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Volumn 5, Issue AUG, 2014, Pages

X-inactivation normalizes O-GlcNAc transferase levels and generates an O-GlcNAc-depleted Barr body

Author keywords

Barr body; Gene silencing; O GlcNAc transferase; O GlcNAcylation; X chromosome inactivation

Indexed keywords

AZACITIDINE; AZASERINE; DNA METHYLTRANSFERASE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GLUTAMINE FRUCTOSE 6 PHOSPHATE AMINOTRANSFERASE; HISTONE H2A; LIPOFECTAMINE; N ACETYLGLUCOSAMINE; RNA POLYMERASE II;

EID: 84906214579     PISSN: None     EISSN: 16648021     Source Type: Journal    
DOI: 10.3389/fgene.2014.00256     Document Type: Article
Times cited : (17)

References (57)
  • 1
    • 84906258726 scopus 로고    scopus 로고
    • Chromosome imbalance as a driver of sex disparity in disease
    • doi: 10.7150/jgen.8123
    • Abramowitz, L. K., Olivier-Van Stichelen, S., and Hanover, J. A (2014). Chromosome imbalance as a driver of sex disparity in disease. J. Genomics 2014, 77-88. doi: 10.7150/jgen.8123
    • (2014) J. Genomics, 2014 , pp. 77-88
    • Abramowitz, L.K.1    Olivier-Van Stichelen, S.2    Hanover, J.A.3
  • 2
    • 69949107901 scopus 로고    scopus 로고
    • X-chromosome gene dosage and the risk of diabetes in Turner syndrome
    • doi: 10.1210/jc.2009-0384
    • Bakalov, V. K., Cheng, C., Zhou, J., and Bondy, C. A. (2009). X-chromosome gene dosage and the risk of diabetes in Turner syndrome. J. Clin. Endocrinol. Metab. 94, 3289-3296. doi: 10.1210/jc.2009-0384
    • (2009) J. Clin. Endocrinol. Metab. , vol.94 , pp. 3289-3296
    • Bakalov, V.K.1    Cheng, C.2    Zhou, J.3    Bondy, C.A.4
  • 3
    • 85045484695 scopus 로고
    • A morphological distinction between neurones of the male and female, and the behaviour of the nucleolar satellite during accelerated nucleoprotein synthesis
    • doi: 10.1038/163676a0
    • Barr, M. L., and Bertam, E. G. (1949). A morphological distinction between neurones of the male and female, and the behaviour of the nucleolar satellite during accelerated nucleoprotein synthesis. Nature 163:676. doi: 10.1038/163676a0
    • (1949) Nature , vol.163 , pp. 676
    • Barr, M.L.1    Bertam, E.G.2
  • 4
    • 0002826398 scopus 로고
    • The normal human female as a mosaic of X-chromosome activity: studies using the gene for C-6-PD-deficiency as a marker
    • doi: 10.1073/pnas.48.1.9
    • Beutler, E., Yeh, M., and Fairbanks, V. F. (1962). The normal human female as a mosaic of X-chromosome activity: studies using the gene for C-6-PD-deficiency as a marker. Proc. Natl. Acad. Sci. U.S.A. 48, 9-16. doi: 10.1073/pnas.48.1.9
    • (1962) Proc. Natl. Acad. Sci. U.S.A. , vol.48 , pp. 9-16
    • Beutler, E.1    Yeh, M.2    Fairbanks, V.F.3
  • 5
    • 42649100978 scopus 로고    scopus 로고
    • SmcHD1, containing a structural-maintenance-of-chromosomes hinge domain, has a critical role in X inactivation
    • doi: 10.1038/ng.142
    • Blewitt, M. E., Gendrel, A.-V., Pang, Z., Sparrow, D. B., Whitelaw, N., Craig, J. M., et al. (2008). SmcHD1, containing a structural-maintenance-of-chromosomes hinge domain, has a critical role in X inactivation. Nat. Genet. 40, 663-669. doi: 10.1038/ng.142
    • (2008) Nat. Genet. , vol.40 , pp. 663-669
    • Blewitt, M.E.1    Gendrel, A.-V.2    Pang, Z.3    Sparrow, D.B.4    Whitelaw, N.5    Craig, J.M.6
  • 6
    • 0016252967 scopus 로고
    • Characterisation of human N-acetyl-beta-hexosaminidase C
