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Volumn 287, Issue 19, 2012, Pages 15395-15408

Insights into O-linked N-acetylglucosamine (O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates

Author keywords

[No Author keywords available]

Indexed keywords

DIVERSE PROTEINS; DYNAMIC EQUILIBRIA; FINE TUNING; IN-VITRO; KINETIC ACTIVITY; KINETIC ANALYSIS; KINETIC EVIDENCE; KINETIC STUDY; MODIFIED PROTEINS; N-ACETYLGLUCOSAMINE; O-LINKED; PROTEIN SUBSTRATE; SPECIFIC ACTIVITY; TARGET PROTEINS; UPPER LIMITS;

EID: 84860871127     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.310664     Document Type: Article
Times cited : (92)

References (56)
  • 1
    • 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
  • 2
    • 0029670515 scopus 로고    scopus 로고
    • Dynamic O-GlcNAcylation of the small heat shock protein α B-crystallin
    • Roquemore, E. P., Chevrier, M. R., Cotter, R. J., and Hart, G. W. (1996) Dynamic O-GlcNAcylation of the small heat shock protein α B-crystallin. Biochemistry 35, 3578-3586
    • (1996) Biochemistry , vol.35 , pp. 3578-3586
    • Roquemore, E.P.1    Chevrier, M.R.2    Cotter, R.J.3    Hart, G.W.4
  • 3
    • 0037166352 scopus 로고    scopus 로고
    • Dynamic interplay between O-glycosylation and O-phosphorylation of nucleocytoplasmic proteins: Alternative glycosylation/phosphorylation of Thr-58, a known mutational hot spot of c-Myc in lymphomas, is regulated by mitogens
    • DOI 10.1074/jbc.M201729200
    • Kamemura, K., Hayes, B. K., Comer, F. I., and Hart, G. W. (2002) Dynamic interplay between O-glycosylation and O-phosphorylation of nucleocytoplasmic proteins. Alternative glycosylation/phosphorylation of Thr-58, a known mutational hot spot of c-Myc in lymphomas, is regulated by mitogens. J. Biol. Chem. 277, 19229-19235 (Pubitemid 34952491)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.21 , pp. 19229-19235
    • Kamemura, K.1    Hayes, B.K.2    Comer, F.I.3    Hart, G.W.4
  • 4
    • 69249155637 scopus 로고    scopus 로고
    • Regulation of calcium/calmodulin-dependent kinase IV by O-GlcNAc modification
    • Dias, W. B., Cheung, W. D., Wang, Z., and Hart, G. W. (2009) Regulation of calcium/calmodulin-dependent kinase IV by O-GlcNAc modification. J. Biol. Chem. 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
  • 5
    • 33749160125 scopus 로고    scopus 로고
    • Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability
    • DOI 10.1038/ncb1470, PII NCB1470
    • Yang, W. H., Kim, J. E., Nam, H. W., Ju, J. W., Kim, H. S., Kim, Y. S., and Cho, J. W. (2006) Modification of p53 with O-linkedN-acetylglucosamine regulates p53 activity and stability. Nat. Cell Biol. 8, 1074-1083 (Pubitemid 44473602)
    • (2006) Nature Cell Biology , vol.8 , Issue.10 , pp. 1074-1083
    • Yang, W.H.1    Kim, J.E.2    Nam, H.W.3    Ju, J.W.4    Kim, H.S.5    Kim, Y.S.6    Cho, J.W.7
  • 7
    • 67650076327 scopus 로고    scopus 로고
    • Essential role of the glycosyltransferase sxc/Ogt in polycomb repression
    • Gambetta, M. C., Oktaba, K., and Müller, J. (2009) Essential role of the glycosyltransferase sxc/Ogt in polycomb repression. Science 325, 93-96
    • (2009) Science , vol.325 , pp. 93-96
    • Gambetta, M.C.1    Oktaba, K.2    Müller, J.3
  • 10
    • 27144515984 scopus 로고    scopus 로고
    • Role of O-linked β-N-acetylglucosamine modification in the subcellular distribution of alpha4 phosphoprotein and Sp1 in rat lymphoma cells
