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Volumn 6, Issue 4, 2011, Pages

O-glcnac-specific antibody CTD110.6 cross-reacts with N-GlcNAc2-modified proteins induced under glucose deprivation

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLGLUCOSAMINIDASE; CD98 ANTIGEN; CTD110.6; DOLICHOL PHOSPHATE; GLYCOPROTEIN; HEAT SHOCK PROTEIN 70; LAMININ BETA3; MANNOSE; N ACETYLGLUCOSAMINE; OXYGEN REGULATED PROTEIN 150; PROTEIN ANTIBODY; PROTEIN MAC2BP; TRANSFERASE; TUNICAMYCIN; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE; CHITOBIOSYLDIPHOSPHODOLICHOL BETA MANNOSYLTRANSFERASE; CHITOBIOSYLDIPHOSPHODOLICHOL BETA-MANNOSYLTRANSFERASE; GLUCOSE; MANNOSYLTRANSFERASE; MONOCLONAL ANTIBODY; N ACETYLGLUCOSAMINYLTRANSFERASE; PROTEIN;

EID: 79955451720     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0018959     Document Type: Article
Times cited : (83)

References (24)
  • 1
    • 11144356519 scopus 로고    scopus 로고
    • Identification by proteomic analysis of calreticulin as a marker for bladder cancer and evaluation of the diagnostic accuracy of its detection in urine
    • Kageyama S, Isono T, Iwaki H, Wakabayashi Y, Okada Y, et al. (2004) Identification by proteomic analysis of calreticulin as a marker for bladder cancer and evaluation of the diagnostic accuracy of its detection in urine. Clin Chem 50: 857-866.
    • (2004) Clin Chem , vol.50 , pp. 857-866
    • Kageyama, S.1    Isono, T.2    Iwaki, H.3    Wakabayashi, Y.4    Okada, Y.5
  • 2
    • 19944429012 scopus 로고    scopus 로고
    • Diagnostic potential in bladder cancer of a panel of tumor markers (calreticulin, gamma -synuclein, and catechol-o-methyltransferase) identified by proteomic analysis
    • Iwaki H, Kageyama S, Isono T, Wakabayashi Y, Okada Y, et al. (2004) Diagnostic potential in bladder cancer of a panel of tumor markers (calreticulin, gamma-synuclein, and catechol-o-methyltransferase) identified by proteomic analysis. Cancer Sci 95: 955-961.
    • (2004) Cancer Sci , vol.95 , pp. 955-961
    • Iwaki, H.1    Kageyama, S.2    Isono, T.3    Wakabayashi, Y.4    Okada, Y.5
  • 3
    • 38149086852 scopus 로고    scopus 로고
    • A novel tumor-related protein, C7orf24, identified by proteome differential display of bladder urothelial carcinoma
    • Kageyama S, Iwaki H, Inoue H, Isono T, Yuasa T, et al. (2007) A novel tumor-related protein, C7orf24, identified by proteome differential display of bladder urothelial carcinoma. Proteomics Clin Appl 1: 192-199.
    • (2007) Proteomics Clin Appl , vol.1 , pp. 192-199
    • Kageyama, S.1    Iwaki, H.2    Inoue, H.3    Isono, T.4    Yuasa, T.5
  • 4
    • 69449086063 scopus 로고    scopus 로고
    • Supressin of cell invasiveness by periostin via TAB1/TAK1
    • Isono T, Kim CJ, Ando Y, Sakurai H, Okada Y, et al. (2009) Supressin of cell invasiveness by periostin via TAB1/TAK1. Int J Oncol 35: 425-432.
    • (2009) Int J Oncol , vol.35 , pp. 425-432
    • Isono, T.1    Kim, C.J.2    Ando, Y.3    Sakurai, H.4    Okada, Y.5
  • 5
    • 3042613480 scopus 로고    scopus 로고
    • O-GlcNAc a sensor of cellular state: the role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress
    • Zachara NE, Hart GW, (2004) O-GlcNAc a sensor of cellular state: the role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress. Biochim Biophys Acta 1673: 13-28.
    • (2004) Biochim Biophys Acta , vol.1673 , pp. 13-28
    • Zachara, N.E.1    Hart, G.W.2
  • 6
    • 34247583996 scopus 로고    scopus 로고
    • Cycling of O-inked β-N-acetylgulcosamine on nucleocytoplasmic proteins
    • Hart GW, Housley MP, Slawson C, (2007) Cycling of O-inked β-N-acetylgulcosamine on nucleocytoplasmic proteins. Nature 446: 1017-1022.
    • (2007) Nature , vol.446 , pp. 1017-1022
    • Hart, G.W.1    Housley, M.P.2    Slawson, C.3
  • 7
    • 77949769388 scopus 로고    scopus 로고
    • O-inked β-N-acetylgulcosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress
    • Butkinaree C, Park K, Hart GW, (2010) O-inked β-N-acetylgulcosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress. Biochim Biophys Acta 2010: 96-106.
    • (2010) Biochim Biophys Acta , vol.2010 , pp. 96-106
    • Butkinaree, C.1    Park, K.2    Hart, G.W.3
  • 8
    • 5444269110 scopus 로고    scopus 로고
    • The cellular fate of gulucose and its relevance in type 2 diabetes
    • Bouche C, Serdy S, Kahn CR, Goldfine AB, (2004) The cellular fate of gulucose and its relevance in type 2 diabetes. Endcrine Rev 25: 807-830.
    • (2004) Endcrine Rev , vol.25 , pp. 807-830
    • Bouche, C.1    Serdy, S.2    Kahn, C.R.3    Goldfine, A.B.4
  • 9
    • 44449166220 scopus 로고    scopus 로고
    • Glucose deprivation stimulates O-GlcNAc modification of proteins through up-regulation of O-inked N-acetylgulcosaminyltransferase
    • Taylor RP, Parker GJ, Hazel MW, Soesanto Y, Fuller W, et al. (2008) Glucose deprivation stimulates O-GlcNAc modification of proteins through up-regulation of O-inked N-acetylgulcosaminyltransferase. J Biol Chem 283: 6050-6057.
    • (2008) J Biol Chem , vol.283 , pp. 6050-6057
    • Taylor, R.P.1    Parker, G.J.2    Hazel, M.W.3    Soesanto, Y.4    Fuller, W.5
  • 10
    • 45149095784 scopus 로고    scopus 로고
    • AMP-activated protein kinase and p38 MAPK activate O-GlcNAcylation of neuronal protein during glucose deprivation
    • Cheung WD, Hart GW, (2008) AMP-activated protein kinase and p38 MAPK activate O-GlcNAcylation of neuronal protein during glucose deprivation. J Biol Chem 283: 13009-13020.
    • (2008) J Biol Chem , vol.283 , pp. 13009-13020
    • Cheung, W.D.1    Hart, G.W.2
  • 11
    • 63649085232 scopus 로고    scopus 로고
    • Up-regulation of O-GlcNAc transferase with Glucose deprivation in HepG2 cells is mediated by deceased hexamine pathway flux
    • Taylor RP, Geisler TS, Chambers JH, McClain DA, (2009) Up-regulation of O-GlcNAc transferase with Glucose deprivation in HepG2 cells is mediated by deceased hexamine pathway flux. J Biol Chem 284: 3428-3432.
    • (2009) J Biol Chem , vol.284 , pp. 3428-3432
    • Taylor, R.P.1    Geisler, T.S.2    Chambers, J.H.3    McClain, D.A.4
  • 12
    • 71749108365 scopus 로고    scopus 로고
    • O-GlcNAc protein modification in cancer cells increases in response to glucose deprivation through glycogen degradation
    • Kang JG, Park SY, Ji S, Jang I, Park S, et al. (2009) O-GlcNAc protein modification in cancer cells increases in response to glucose deprivation through glycogen degradation. J Biol Chem 284: 34777-34784.
    • (2009) J Biol Chem , vol.284 , pp. 34777-34784
    • Kang, J.G.1    Park, S.Y.2    Ji, S.3    Jang, I.4    Park, S.5
  • 14
    • 0032526394 scopus 로고    scopus 로고
    • N-Glycosylation by transfer of GlcNAc2 from dolichol-PP- GlcNAc2 to the protein moiety of the major yeast exoglucanase
    • Cueva., Cotano C, Larriba G, (1998) N-Glycosylation by transfer of GlcNAc2 from dolichol-PP- GlcNAc2 to the protein moiety of the major yeast exoglucanase. Yeast 14: 773-781.
    • (1998) Yeast , vol.14 , pp. 773-781
    • Cueva1    Cotano, C.2    Larriba, G.3
  • 15
    • 0028107097 scopus 로고
    • Growth-ralated coordinate regulation of the early N-Glycosylation genes in yeast
    • Kukuruzinska MA, Lennon K, (1994) Growth-ralated coordinate regulation of the early N-Glycosylation genes in yeast. Glycobiol 4: 437-443.
    • (1994) Glycobiol , vol.4 , pp. 437-443
    • Kukuruzinska, M.A.1    Lennon, K.2
  • 16
    • 0035876021 scopus 로고    scopus 로고
    • Characterization of a mouse monoclonal antibody specific for O-linked N-Acetylglucosamin
    • Comer FI, Vosseller K, Wells L, Accavitti MA, Hart GW, (2001) Characterization of a mouse monoclonal antibody specific for O-linked N-Acetylglucosamin. Anal Biochem 293: 169-177.
    • (2001) Anal Biochem , vol.293 , pp. 169-177
    • Comer, F.I.1    Vosseller, K.2    Wells, L.3    Accavitti, M.A.4    Hart, G.W.5