    • doi: 10.1016/0014-5793(74)81206-8
    • Braidman, I., Carroll, M., Dance, N., Robinson, D., Poenaru, L., Weber, A., et al. (1974). Characterisation of human N-acetyl-beta-hexosaminidase C. FEBS Lett. 41, 181-184. doi: 10.1016/0014-5793(74)81206-8
    • (1974) FEBS Lett. , vol.41 , pp. 181-184
    • Braidman, I.1    Carroll, M.2    Dance, N.3    Robinson, D.4    Poenaru, L.5    Weber, A.6
  • 7
    • 0026007719 scopus 로고
    • Localization of the X inactivation centre on the human X chromosome in Xq13
    • doi: 10.1038/349082a0
    • Brown, C. J., Lafreniere, R. G., Powers, V. E., Sebastio, G., Ballabio, A., Pettigrew, A. L., et al. (1991). Localization of the X inactivation centre on the human X chromosome in Xq13. Nature 349, 82-84. doi: 10.1038/349082a0
    • (1991) Nature , vol.349 , pp. 82-84
    • Brown, C.J.1    Lafreniere, R.G.2    Powers, V.E.3    Sebastio, G.4    Ballabio, A.5    Pettigrew, A.L.6
  • 8
    • 15244353967 scopus 로고    scopus 로고
    • X-inactivation profile reveals extensive variability in X-linked gene expression in females
    • doi: 10.1038/nature03479
    • Carrel, L., and Willard, H. F. (2005). X-inactivation profile reveals extensive variability in X-linked gene expression in females. Nature 434, 400-404. doi: 10.1038/nature03479
    • (2005) Nature , vol.434 , pp. 400-404
    • Carrel, L.1    Willard, H.F.2
  • 9
    • 0042379770 scopus 로고    scopus 로고
    • Chromatin of the Barr body: histone and non-histone proteins associated with or excluded from the inactive X chromosome
    • doi: 10.1093/hmg/ddg229
    • Chadwick, B., and Willard, H. (2003). Chromatin of the Barr body: histone and non-histone proteins associated with or excluded from the inactive X chromosome. Hum. Mol. Genet. 12, 2167-2178. doi: 10.1093/hmg/ddg229
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2167-2178
    • Chadwick, B.1    Willard, H.2
  • 10
    • 84880627384 scopus 로고    scopus 로고
    • Proteomic analysis and abrogated expression of O-GlcNAcylated proteins associated with primary breast cancer
    • doi: 10.1002/pmic.201200126
    • Champattanachai, V., Netsirisawan, P., Chaiyawat, P., Phueaouan, T., Charoenwattanasatien, R., Chokchaichamnankit, D., et al. (2013). Proteomic analysis and abrogated expression of O-GlcNAcylated proteins associated with primary breast cancer. Proteomics 13, 2088-2099. doi: 10.1002/pmic.201200126
    • (2013) Proteomics , vol.13 , pp. 2088-2099
    • Champattanachai, V.1    Netsirisawan, P.2    Chaiyawat, P.3    Phueaouan, T.4    Charoenwattanasatien, R.5    Chokchaichamnankit, D.6
  • 11
    • 84863741439 scopus 로고    scopus 로고
    • Chromatin isolation by RNA purification (ChIRP)
    • doi: 10.3791/3912
    • Chu, C., Quinn, J., and Chang, H. (2011). Chromatin isolation by RNA purification (ChIRP). J. Vis. Exp. 61:e3912. doi: 10.3791/3912
    • (2011) J. Vis. Exp , vol.61
    • Chu, C.1    Quinn, J.2    Chang, H.3
  • 12
    • 84893414724 scopus 로고    scopus 로고
    • O-GlcNAcylation regulates EZH2 protein stability and function
    • doi: 10.1073/pnas.1323226111
    • Chu, C.-S., Lo, P.-W., Yeh, Y.-H., Hsu, P.-H., Peng, S.-H., Teng, Y.-C., et al. (2014). O-GlcNAcylation regulates EZH2 protein stability and function. Proc. Natl. Acad. Sci. U.S.A. 111, 1355-1360. doi: 10.1073/pnas.1323226111
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 1355-1360