    • DOI 10.1002/jcb.20508
    • Dauphinee, S. M., Ma, M., and Too, C. K. (2005) Role of O-linked β-Nacetylglucosamine modification in the subcellular distribution of α4 phosphoprotein and Sp1 in rat lymphoma cells. J. Cell Biochem. 96, 579-588 (Pubitemid 41504655)
    • (2005) Journal of Cellular Biochemistry , vol.96 , Issue.3 , pp. 579-588
    • Dauphinee, S.M.1    Ma, M.2    Too, C.K.L.3
  • 15
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • DOI 10.1126/science.1075762
    • Manning, G., Whyte, D. B., Martinez, R., Hunter, T., and Sudarsanam, S. (2002) The protein kinase complement of the human genome. Science 298, 1912-1934 (Pubitemid 35425239)
    • (2002) Science , vol.298 , Issue.5600 , pp. 1912-1934
    • Manning, G.1    Whyte, D.B.2    Martinez, R.3    Hunter, T.4    Sudarsanam, S.5
  • 16
    • 34247583996 scopus 로고    scopus 로고
    • Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins
    • DOI 10.1038/nature05815, PII NATURE05815
    • Hart, G. W., Housley, M. P., and Slawson, C. (2007) Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins. Nature 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
  • 17
    • 0037440370 scopus 로고    scopus 로고
    • Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc transferase encoded by a single mammalian gene
    • DOI 10.1016/S0003-9861(02)00578-7, PII S0003986102005787
    • Hanover, J. A., Yu, S., Lubas, W. B., Shin, S. H., Ragano-Caracciola, M., Kochran, J., and Love, D. C. (2003) Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc transferase encoded by a single mammalian gene. Arch. Biochem. Biophys. 409, 287-297 (Pubitemid 36259596)
    • (2003) Archives of Biochemistry and Biophysics , vol.409 , Issue.2 , pp. 287-297
    • Hanover, J.A.1    Yu, S.2    Lubas, W.B.3    Shin, S.-H.4    Ragano-Caracciola, M.5    Kochran, J.6    Love, D.C.7
  • 18
    • 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. K., Blomberg, M. A., and Hart, G. W. (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 (Pubitemid 27154943)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.14 , pp. 9308-9315
    • Kreppel, L.K.1    Blomberg, M.A.2    Hart, G.W.3
  • 19
    • 0030944105 scopus 로고    scopus 로고
    • O-linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats
    • DOI 10.1074/jbc.272.14.9316
    • Lubas, W. A., Frank, D. W., Krause, M., and Hanover, J. A. (1997) O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats. J. Biol. Chem. 272, 9316-9324 (Pubitemid 27154944)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.14 , pp. 9316-9324
    • Lubas, W.A.1    Frank, D.W.2    Krause, M.3    Hanover, J.A.4
  • 20
    • 0028085881 scopus 로고
    • Purification and characterization of an O-GlcNAc-selective N-acetyl-β-D-glucosaminidase from rat spleen cytosol
    • Dong, D. L., and Hart, G. W. (1994) Purification and characterization of an O-GlcNAc-selective N-acetyl-β-D-glucosaminidase from rat spleen cytosol. J. Biol. Chem. 269, 19321-19330
    • (1994) J. Biol. Chem. , vol.269 , pp. 19321-19330
    • Dong, D.L.1    Hart, G.W.2
  • 21
    • 0035971182 scopus 로고    scopus 로고
    • Dynamic O-glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a neutral, cytosolic β-N-acetylglucosaminidase from human brain