  • 17
    • 13444281918 scopus 로고    scopus 로고
    • The diversity of dolichol-linked precursors to Asn-linked glycans likely results from secondary loss of sets of glycosyltransferases
    • Samuelson J, Benerjee S, Magnelli P, Cui J, Kelleher DJ, et al. (2005) The diversity of dolichol-linked precursors to Asn-linked glycans likely results from secondary loss of sets of glycosyltransferases. Proc Natl Acad Sci 102: 1548-1553.
    • (2005) Proc Natl Acad Sci , vol.102 , pp. 1548-1553
    • Samuelson, J.1    Benerjee, S.2    Magnelli, P.3    Cui, J.4    Kelleher, D.J.5
  • 18
    • 79955417916 scopus 로고    scopus 로고
    • Congenital disorder of glycosylation: An update on defects affecting the biosynthesis of dolichol-linked oligosaccharides
    • Haeuptle M, Hennet T, (2009) Congenital disorder of glycosylation: An update on defects affecting the biosynthesis of dolichol-linked oligosaccharides. Human Mutation 130: 1-14.
    • (2009) Human Mutation , vol.130 , pp. 1-14
    • Haeuptle, M.1    Hennet, T.2
  • 19
    • 1542329546 scopus 로고    scopus 로고
    • Deficiency of the first mannosylation step in the N-glycosylation pathway causes congenital disorder of glycosylation type Ik
    • Grubenmann CE, Frank CG, Hulsmeier J, Schillen E, Matthijs G, et al. (2004) Deficiency of the first mannosylation step in the N-glycosylation pathway causes congenital disorder of glycosylation type Ik. Human Mol Genetics 13: 535-542.
    • (2004) Human Mol Genetics , vol.13 , pp. 535-542
    • Grubenmann, C.E.1    Frank, C.G.2    Hulsmeier, J.3    Schillen, E.4    Matthijs, G.5
  • 20
    • 10644251833 scopus 로고    scopus 로고
    • Serum and Glucocorticoid-regulated kinase Sgk1 inhibits insulin-dependent activation of phosphomannomutase 2 in transfected COS-7 cells
    • Menniti M, Iuliano R, Amato R, Boito R, Corea M, et al. (2004) Serum and Glucocorticoid-regulated kinase Sgk1 inhibits insulin-dependent activation of phosphomannomutase 2 in transfected COS-7 cells. Am J Physiol Cell Physiol 288: C148-C155.
    • (2004) Am J Physiol Cell Physiol , vol.288
    • Menniti, M.1    Iuliano, R.2    Amato, R.3    Boito, R.4    Corea, M.5
  • 21
    • 0015782448 scopus 로고
    • Established cell line of urinary bldder carcinma (T24) containing tumour-specific antigen
    • Bubenik J, Baresiva M, Viklicky V, Jakoubkova J, Sainerova H, et al. (1973) Established cell line of urinary bldder carcinma (T24) containing tumour-specific antigen. Int J Cancer 11: 766-773.
    • (1973) Int J Cancer , vol.11 , pp. 766-773
    • Bubenik, J.1    Baresiva, M.2    Viklicky, V.3    Jakoubkova, J.4    Sainerova, H.5
  • 22
    • 0023084783 scopus 로고
    • Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system
    • Dubridge RB, Tang P, Hsia HC, Leong PM, Miller JH, et al. (1987) Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system. Mol Cell Biol 7: 379-387.
    • (1987) Mol Cell Biol , vol.7 , pp. 379-387
    • Dubridge, R.B.1    Tang, P.2    Hsia, H.C.3    Leong, P.M.4    Miller, J.H.5
  • 23
    • 38649109196 scopus 로고    scopus 로고
    • Role of alternative splicing of periostin in human bladder carcinogenesisi
    • Kim CJ, Isono T, Tambe Y, Chano T, Okabe H, et al. (2008) Role of alternative splicing of periostin in human bladder carcinogenesisi. Int J Oncol 32: 161-169.
    • (2008) Int J Oncol , vol.32 , pp. 161-169
    • Kim, C.J.1    Isono, T.2    Tambe, Y.3    Chano, T.4    Okabe, H.5
  • 24
    • 0036892163 scopus 로고    scopus 로고
    • Structural diversity of cancer-related and non-cancer-related prostate-specific antigen
    • Isono T, Tanaka T, Kageyama S, Yoshiki, (2002) Structural diversity of cancer-related and non-cancer-related prostate-specific antigen. Clin Chem 48: 2187-2194.
    • (2002) Clin Chem , vol.48 , pp. 2187-2194
    • Isono, T.1    Tanaka, T.2    Kageyama, S.3    Yoshiki4


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