    • Chu, C.-S.1    Lo, P.-W.2    Yeh, Y.-H.3    Hsu, P.-H.4    Peng, S.-H.5    Teng, Y.-C.6
  • 13
    • 0030034051 scopus 로고    scopus 로고
    • XIST RNA paints the inactive X chromosome at interphase: evidence for a novel RNA involved in nuclear/chromosome structure
    • doi: 10.1083/jcb.132.3.259
    • Clemson, C. M., McNeil, J. A., Willard, H. F., and Lawrence, J. B. (1996). XIST RNA paints the inactive X chromosome at interphase: evidence for a novel RNA involved in nuclear/chromosome structure. J. Cell Biol. 132, 259-275. doi: 10.1083/jcb.132.3.259
    • (1996) J. Cell Biol. , vol.132 , pp. 259-275
    • Clemson, C.M.1    McNeil, J.A.2    Willard, H.F.3    Lawrence, J.B.4
  • 14
    • 0035800086 scopus 로고    scopus 로고
    • Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II
    • doi: 10.1021/bi0027480
    • Comer, F., and Hart, G. (2001). Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II. Biochemistry 40, 7845-7852. doi: 10.1021/bi0027480
    • (2001) Biochemistry , vol.40 , pp. 7845-7852
    • Comer, F.1    Hart, G.2
  • 15
    • 7744228427 scopus 로고    scopus 로고
    • Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation
    • doi: 10.1016/j.devcel.2004.10.005
    • De Napoles, M., Mermoud, J. E., Wakao, R., Tang, Y. A., Endoh, M., Appanah, R., et al. (2004). Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation. Dev. Cell 7, 663-676. doi: 10.1016/j.devcel.2004.10.005
    • (2004) Dev. Cell , vol.7 , pp. 663-676
    • De Napoles, M.1    Mermoud, J.E.2    Wakao, R.3    Tang, Y.A.4    Endoh, M.5    Appanah, R.6
  • 16
    • 0033460319 scopus 로고    scopus 로고
    • Escapees on the X chromosome
    • doi: 10.1073/pnas.96.25.14180
    • Disteche, C. M. (1999). Escapees on the X chromosome. Proc. Natl. Acad. Sci. U.S.A. 96, 14180-14182. doi: 10.1073/pnas.96.25.14180
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 14180-14182
    • Disteche, C.M.1
  • 17
    • 84884310305 scopus 로고    scopus 로고
    • O-GlcNAcylation: a New Cancer Hallmark?
    • doi: 10.3389/fendo.2013.00099
    • Fardini, Y., Dehennaut, V., Lefebvre, T., and Issad, T. (2012). O-GlcNAcylation: a New Cancer Hallmark? Front. Endocrinol. 4:99. doi: 10.3389/fendo.2013.00099
    • (2012) Front. Endocrinol , vol.4 , pp. 99
    • Fardini, Y.1    Dehennaut, V.2    Lefebvre, T.3    Issad, T.4
  • 18
    • 67650076327 scopus 로고    scopus 로고
    • Essential role of the glycosyltransferase sxc/Ogt in polycomb repression
    • doi: 10.1126/science.1169727
    • Gambetta, M. C., Oktaba, K., and Müller, J. (2009). Essential role of the glycosyltransferase sxc/Ogt in polycomb repression. Science 325, 93-96. doi: 10.1126/science.1169727
    • (2009) Science , vol.325 , pp. 93-96
    • Gambetta, M.C.1    Oktaba, K.2    Müller, J.3
  • 19
    • 0020987354 scopus 로고
    • Mammalian X-chromosome inactivation
    • doi: 10.1146/annurev.ge.17.120183.001103
    • Gartler, S. M., and Riggs, A. D. (1983). Mammalian X-chromosome inactivation. Annu. Rev. Genet. 17, 155-190. doi: 10.1146/annurev.ge.17.120183.001103
    • (1983) Annu. Rev. Genet. , vol.17 , pp. 155-190
    • Gartler, S.M.1    Riggs, A.D.2
  • 20
    • 77955401818 scopus 로고    scopus 로고
    • GlcNAcylation plays an essential role in breast cancer metastasis
    • doi: 10.1158/0008-5472.CAN-09-1887
    • Gu, Y., Mi, W., Ge, Y., Liu, H., Fan, Q., Han, C., et al. (2010). GlcNAcylation plays an essential role in breast cancer metastasis. Cancer Res. 70, 6344-6351. doi: 10.1158/0008-5472.CAN-09-1887