    • Gao, Y., Wells, L., Comer, F. I., Parker, G. J., and Hart, G. W. (2001) Dynamic O-glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a neutral, cytosolic β-N-acetylglucosaminidase from human brain. J. Biol. Chem. 276, 9838-9845
    • (2001) J. Biol. Chem. , vol.276 , pp. 9838-9845
    • Gao, Y.1    Wells, L.2    Comer, F.I.3    Parker, G.J.4    Hart, G.W.5
  • 22
    • 33646890020 scopus 로고    scopus 로고
    • Disrupting the enzyme complex regulating O-GlcNAcylation blocks signaling and development
    • DOI 10.1093/glycob/cwj096
    • Whisenhunt, T. R., Yang, X., Bowe, D. B., Paterson, A. J., Van Tine, B. A., and Kudlow, J. E. (2006) Disrupting the enzyme complex regulating O-GlcNAcylation blocks signaling and development. Glycobiology 16, 551-563 (Pubitemid 43779050)
    • (2006) Glycobiology , vol.16 , Issue.6 , pp. 551-563
    • Whisenhunt, T.R.1    Yang, X.2    Bowe, D.B.3    Paterson, A.J.4    Van Tine, B.A.5    Kudlow, J.E.6
  • 23
    • 57749088688 scopus 로고    scopus 로고
    • O-Linked β-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins
    • Cheung, W. D., Sakabe, K., Housley, M. P., Dias, W. B., and Hart, G. W. (2008) O-Linked β-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins. J. Biol. Chem. 283, 33935-33941
    • (2008) J. Biol. Chem. , vol.283 , pp. 33935-33941
    • Cheung, W.D.1    Sakabe, K.2    Housley, M.P.3    Dias, W.B.4    Hart, G.W.5
  • 24
    • 79955475591 scopus 로고    scopus 로고
    • Denitrosylation of S-nitrosylated OGT is triggered in LPS-stimulated innate immune response
    • Ryu, I. H., and Do, S. I. (2011) Denitrosylation of S-nitrosylated OGT is triggered in LPS-stimulated innate immune response. Biochem. Biophys. Res. Commun. 408, 52-57
    • (2011) Biochem. Biophys. Res. Commun. , vol.408 , pp. 52-57
    • Ryu, I.H.1    Do, S.I.2
  • 25
    • 34250309514 scopus 로고    scopus 로고
    • A high-throughput assay for O-GlcNAc transferase detects primary sequence preferences in peptide substrates
    • DOI 10.1016/j.bmcl.2007.05.008, PII S0960894X07005598
    • Leavy, T. M., and Bertozzi, C. R. (2007) A high-throughput assay for O-GlcNAc transferase detects primary sequence preferences in peptide substrates. Bioorg. Med. Chem. Lett. 17, 3851-3854 (Pubitemid 46920951)
    • (2007) Bioorganic and Medicinal Chemistry Letters , vol.17 , Issue.14 , pp. 3851-3854
    • Leavy, T.M.1    Bertozzi, C.R.2
  • 26
    • 0034646669 scopus 로고    scopus 로고
    • Functional expression of O-linked GLcNAc transferase. Domain structure and substrate specificity
    • DOI 10.1074/jbc.275.15.10983
    • Lubas, W. A., and Hanover, J. A. (2000) Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity. J. Biol. Chem. 275, 10983-10988 (Pubitemid 30212736)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.15 , pp. 10983-10988
    • Lubas, W.A.1    Hanover, J.A.2
  • 27
    • 0033527739 scopus 로고    scopus 로고
    • Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats
    • Kreppel, L. K., and Hart, G. W. (1999) Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats. J. Biol. Chem. 274, 32015-32022
    • (1999) J. Biol. Chem. , vol.274 , pp. 32015-32022
    • Kreppel, L.K.1    Hart, G.W.2
  • 29
    • 0028916742 scopus 로고
    • Analysis of nuclear pore protein p62 glycosylation
    • Lubas, W. A., Smith, M., Starr, C. M., and Hanover, J. A. (1995) Analysis of nuclear pore protein p62 glycosylation. Biochemistry 34, 1686-1694
    • (1995) Biochemistry , vol.34 , pp. 1686-1694
    • Lubas, W.A.1    Smith, M.2    Starr, C.M.3    Hanover, J.A.4
