopus 로고    scopus 로고
    • Quantitative analysis of both protein expression and serine/threonine post-translational modifications through stable isotope labeling with dithiothreitol
    • DOI 10.1002/pmic.200401066
    • Vosseller K, Hansen KC, Chalkley RJ, Trinidad JC, Wells L, Hart GW, Burlingame AL: Quantitative analysis of both protein expression and serine/threonine post-Translational modifications through stable isotope labeling with dithiothreitol. Proteomics 2005, 5:388-398. (Pubitemid 40262055)
    • (2005) Proteomics , vol.5 , Issue.2 , pp. 388-398
    • Vosseller, K.1    Hansen, K.C.2    Chalkley, R.J.3    Trinidad, J.C.4    Wells, L.5    Hart, G.W.6    Burlingame, A.L.7
  • 97
    • 0026015290 scopus 로고
    • Determination and location of phosphoserine in proteins and peptides by conversion to S-ethylcysteine
    • Meyer HE, Hoffmann-Posorske E, Heilmeyer LM Jr: Determination and location of phosphoserine in proteins and peptides by conversion to S-ethylcysteine. Methods Enzymol 1991, 201:169-185.
    • (1991) Methods Enzymol , vol.201 , pp. 169-185
    • Meyer, H.E.1    Hoffmann-Posorske, E.2    Heilmeyer Jr., L.M.3
  • 98
    • 0036006576 scopus 로고    scopus 로고
    • Identification of substituted sites on MUC5AC mucin motif peptides after enzymatic O-glycosylation combining β-elimination and fixed-charge derivatization
    • DOI 10.1002/rcm.532
    • Czeszak X, Ricart G, Tetaert D, Michalski JC, Lemoine J: Identification of substituted sites on MUC5AC mucin motif peptides after enzymatic Oglycosylation combining beta-elimination and fixed-charge derivatization. Rapid Commun Mass Spectrom 2002, 16:27-34. (Pubitemid 34032277)
    • (2002) Rapid Communications in Mass Spectrometry , vol.16 , Issue.1 , pp. 27-34
    • Czeszak, X.1    Ricart, G.2    Tetaert, D.3    Michalski, J.C.4    Lemoine, J.5
  • 99
    • 65349126348 scopus 로고    scopus 로고
    • Mapping of O-linked beta-nacetylglucosamine modification sites in key contractile proteins of rat skeletal muscle
    • Hédou J, Bastide B, Page A, Michalski JC, Morelle W: Mapping of O-linked beta-Nacetylglucosamine modification sites in key contractile proteins of rat skeletal muscle. Proteomics 2009, 9:2139-2148.
    • (2009) Proteomics , vol.9 , pp. 2139-2148
    • Hédou, J.1    Bastide, B.2    Page, A.3    Michalski, J.C.4    Morelle, W.5
  • 101
    • 0037036376 scopus 로고    scopus 로고
    • Structure-based design of β1,4-galactosyltransferase I (β4Gal-T1) with equally efficient N-acetylgalactosaminyltransferase activity: Point mutation broadens β4Gal-T1 donor specificity
    • DOI 10.1074/jbc.M111183200
    • Ramakrishnan B, Qasba PK: Structure-based design of beta 1, 4-galactosyltransferase I (beta 4Gal-T1) with equally efficient N-Acetylgalactosaminyltransferase activity: point mutation broadens beta 4Gal-T1 donor specificity. J Biol Chem 2002, 277:20833-20839. (Pubitemid 34967390)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.23 , pp. 20833-20839
    • Ramakrishnan, B.1    Qasba, P.K.2
  • 107
    • 76649126396 scopus 로고    scopus 로고
    • Enrichment and site mapping of O-linked N-Acetylglucosamine by a combination of chemical/enzymatic tagging, photochemical cleavage, and electron transfer dissociation mass spectrometry
    • Wang Z, Udeshi ND, O'Malley M, Shabanowitz J, Hunt DF, Hart GW: Enrichment and site mapping of O-linked N-Acetylglucosamine by a combination of chemical/enzymatic tagging, photochemical cleavage, and electron transfer dissociation mass spectrometry. Mol Cell Proteomics 2010, 9:153-160.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 153-160
    • Wang, Z.1    Udeshi, N.D.2    O'Malley, M.3    Shabanowitz, J.4    Hunt, D.F.5    Hart, G.W.6
  • 110
    • 79953679905 scopus 로고    scopus 로고
    • Purification and identification of O-GlcNAc -modified peptides using phosphatebased alkyne click chemistry in combination with titanium dioxide chromatography and mass spectrometry
    • Parker BL, Gupta P, Cordwell SJ, Larsen MR, Palmisano G: Purification and identification of O-GlcNAc-modified peptides using phosphatebased alkyne CLICK chemistry in combination with titanium dioxide chromatography and mass spectrometry. J Proteome Res 2011, 10:1449-1458.