    • (2010) Cancer Res. , vol.70 , pp. 6344-6351
    • Gu, Y.1    Mi, W.2    Ge, Y.3    Liu, H.4    Fan, Q.5    Han, C.6
  • 21
    • 0026795976 scopus 로고
    • Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase
    • Haltiwanger, R. S., Blomberg, M. A., and Hart, G. W. (1992). Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase. J. Biol. Chem. 267, 9005-9013.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9005-9013
    • Haltiwanger, R.S.1    Blomberg, M.A.2    Hart, G.W.3
  • 22
    • 0034854157 scopus 로고    scopus 로고
    • Glycan-dependent signaling: O-linked N-acetylglucosamine
    • doi: 10.1096/fj.01-0094rev
    • Hanover, J. (2001). Glycan-dependent signaling: O-linked N-acetylglucosamine. FASEB J. 15, 1865-1876. doi: 10.1096/fj.01-0094rev
    • (2001) FASEB J. , vol.15 , pp. 1865-1876
    • Hanover, J.1
  • 23
    • 77949295164 scopus 로고    scopus 로고
    • The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine
    • doi: 10.1016/j.bbagen.2009.07.017
    • Hanover, J. A., Krause, M. W., and Love, D. C. (2010). The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine. Biochim. Biophys. Acta 1800, 80-95. doi: 10.1016/j.bbagen.2009.07.017
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 80-95
    • Hanover, J.A.1    Krause, M.W.2    Love, D.C.3
  • 24
    • 84875923589 scopus 로고    scopus 로고
    • Overexpression of X-linked genes in T cells from women with lupus
    • doi: 10.1016/j.jaut.2012.12.006
    • Hewagama, A., Gorelik, G., Patel, D., Liyanarachchi, P., McCune, W. J., Somers, E., et al. (2013). Overexpression of X-linked genes in T cells from women with lupus. J. Autoimmun. 41, 60-71. doi: 10.1016/j.jaut.2012.12.006
    • (2013) J. Autoimmun. , vol.41 , pp. 60-71
    • Hewagama, A.1    Gorelik, G.2    Patel, D.3    Liyanarachchi, P.4    McCune, W.J.5    Somers, E.6
  • 25
    • 0037068358 scopus 로고    scopus 로고
    • Reactivating the expression of methylation silenced genes in human cancer
    • doi: 10.1038/sj.onc.1205602
    • Karpf, A. R., and Jones, D. A. (2002). Reactivating the expression of methylation silenced genes in human cancer. Oncogene 21, 5496-5503. doi: 10.1038/sj.onc.1205602
    • (2002) Oncogene , vol.21 , pp. 5496-5503
    • Karpf, A.R.1    Jones, D.A.2
  • 26
    • 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, W. G., and Hart, G. W. (1989). Glycosylation of chromosomal proteins: localization of O-linked N-acetylglucosamine in Drosophila chromatin. Cell 57, 243-251. doi: 10.1016/0092-8674(89)90962-8
    • (1989) Cell , vol.57 , pp. 243-251
    • Kelly, W.G.1    Hart, G.W.2
  • 27
    • 0030959555 scopus 로고    scopus 로고
    • Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats
    • doi: 10.1074/jbc.272.14.9308
    • Kreppel, L., Blomberg, M., and Hart, G. (1997). Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats. J. Biol. Chem. 272, 9308-9315. doi: 10.1074/jbc.272.14.9308
    • (1997) J. Biol. Chem. , vol.272 , pp. 9308-9315
    • Kreppel, L.1    Blomberg, M.2    Hart, G.3
  • 28
    • 84858148966 scopus 로고    scopus 로고
    • Gene expression of O-GlcNAc cycling enzymes in human breast cancers
    • doi: 10.1007/s10238-011-0138-5
    • Krzeslak, A., Forma, E., Bernaciak, M., Romanowicz, H., and Brys, M. (2012). Gene expression of O-GlcNAc cycling enzymes in human breast cancers. Clin. Exp. Med. 12, 61-65. doi: 10.1007/s10238-011-0138-5