  • 31
    • 29044433378 scopus 로고    scopus 로고
    • O-GlcNAcase catalyzes cleavage of thioglycosides without general acid catalysis
    • DOI 10.1021/ja0567687
    • Macauley, M. S., Stubbs, K. A., and Vocadlo, D. J. (2005) O-GlcNAcase catalyzes cleavage of thioglycosides without general acid catalysis. J. Am. Chem. Soc. 127, 17202-17203 (Pubitemid 41791036)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.49 , pp. 17202-17203
    • Macauley, M.S.1    Stubbs, K.A.2    Vocadlo, D.J.3
  • 33
    • 79954437580 scopus 로고    scopus 로고
    • Mapping O-GlcNAc modification sites on Tau and generation of a site-specific O-GlcNAc Tau antibody
    • Yuzwa, S. A., Yadav, A. K., Skorobogatko, Y., Clark, T., Vosseller, K., and Vocadlo, D. J. (2011) Mapping O-GlcNAc modification sites on Tau and generation of a site-specific O-GlcNAc Tau antibody. Amino Acids 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
  • 34
    • 0011756062 scopus 로고    scopus 로고
    • Version 5, Erithacus Software Ltd., Horley, UK
    • Leatherbarrow, R. J. (2001) GraFit, Version 5, Erithacus Software Ltd., Horley, UK
    • (2001) GraFit
    • Leatherbarrow, R.J.1
  • 35
    • 0000588587 scopus 로고    scopus 로고
    • Selectin-carbohydrate interactions: From natural ligands to designed mimics
    • Simanek, E. E., McGarvey, G. J., Jablonowski, J. A., and Wong, C. H. (1998) Selectin-carbohydrate interactions. From natural ligands to designed mimics. Chem. Rev. 98, 833-862 (Pubitemid 128631443)
    • (1998) Chemical Reviews , vol.98 , Issue.2 , pp. 833-862
    • Simanek, E.E.1    McGarvey, G.J.2    Jablonowski, J.A.3    Wong, C.-H.4
  • 36
    • 33748579587 scopus 로고    scopus 로고
    • 16 Induce Different Conformational Disturbances to the N Terminus of Murine Estrogen Receptor β
    • DOI 10.1016/j.chembiol.2006.06.017, PII S1074552106002328
    • Chen, Y. X., Du, J. T., Zhou, L. X., Liu, X. H., Zhao, Y. F., Nakanishi, H., and Li, Y. M. (2006) Alternative O-GlcNAcylation/O-phosphorylation of Ser-16 induce different conformational disturbances to the N terminus of murine estrogen receptor β. Chem. Biol. 13, 937-944 (Pubitemid 44375169)
    • (2006) Chemistry and Biology , vol.13 , Issue.9 , pp. 937-944
    • Chen, Y.-X.1    Du, J.-T.2    Zhou, L.-X.3    Liu, X.-H.4    Zhao, Y.-F.5    Nakanishi, H.6    Li, Y.-M.7
  • 37
    • 0031573567 scopus 로고    scopus 로고
    • High-performance liquid chromatographic analysis of complexN-linked glycans derivatized with 2-aminoacridone
    • Okafo, G., Langridge, J., North, S., Organ, A., West, A., Morris, M., and Camilleri, P. (1997) High-performance liquid chromatographic analysis of complexN-linked glycans derivatized with 2-aminoacridone. Anal. Chem. 69, 4985-4993
    • (1997) Anal. Chem. , vol.69 , pp. 4985-4993
    • Okafo, G.1    Langridge, J.2    North, S.3    Organ, A.4    West, A.5    Morris, M.6    Camilleri, P.7
  • 39
    • 0036091929 scopus 로고    scopus 로고
    • Production of O-GlcNAc modified recombinant proteins in Escherichia coli
    • Lim, K. H., Ha, C. H., and Chang, H. I. (2002) Production of O-GlcNAc modified recombinant proteins in Escherichia coli. J. Microbiol. Biotechnol. 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
  • 40
    • 0035876021 scopus 로고    scopus 로고
    • Characterization of a mouse monoclonal antibody specific for O-linked N-acetylglucosamine