    • (2011) J Proteome Res , vol.10 , pp. 1449-1458
    • Parker, B.L.1    Gupta, P.2    Cordwell, S.J.3    Larsen, M.R.4    Palmisano, G.5
  • 111
    • 77953531317 scopus 로고    scopus 로고
    • O- GlcNAc cycling enzymes associate with the translational machinery and modify core ribosomal proteins
    • Zeidan Q, Wang Z, De Maio A, Hart GW: O-GlcNAc cycling enzymes associate with the translational machinery and modify core ribosomal proteins. Mol Biol Cell 2010, 21:1922-1936.
    • (2010) Mol Biol Cell , vol.21 , pp. 1922-1936
    • Zeidan, Q.1    Wang, Z.2    De Maio, A.3    Hart, G.W.4
  • 112
    • 78650447665 scopus 로고    scopus 로고
    • ß-N-Acetylglucosamine (O-GlcNAc) is part of the histone code
    • Sakabe K, Wang Z, Hart GW: ß-N-Acetylglucosamine (O-GlcNAc) is part of the histone code. Proc Natl Acad Sci USA 2010, 107:19915-19920.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 19915-19920
    • Sakabe, K.1    Wang, Z.2    Hart, G.W.3
  • 114
    • 63249106433 scopus 로고    scopus 로고
    • Site-specific GlcNAcylation of human erythrocyte proteins: Potential biomarker(s) for diabetes
    • Wang Z, Park K, Comer F, Hsieh-Wilson LC, Saudek CD, Hart GW: Site-specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes. Diabetes 2009, 58:309-317.
    • (2009) Diabetes , vol.58 , pp. 309-317
    • Wang, Z.1    Park, K.2    Comer, F.3    Hsieh-Wilson, L.C.4    Saudek, C.D.5    Hart, G.W.6
  • 120
    • 84873350431 scopus 로고    scopus 로고
    • Proteome wide purification and identification of O-GlcNAc -modified proteins using click chemistry and mass spectrometry
    • Hahne H, Sobotzki N, Nyberg T, Helm D, Borodkin VS, van Aalten DM, Agnew B, Kuster B: Proteome wide purification and identification of O-GlcNAc-modified proteins using click chemistry and mass spectrometry. J Proteome Res 2013, 12:927-936.
    • (2013) J Proteome Res , vol.12 , pp. 927-936
    • Hahne, H.1    Sobotzki, N.2    Nyberg, T.3    Helm, D.4    Borodkin, V.S.5    Van Aalten, D.M.6    Agnew, B.7    Kuster, B.8
  • 121
    • 79957694784 scopus 로고    scopus 로고
    • Chemical reporters for fluorescent detection and identification of O-GlcNAc -modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1
    • Zaro BW, Yang YY, Hang HC, Pratt MR: Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1. Proc Natl Acad Sci USA 2011, 108:8146-8151.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 8146-8151
    • Zaro, B.W.1    Yang, Y.Y.2    Hang, H.C.3    Pratt, M.R.4
  • 122
    • 77957293282 scopus 로고    scopus 로고
    • Chemoselective attachment of small molecule effector functionality to human adenoviruses facilitates gene delivery to cancer cells
    • Banerjee PS, Ostapchuk P, Hearing P, Carrico I: Chemoselective attachment of small molecule effector functionality to human adenoviruses facilitates gene delivery to cancer cells. J Am Chem Soc 2010, 132:13615- 13617.