    • (2012) Clin. Exp. Med. , vol.12 , pp. 61-65
    • Krzeslak, A.1    Forma, E.2    Bernaciak, M.3    Romanowicz, H.4    Brys, M.5
  • 29
    • 0030895047 scopus 로고    scopus 로고
    • Long-range cis effects of ectopic X-inactivation centres on a mouse autosome
    • doi: 10.1038/386275a0
    • Lee, J. T., and Jaenisch, R. (1997). Long-range cis effects of ectopic X-inactivation centres on a mouse autosome. Nature 386, 275-279. doi: 10.1038/386275a0
    • (1997) Nature , vol.386 , pp. 275-279
    • Lee, J.T.1    Jaenisch, R.2
  • 30
    • 0141788582 scopus 로고    scopus 로고
    • Novel perspective: focusing on the X chromosome in reproductive cancers
    • doi: 10.1081/CNV-120022385
    • Liao, D. J., Du, Q., Yu, B. W., Grignon, D., and Sarkar, F. H. (2003). Novel perspective: focusing on the X chromosome in reproductive cancers. Cancer Invest. 21, 641-658. doi: 10.1081/CNV-120022385
    • (2003) Cancer Invest. , vol.21 , pp. 641-658
    • Liao, D.J.1    Du, Q.2    Yu, B.W.3    Grignon, D.4    Sarkar, F.H.5
  • 31
    • 38749117957 scopus 로고    scopus 로고
    • Dosage compensation in the mouse balances up-regulation and silencing of X-linked genes
    • doi: 10.1371/journal.pbio.0050326
    • Lin, H., Gupta, V., Vermilyea, M. D., Falciani, F., Lee, J. T., O'Neill, L. P., et al. (2007). Dosage compensation in the mouse balances up-regulation and silencing of X-linked genes. PLoS Biol. 5:e326. doi: 10.1371/journal.pbio.0050326
    • (2007) PLoS. Biol , vol.5
    • Lin, H.1    Gupta, V.2    Vermilyea, M.D.3    Falciani, F.4    Lee, J.T.5    O'Neill, L.P.6
  • 32
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • doi: 10.1006/meth.2001.1262
    • Livak, K. J., and Schmittgen, T. D. (2001). Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 25, 402-408. doi: 10.1006/meth.2001.1262
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 33
    • 77952171341 scopus 로고    scopus 로고
    • Dynamic O-GlcNAc cycling at promoters of Caenorhabditis elegans genes regulating longevity, stress, and immunity
    • doi: 10.1073/pnas.0911857107
    • Love, D., Ghosh, S., Mondoux, M., Fukushige, T., Wang, P., Wilson, M., et al. (2010). Dynamic O-GlcNAc cycling at promoters of Caenorhabditis elegans genes regulating longevity, stress, and immunity. Proc. Natl. Acad. Sci. U.S.A. 107, 7413-7418. doi: 10.1073/pnas.0911857107
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 7413-7418
    • Love, D.1    Ghosh, S.2    Mondoux, M.3    Fukushige, T.4    Wang, P.5    Wilson, M.6
  • 34
    • 0030944105 scopus 로고    scopus 로고
    • O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats
    • Lubas, W., Frank, D., Krause, M., and Hanover, J. (1997). O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats. J. Biol. Chem. 272, 9316-9324
    • (1997) J. Biol. Chem , vol.272 , pp. 9316-9324
    • Lubas, W.1    Frank, D.2    Krause, M.3    Hanover, J.4
  • 35
    • 7144223296 scopus 로고
    • Gene action in the X-chromosome of the mouse (Mus musculus L.)
    • doi: 10.1038/190372a0
    • Lyon, M. F. (1961). Gene action in the X-chromosome of the mouse (Mus musculus L.). Nature 190, 372-373. doi: 10.1038/190372a0
    • (1961) Nature , vol.190 , pp. 372-373
    • Lyon, M.F.1
  • 36
    • 0030579607 scopus 로고    scopus 로고
    • X-chromosome inactivation. Pinpointing the centre
    • Lyon, M. F. (1996). X-chromosome inactivation. Pinpointing the centre. Nature 379, 116-117.