    • DOI 10.1006/abio.2001.5132
    • Comer, F. I., Vosseller, K., Wells, L., Accavitti, M. A., and Hart, G. W. (2001) Characterization of a mouse monoclonal antibody specific for O-linked N-acetylglucosamine. Anal. Biochem. 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
  • 41
    • 33646159532 scopus 로고    scopus 로고
    • Recombinant O-GlcNAc transferase isoforms. Identification ofO-GlcNAcase, Yes tyrosine kinase, and Tau as isoform-specific substrates
    • Lazarus, B. D., Love, D. C., and Hanover, J. A. (2006) Recombinant O-GlcNAc transferase isoforms. Identification ofO-GlcNAcase, Yes tyrosine kinase, and Tau as isoform-specific substrates. Glycobiology 16, 415-421
    • (2006) Glycobiology , vol.16 , pp. 415-421
    • Lazarus, B.D.1    Love, D.C.2    Hanover, J.A.3
  • 42
    • 33645226771 scopus 로고    scopus 로고
    • Identification of Asp-174 and Asp-175 as the key catalytic residues of human O-GlcNAcase by functional analysis of site-directed mutants
    • Cetinbas, N., Macauley, M. S., Stubbs, K. A., Drapala, R., and Vocadlo, D. J. (2006) Identification of Asp-174 and Asp-175 as the key catalytic residues of human O-GlcNAcase by functional analysis of site-directed mutants. Biochemistry 45, 3835-3844
    • (2006) Biochemistry , vol.45 , pp. 3835-3844
    • Cetinbas, N.1    Macauley, M.S.2    Stubbs, K.A.3    Drapala, R.4    Vocadlo, D.J.5
  • 44
    • 4744341309 scopus 로고    scopus 로고
    • The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin α
    • DOI 10.1038/nsmb833
    • Jínek, M., Rehwinkel, J., Lazarus, B. D., Izaurralde, E., Hanover, J. A., and Conti, E. (2004) The superhelical TPR-repeat domain ofO-linked GlcNAc transferase exhibits structural similarities to importin α. Nat. Struct. Mol. Biol. 11, 1001-1007 (Pubitemid 39315305)
    • (2004) Nature Structural and Molecular Biology , vol.11 , Issue.10 , pp. 1001-1007
    • Jinek, M.1    Rehwinkel, J.2    Lazarus, B.D.3    Izaurralde, E.4    Hanover, J.A.5    Conti, E.6
  • 45
    • 79251611901 scopus 로고    scopus 로고
    • Structure of human O-GlcNAc transferase and its complex with a peptide substrate
    • Lazarus, M. B., Nam, Y., Jiang, J., Sliz, P., and Walker, S. (2011) Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature 469, 564-567
    • (2011) Nature , vol.469 , pp. 564-567
    • Lazarus, M.B.1    Nam, Y.2    Jiang, J.3    Sliz, P.4    Walker, S.5
  • 46
    • 33645735070 scopus 로고    scopus 로고
    • Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis
    • Rao, F. V., Dorfmueller, H. C., Villa, F., Allwood, M., Eggleston, I. M., and van Aalten, D. M. (2006) Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis. EMBO J. 25, 1569-1578
    • (2006) EMBO J. , vol.25 , pp. 1569-1578
    • Rao, F.V.1    Dorfmueller, H.C.2    Villa, F.3    Allwood, M.4    Eggleston, I.M.5    Van Aalten, D.M.6
  • 47
  • 48
    • 70349388222 scopus 로고    scopus 로고
    • Probing synergy between two catalytic strategies in the glycoside hydrolase O-GlcNAcase using multiple linear free energy relationships
    • Greig, I. R., Macauley, M. S., Williams, I. H., and Vocadlo, D. J. (2009) Probing synergy between two catalytic strategies in the glycoside hydrolase O-GlcNAcase using multiple linear free energy relationships. J. Am. Chem. Soc. 131, 13415-13422
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 13415-13422
    • Greig, I.R.1    Macauley, M.S.2    Williams, I.H.3    Vocadlo, D.J.4