    • (2010) J Am Chem Soc , vol.132 , pp. 13615-13617
    • Banerjee, P.S.1    Ostapchuk, P.2    Hearing, P.3    Carrico, I.4
  • 123
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong SE, Blagoev B, Kratchmarova I, Kristensen DB, Steen H, Pandey A, Mann M: Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 2002, 1:376-386.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 124
    • 34247396011 scopus 로고    scopus 로고
    • A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC)
    • Ong SE, Mann M: A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC). Nat Protoc 2007, 1:2650-2660.
    • (2007) Nat Protoc , vol.1 , pp. 2650-2660
    • Ong, S.E.1    Mann, M.2
  • 125
    • 40649095957 scopus 로고    scopus 로고
    • Quantitative proteomics using stable isotope labeling with amino acids in cell culture
    • DOI 10.1038/nprot.2008.2, PII NPROT.2008.2
    • Harsha HC, Molina H, Pandey A: Quantitative proteomics using stable isotope labeling with amino acids in cell culture. Nat Protoc 2008, 3:505- 516. (Pubitemid 351372235)
    • (2008) Nature Protocols , vol.3 , Issue.3 , pp. 505-516
    • Harsha, H.C.1    Molina, H.2    Pandey, A.3
  • 126
    • 47549099572 scopus 로고    scopus 로고
    • SILAC Mouse for Quantitative Proteomics Uncovers Kindlin-3 as an Essential Factor for Red Blood Cell Function
    • DOI 10.1016/j.cell.2008.05.033, PII S0092867408006958
    • Krüger M, Moser M, Ussar S, Thievessen I, Luber CA, Forner F, Schmidt S, Zanivan S, Fässler R, Mann M: SILAC mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function. Cell 2008, 134:353-64. (Pubitemid 352010327)
    • (2008) Cell , vol.134 , Issue.2 , pp. 353-364
    • Kruger, M.1    Moser, M.2    Ussar, S.3    Thievessen, I.4    Luber, C.A.5    Forner, F.6    Schmidt, S.7    Zanivan, S.8    Fassler, R.9    Mann, M.10
  • 128
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • DOI 10.1038/13690
    • Gygi SP, Rist B, Gerber SA, Turecek F, Gelb MH, Aebersold R: Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat Biotechnol 1999, 17:994-999. (Pubitemid 29474856)
    • (1999) Nature Biotechnology , vol.17 , Issue.10 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 129
    • 66749114309 scopus 로고    scopus 로고
    • 18O2-labeling in quantitative proteomic strategies: A status report
    • Fenselau C, Yao X: 18O2-labeling in quantitative proteomic strategies: A status report. J Proteome Res 2009, 8:2140-2143.
    • (2009) J Proteome Res , vol.8 , pp. 2140-2143
    • Fenselau, C.1    Yao, X.2
  • 131
    • 0348014635 scopus 로고    scopus 로고
    • Stable-isotope dimethyl labeling for quantitative proteomics
    • Hsu JL, Huang SY, Chow NH, Chen SH: Stable-isotope dimethyl labeling for quantitative proteomics. Anal Chem 2003, 75:6843-6852.
    • (2003) Anal Chem , vol.75 , pp. 6843-6852
    • Hsu, J.L.1    Huang, S.Y.2    Chow, N.H.3    Chen, S.H.4
  • 132
    • 64749108158 scopus 로고    scopus 로고
    • Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics
    • Boersema PJ, Raijmakers R, Lemeer S, Mohammed S, Heck AJ: Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics. Nat Protoc 2009, 4:484-494.