    • (1996) Nature , vol.379 , pp. 116-117
    • Lyon, M.F.1
  • 37
    • 84903767444 scopus 로고    scopus 로고
    • O-GlcNAc profiling: from proteins to proteomes
    • doi: 10.1186/1559-0275-11-8
    • Ma, J., and Hart, G. W. (2014). O-GlcNAc profiling: from proteins to proteomes. Clin. Proteomics 11:8. doi: 10.1186/1559-0275-11-8
    • (2014) Clin. Proteomics , vol.11 , pp. 8
    • Ma, J.1    Hart, G.W.2
  • 38
    • 0031044166 scopus 로고    scopus 로고
    • XIST-deficient mice are defective in dosage compensation but not spermatogenesis
    • doi: 10.1101/gad.11.2.156
    • Marahrens, Y., Panning, B., Dausman, J., Strauss, W., and Jaenisch, R. (1997). XIST-deficient mice are defective in dosage compensation but not spermatogenesis. Genes Dev. 11, 156-166. doi: 10.1101/gad.11.2.156
    • (1997) Genes Dev. , vol.11 , pp. 156-166
    • Marahrens, Y.1    Panning, B.2    Dausman, J.3    Strauss, W.4    Jaenisch, R.5
  • 39
    • 84875224972 scopus 로고    scopus 로고
    • A sweet TET-à-tête-synergy of TET proteins and O-GlcNAc transferase in transcription
    • doi: 10.1038/emboj.2013.26
    • Mariappa, D., Pathak, S., and van Aalten, D. M. (2013). A sweet TET-à-tête-synergy of TET proteins and O-GlcNAc transferase in transcription. EMBO J. 32, 612-613. doi: 10.1038/emboj.2013.26
    • (2013) EMBO J. , vol.32 , pp. 612-613
    • Mariappa, D.1    Pathak, S.2    van Aalten, D.M.3
  • 40
    • 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., and Traxinger, R. R. (1991). 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 266, 4706-4712.
    • (1991) J. Biol. Chem , vol.266 , pp. 4706-4712
    • Marshall, S.1    Bacote, V.2    Traxinger, R.R.3
  • 41
    • 0022762876 scopus 로고
    • Structural analysis of the X-linked gene encoding human glucose 6-phosphate dehydrogenase
    • Martini, G., Toniolo, D., Vulliamy, T., Luzzatto, L., Dono, R., Viglietto, G., et al. (1986). Structural analysis of the X-linked gene encoding human glucose 6-phosphate dehydrogenase. EMBO J. 5, 1849-1855.
    • (1986) EMBO J. , vol.5 , pp. 1849-1855
    • Martini, G.1    Toniolo, D.2    Vulliamy, T.3    Luzzatto, L.4    Dono, R.5    Viglietto, G.6
  • 42
    • 0033611106 scopus 로고    scopus 로고
    • Histone macroH2A1.2 relocates to the inactive X chromosome after initiation and propagation of X-inactivation
    • doi: 10.1083/jcb.147.7.1399
    • Mermoud, J. E., Costanzi, C., Pehrson, J. R., and Brockdorff, N. (1999). Histone macroH2A1.2 relocates to the inactive X chromosome after initiation and propagation of X-inactivation. J. Cell Biol. 147, 1399-1408. doi: 10.1083/jcb.147.7.1399
    • (1999) J. Cell Biol. , vol.147 , pp. 1399-1408
    • Mermoud, J.E.1    Costanzi, C.2    Pehrson, J.R.3    Brockdorff, N.4
  • 43
    • 79959334683 scopus 로고    scopus 로고
    • Polycomb repressive complex 2 is necessary for the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells
    • doi: 10.1073/pnas.1019289108
    • Myers, S. A., Panning, B., and Burlingame, A. L. (2011). Polycomb repressive complex 2 is necessary for the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells. Proc. Natl. Acad. Sci. U.S.A. 108, 9490-9495. doi: 10.1073/pnas.1019289108
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 9490-9495
    • Myers, S.A.1    Panning, B.2    Burlingame, A.L.3
  • 44
    • 84906216635 scopus 로고    scopus 로고
    • X Marks the Spot: Does it matter that O-GlcNAc Transferase is an X-linked gene?
    • doi: 10.1016/j.bbrc.2014.06.068. [Epub ahead of print].
    • Olivier-Van Stichelen, S., Abramowitz, L. K., and Hanover, J. A. (2014). X Marks the Spot: Does it matter that O-GlcNAc Transferase is an X-linked gene? Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2014.06.068. [Epub ahead of print].