  • 49
    • 4143074732 scopus 로고    scopus 로고
    • Dynamic actions of glucose and glucosamine on hexosamine biosynthesis in isolated adipocytes: Differential effects on glucosamine 6-phosphate, UDP-N-acetylglucosamine, and ATP levels
    • DOI 10.1074/jbc.M404133200
    • Marshall, S., Nadeau, O., and Yamasaki, K. (2004) Dynamic actions of glucose and glucosamine on hexosamine biosynthesis in isolated adipocytes. Differential effects on glucosamine 6-phosphate, UDP-N-acetylglucosamine, and ATP levels. J. Biol. Chem. 279, 35313-35319 (Pubitemid 39100529)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.34 , pp. 35313-35319
    • Marshall, S.1    Nadeau, O.2    Yamasaki, K.3
  • 50
    • 63649085232 scopus 로고    scopus 로고
    • Up-regulation of O-GlcNAc transferase with glucose deprivation in HepG2 cells is mediated by decreased hexosamine pathway flux
    • Taylor, R. P., Geisler, T. S., Chambers, J. H., and McClain, D. A. (2009) Up-regulation of O-GlcNAc transferase with glucose deprivation in HepG2 cells is mediated by decreased hexosamine pathway flux. J. Biol. Chem. 284, 3425-3432
    • (2009) J. Biol. Chem. , vol.284 , pp. 3425-3432
    • Taylor, R.P.1    Geisler, T.S.2    Chambers, J.H.3    McClain, D.A.4
  • 51
    • 0042090275 scopus 로고    scopus 로고
    • Roles of the Tetratricopeptide Repeat Domain in O-GlcNAc Transferase Targeting and Protein Substrate Specificity
    • DOI 10.1074/jbc.M300036200
    • Iyer, S. P., and Hart, G. W. (2003) Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity. J. Biol. Chem. 278, 24608-24616 (Pubitemid 37548614)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.27 , pp. 24608-24616
    • Iyer, S.P.N.1    Hart, G.W.2
  • 52
    • 77955865876 scopus 로고    scopus 로고
    • Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags
    • Rexach, J. E., Rogers, C. J., Yu, S. H., Tao, J., Sun, Y. E., and Hsieh-Wilson, L. C. (2010) Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags. Nat. Chem. Biol. 6, 645-651
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 645-651
    • Rexach, J.E.1    Rogers, C.J.2    Yu, S.H.3    Tao, J.4    Sun, Y.E.5    Hsieh-Wilson, L.C.6
  • 53
    • 0023225084 scopus 로고
    • Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine
    • DOI 10.1083/jcb.104.5.1157
    • Holt, G. D., Snow, C. M., Senior, A., Haltiwanger, R. S., Gerace, L., and Hart, G. W. (1987) Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine. J. Cell Biol. 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
  • 54
    • 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., and Hart, G. W. (2007) Dynamic interplay between O-linked N-acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation. Mol. Cell Proteomics 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
  • 55
    • 52949123249 scopus 로고    scopus 로고
    • Cross-talk between GlcNAcylation and phosphorylation. Site-specific phosphorylation dynamics in response to globally elevated O-GlcNAc
    • Wang, Z., Gucek, M., and Hart, G. W. (2008) Cross-talk between GlcNAcylation and phosphorylation. Site-specific phosphorylation dynamics in response to globally elevated O-GlcNAc. Proc. Natl. Acad. Sci. U.S.A. 105, 13793-13798
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 13793-13798
    • Wang, Z.1    Gucek, M.2    Hart, G.W.3


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