    • (2009) Nat Protoc , vol.4 , pp. 484-494
    • Boersema, P.J.1    Raijmakers, R.2    Lemeer, S.3    Mohammed, S.4    Heck, A.J.5
  • 133
    • 74049115774 scopus 로고    scopus 로고
    • Mass spectrometrybased label-free quantitative proteomics
    • Article ID 840518, doi:10.1155/2010/840518
    • Zhu W, Smith JW, Huang CM: Mass spectrometrybased label-free quantitative proteomics. J Biomed Biotechnol 2010. Article ID 840518, doi:10.1155/2010/ 840518. http://www.hindawi.com/journals/bmri/2010/840518/.
    • (2010) J Biomed Biotechnol
    • Zhu, W.1    Smith, J.W.2    Huang, C.M.3
  • 134
    • 54049090766 scopus 로고    scopus 로고
    • Selected reaction monitoring for quantitative proteomics: A tutorial
    • Lange V, Picotti P, Domon B, Aebersold R: Selected reaction monitoring for quantitative proteomics: A tutorial. Mol Syst Biol 2008, 4:222.
    • (2008) Mol Syst Biol , vol.4 , pp. 222
    • Lange, V.1    Picotti, P.2    Domon, B.3    Aebersold, R.4
  • 135
    • 84891807954 scopus 로고    scopus 로고
    • Multiple reaction monitoring mass spectrometry for the discovery and quantification of O-GlcNAc -modified proteins
    • Maury JJ, Ng D, Bi X, Bardor M, Choo A: Multiple reaction monitoring mass spectrometry for the discovery and quantification of O-GlcNAc-Modified Proteins. Anal Chem 2014, 86:395-402.
    • (2014) Anal Chem , vol.86 , pp. 395-402
    • Maury, J.J.1    Ng, D.2    Bi, X.3    Bardor, M.4    Choo, A.5
  • 136
    • 66849089268 scopus 로고    scopus 로고
    • Protein microarrays: High-Throughput tools for proteomics
    • Stoevesandt O, Taussig MJ, He M: Protein microarrays: high-Throughput tools for proteomics. Expert Rev Proteomics 2009, 6:145-157.
    • (2009) Expert Rev Proteomics , vol.6 , pp. 145-157
    • Stoevesandt, O.1    Taussig, M.J.2    He, M.3
  • 138
    • 69249155637 scopus 로고    scopus 로고
    • Regulation of calcium/calmodulin-dependent kinase IV by O-GlcNAc modification
    • Dias WB, Cheung WD, Wang Z, Hart GW: Regulation of calcium/calmodulin- dependent kinase IV by O-GlcNAc modification. J Biol Chem 2009, 284:21327-21337.
    • (2009) J Biol Chem , vol.284 , pp. 21327-21337
    • Dias, W.B.1    Cheung, W.D.2    Wang, Z.3    Hart, G.W.4
  • 141
    • 62549161375 scopus 로고    scopus 로고
    • Loss of p53 enhances catalytic activity of IKK -beta through O-linked beta-N-Acetyl glucosamine modification
    • Kawauchi K, Araki K, Tobiume K, Tanaka N: Loss of p53 enhances catalytic activity of IKK-beta through O-linked beta-N-Acetyl glucosamine modification. Proc Natl Acad Sci USA 2009, 106:3431-3436.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 3431-3436
    • Kawauchi, K.1    Araki, K.2    Tobiume, K.3    Tanaka, N.4
  • 142
    • 34247583996 scopus 로고    scopus 로고
    • Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins
    • DOI 10.1038/nature05815, PII NATURE05815
    • Hart GW, Housley MP, Slawson C: Cycling of O-linked ß-N- Acetylgluco- samine on nucleocytoplasmic proteins. Nature 2007, 446:1017- 1022. (Pubitemid 46676063)
    • (2007) Nature , vol.446 , Issue.7139 , pp. 1017-1022
    • Hart, G.W.1    Housley, M.P.2    Slawson, C.3


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