    • (2014) Biochem. Biophys. Res. Commun
    • Olivier-Van Stichelen, S.1    Abramowitz, L.K.2    Hanover, J.A.3
  • 45
    • 77953713601 scopus 로고    scopus 로고
    • Modulation of transcription factor function by O-GlcNAc modification
    • doi: 10.1016/j.bbagrm.2010.02.005
    • Ozcan, S., Andrali, S. S., and Cantrell, J. E. L. (2010). Modulation of transcription factor function by O-GlcNAc modification. Biochim. Biophys. Acta 1799, 353-364. doi: 10.1016/j.bbagrm.2010.02.005
    • (2010) Biochim. Biophys. Acta , vol.1799 , pp. 353-364
    • Ozcan, S.1    Andrali, S.S.2    Cantrell, J.E.L.3
  • 46
    • 33847028789 scopus 로고    scopus 로고
    • BRCA1 does not paint the inactive X to localize XIST RNA but may contribute to broad changes in cancer that impact XIST and Xi heterochromatin
    • doi: 10.1002/jcb.21188
    • Pageau, G. J., Hall, L. L., and Lawrence, J. B. (2007). BRCA1 does not paint the inactive X to localize XIST RNA but may contribute to broad changes in cancer that impact XIST and Xi heterochromatin. J. Cell Biochem. 100, 835-850. doi: 10.1002/jcb.21188
    • (2007) J. Cell Biochem. , vol.100 , pp. 835-850
    • Pageau, G.J.1    Hall, L.L.2    Lawrence, J.B.3
  • 47
    • 65249115919 scopus 로고    scopus 로고
    • Dynamic changes in paternal X-chromosome activity during imprinted X-chromosome inactivation in mice
    • doi: 10.1073/pnas.0810683106
    • Patrat, C., Okamoto, I., Diabangouaya, P., Vialon, V., Le Baccon, P., Chow, J., et al. (2009). Dynamic changes in paternal X-chromosome activity during imprinted X-chromosome inactivation in mice. Proc. Natl. Acad. Sci. U.S.A. 106, 5198-5203. doi: 10.1073/pnas.0810683106
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 5198-5203
    • Patrat, C.1    Okamoto, I.2    Diabangouaya, P.3    Vialon, V.4    Le Baccon, P.5    Chow, J.6
  • 48
    • 0036338205 scopus 로고    scopus 로고
    • Histone H3 lysine 9 methylation is an epigenetic imprint of facultative heterochromatin
    • doi: 10.1038/ng789
    • Peters, A. H. F. M., Mermoud, J. E., O'Carroll, D., Pagani, M., Schweizer, D., Brockdorff, N., et al. (2002). Histone H3 lysine 9 methylation is an epigenetic imprint of facultative heterochromatin. Nat. Genet. 30, 77-80. doi: 10.1038/ng789
    • (2002) Nat. Genet. , vol.30 , pp. 77-80
    • Peters, A.H.F.M.1    Mermoud, J.E.2    O'Carroll, D.3    Pagani, M.4    Schweizer, D.5    Brockdorff, N.6
  • 49
    • 0242668706 scopus 로고    scopus 로고
    • Role of histone H3 lysine 27 methylation in X inactivation
    • doi: 10.1126/science.1084274
    • Plath, K., Fang, J., Mlynarczyk-Evans, S. K., Cao, R., Worringer, K. A., Wang, H., et al. (2003). Role of histone H3 lysine 27 methylation in X inactivation. Science 300, 131-135. doi: 10.1126/science.1084274
    • (2003) Science , vol.300 , pp. 131-135
    • Plath, K.1    Fang, J.2    Mlynarczyk-Evans, S.K.3    Cao, R.4    Worringer, K.A.5    Wang, H.6
  • 50
    • 84863610013 scopus 로고    scopus 로고
    • Evidence of the involvement of O-GlcNAc-modified human RNA polymerase II CTD in transcription in vitro and in vivo
    • doi: 10.1074/jbc.M111.330910
    • Ranuncolo, S. M., Ghosh, S., Hanover, J. A., Hart, G. W., and Lewis, B. A. (2012). Evidence of the involvement of O-GlcNAc-modified human RNA polymerase II CTD in transcription in vitro and in vivo. J. Biol. Chem. 287, 23549-23561. doi: 10.1074/jbc.M111.330910
    • (2012) J. Biol. Chem. , vol.287 , pp. 23549-23561
    • Ranuncolo, S.M.1    Ghosh, S.2    Hanover, J.A.3    Hart, G.W.4    Lewis, B.A.5
  • 51
    • 78650447665 scopus 로고    scopus 로고
    • Beta-N-acetylglucosamine (O-GlcNAc) is part of the histone code
    • doi: 10.1073/pnas.1009023107
    • Sakabe, K., Wang, Z., and Hart, G. W. (2010). Beta-N-acetylglucosamine (O-GlcNAc) is part of the histone code. Proc. Natl. Acad. Sci. U.S.A. 107, 19915-19920. doi: 10.1073/pnas.1009023107
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 19915-19920
    • Sakabe, K.1    Wang, Z.2    Hart, G.W.3
  • 52
    • 0034705030 scopus 로고    scopus 로고
    • The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny
    • doi: 10.1073/pnas.100471497
    • Shafi, R., Iyer, S. P., Ellies, L. G., O'Donnell, N., Marek, K. W., Chui, D., et al. (2000). The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny. Proc. Natl. Acad. Sci. U.S.A. 97, 5735-5739. doi: 10.1073/pnas.100471497
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 5735-5739
    • Shafi, R.1    Iyer, S.P.2    Ellies, L.G.3    O'Donnell, N.4    Marek, K.W.5    Chui, D.6
  • 53
    • 69449092638 scopus 로고    scopus 로고
    • Drosophila O-GlcNAc transferase (OGT) is encoded by the Polycomb group (PcG) gene, super sex combs (sxc)
    • doi: 10.1073/pnas.0904638106
    • Sinclair, D. A. R., Syrzycka, M., Macauley, M. S., Rastgardani, T., Komljenovic, I., Vocadlo, D. J., et al. (2009). Drosophila O-GlcNAc transferase (OGT) is encoded by the Polycomb group (PcG) gene, super sex combs (sxc). Proc. Natl. Acad. Sci. U.S.A. 106, 13427-13432. doi: 10.1073/pnas.0904638106
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 13427-13432
    • Sinclair, D.A.R.1    Syrzycka, M.2    Macauley, M.S.3    Rastgardani, T.4    Komljenovic, I.5    Vocadlo, D.J.6
  • 54
    • 0035964998 scopus 로고    scopus 로고
    • Increased N-acetyl-beta-glucosaminidase activity in primary breast carcinomas corresponds to a decrease in N-acetylglucosamine containing proteins
    • doi: 10.1016/S0925-4439(01)00067-9
    • Slawson, C., Pidala, J., and Potter, R. (2001). Increased N-acetyl-beta-glucosaminidase activity in primary breast carcinomas corresponds to a decrease in N-acetylglucosamine containing proteins. Biochim. Biophys. Acta 1537, 147-157. doi: 10.1016/S0925-4439(01)00067-9
    • (2001) Biochim. Biophys. Acta , vol.1537 , pp. 147-157
    • Slawson, C.1    Pidala, J.2    Potter, R.3
  • 55
    • 0021677212 scopus 로고
    • Cytological mapping of the human glucose-6-phosphate dehydrogenase gene distal to the fragile-X site suggests a high rate of meiotic recombination across this site
    • doi: 10.1073/pnas.81.24.7855
    • Szabo, P., Purrello, M., Rocchi, M., Archidiacono, N., Alhadeff, B., Filippi, G., et al. (1984). Cytological mapping of the human glucose-6-phosphate dehydrogenase gene distal to the fragile-X site suggests a high rate of meiotic recombination across this site. Proc. Natl. Acad. Sci. U.S.A. 81, 7855-7859. doi: 10.1073/pnas.81.24.7855
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 7855-7859
    • Szabo, P.1    Purrello, M.2    Rocchi, M.3    Archidiacono, N.4    Alhadeff, B.5    Filippi, G.6
  • 56
    • 0021280147 scopus 로고
    • Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc
    • Torres, C. R., and Hart, G. W. (1984). Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc. J. Biol. Chem 259, 3308-3317.
    • (1984) J. Biol. Chem , vol.259 , pp. 3308-3317
    • Torres, C.R.1    Hart, G.W.2
  • 57
    • 77951794067 scopus 로고    scopus 로고
    • Global survey of escape from X inactivation by RNA-sequencing in mouse
    • doi: 10.1101/gr.103200.109
    • Yang, F., Babak, T., Shendure, J., and Disteche, C. M. (2010). Global survey of escape from X inactivation by RNA-sequencing in mouse. Genome Res. 20, 614-622. doi: 10.1101/gr.103200.109
    • (2010) Genome Res. , vol.20 , pp. 614-622
    • Yang, F.1    Babak, T.2    Shendure, J.3    Disteche, C.M.4


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