메뉴 건너뛰기




Volumn 197, Issue 8, 2016, Pages 3086-3098

Global analysis of O-GlcNAc glycoproteins in activated human t cells

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLGLUCOSAMINIDASE; GLYCOPROTEIN; INTERLEUKIN 2; ISOPROTEIN; N ACETYLGLUCOSAMINE; RNA; SERINE; THREONINE; LYMPHOCYTE ANTIGEN RECEPTOR; N ACETYLGLUCOSAMINYLTRANSFERASE; UDP-N-ACETYLGLUCOSAMINE-PEPTIDE BETA-N-ACETYLGLUCOSAMINYLTRANSFERASE;

EID: 84991511950     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1502031     Document Type: Article
Times cited : (68)

References (89)
  • 1
    • 50249105938 scopus 로고    scopus 로고
    • Tailoring T-cell receptor signals by proximal negative feedback mechanisms
    • Acuto, O., V. Di Bartolo, and F. Michel. 2008. Tailoring T-cell receptor signals by proximal negative feedback mechanisms. Nat. Rev. Immunol. 8: 699-712.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 699-712
    • Acuto, O.1    Bartolo, V.D.I.2    Michel, F.3
  • 3
    • 0030746106 scopus 로고    scopus 로고
    • S-acylation of LCK protein tyrosine kinase is essential for its signalling function in T lymphocytes
    • Kabouridis, P. S., A. I. Magee, and S. C. Ley. 1997. S-acylation of LCK protein tyrosine kinase is essential for its signalling function in T lymphocytes. EMBO J. 16: 4983-4998.
    • (1997) EMBO J. , vol.16 , pp. 4983-4998
    • Kabouridis, P.S.1    Magee, A.I.2    Ley, S.C.3
  • 4
    • 0036305450 scopus 로고    scopus 로고
    • T(H) cell differentiation is accompanied by dynamic changes in histone acetylation of cytokine genes
    • Avni, O., D. Lee, F. Macian, S. J. Szabo, L. H. Glimcher, and A. Rao. 2002. T(H) cell differentiation is accompanied by dynamic changes in histone acetylation of cytokine genes. Nat. Immunol. 3: 643-651.
    • (2002) Nat. Immunol. , vol.3 , pp. 643-651
    • Avni, O.1    Lee, D.2    Macian, F.3    Szabo, S.J.4    Glimcher, L.H.5    Rao, A.6
  • 6
    • 3142726114 scopus 로고    scopus 로고
    • The Cbl family and other ubiquitin ligases: Destructive forces in control of antigen receptor signaling
    • Duan, L., A. L. Reddi, A. Ghosh, M. Dimri, and H. Band. 2004. The Cbl family and other ubiquitin ligases: destructive forces in control of antigen receptor signaling. Immunity 21: 7-17.
    • (2004) Immunity , vol.21 , pp. 7-17
    • Duan, L.1    Reddi, A.L.2    Ghosh, A.3    Dimri, M.4    Band, H.5
  • 7
    • 4644285392 scopus 로고    scopus 로고
    • E3 ubiquitin ligases as T cell anergy factors
    • Mueller, D. L. 2004. E3 ubiquitin ligases as T cell anergy factors. Nat. Immunol. 5: 883-890.
    • (2004) Nat. Immunol. , vol.5 , pp. 883-890
    • Mueller, D.L.1
  • 8
    • 28544435897 scopus 로고    scopus 로고
    • Immunity by ubiquitylation: A reversible process of modification
    • Liu, Y. C., J. Penninger, and M. Karin. 2005. Immunity by ubiquitylation: a reversible process of modification. Nat. Rev. Immunol. 5: 941-952.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 941-952
    • Liu, Y.C.1    Penninger, J.2    Karin, M.3
  • 10
    • 52649167708 scopus 로고    scopus 로고
    • CD4 T cells: Fates, functions, and faults
    • Zhu, J., and W. E. Paul. 2008. CD4 T cells: fates, functions, and faults. Blood 112: 1557-1569.
    • (2008) Blood , vol.112 , pp. 1557-1569
    • Zhu, J.1    Paul, W.E.2
  • 13
    • 77954462446 scopus 로고    scopus 로고
    • + T cell differentiation and functionality
    • + T cell differentiation and functionality. J. Immunol. 184: 4631-4636.
    • (2010) J. Immunol. , vol.184 , pp. 4631-4636
    • Dispirito, J.R.1    Shen, H.2
  • 14
    • 77956175013 scopus 로고    scopus 로고
    • NFAT, immunity and cancer: A transcription factor comes of age
    • Muller, M. R., and A. Rao. 2010. NFAT, immunity and cancer: a transcription factor comes of age. Nat. Rev. Immunol. 10: 645-656.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 645-656
    • Muller, M.R.1    Rao, A.2
  • 15
    • 77953289183 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase GRAIL regulates T cell tolerance and regulatory T cell function by mediating T cell receptor-CD3 degradation
    • Nurieva, R. I., S. Zheng, W. Jin, Y. Chung, Y. Zhang, G. J. Martinez, J. M. Reynolds, S. L. Wang, X. Lin, S. C. Sun, et al. 2010. The E3 ubiquitin ligase GRAIL regulates T cell tolerance and regulatory T cell function by mediating T cell receptor-CD3 degradation. Immunity 32: 670-680.
    • (2010) Immunity , vol.32 , pp. 670-680
    • Nurieva, R.I.1    Zheng, S.2    Jin, W.3    Chung, Y.4    Zhang, Y.5    Martinez, G.J.6    Reynolds, J.M.7    Wang, S.L.8    Lin, X.9    Sun, S.C.10
  • 16
    • 78650436475 scopus 로고    scopus 로고
    • GRAIL: A unique mediator of CD4 T-lymphocyte unresponsiveness
    • Whiting, C. C., L. L. Su, J. T. Lin, and C. G. Fathman. 2011. GRAIL: a unique mediator of CD4 T-lymphocyte unresponsiveness. FEBS J. 278: 47-58.
    • (2011) FEBS J. , vol.278 , pp. 47-58
    • Whiting, C.C.1    Su, L.L.2    Lin, J.T.3    Fathman, C.G.4
  • 18
    • 84875233825 scopus 로고    scopus 로고
    • Emerging roles for protein Spalmitoylation in immunity from chemical proteomics
    • Yount, J. S., M. M. Zhang, and H. C. Hang. 2013. Emerging roles for protein Spalmitoylation in immunity from chemical proteomics. Curr. Opin. Chem. Biol. 17: 27-33.
    • (2013) Curr. Opin. Chem. Biol. , vol.17 , pp. 27-33
    • Yount, J.S.1    Zhang, M.M.2    Hang, H.C.3
  • 19
    • 84905984263 scopus 로고    scopus 로고
    • The interface between transcriptional and epigenetic control of effector and memory CD8 T-cell differentiation
    • Gray, S. M., S. M. Kaech, and M. M. Staron. 2014. The interface between transcriptional and epigenetic control of effector and memory CD8 T-cell differentiation. Immunol. Rev. 261: 157-168.
    • (2014) Immunol. Rev. , vol.261 , pp. 157-168
    • Gray, S.M.1    Kaech, S.M.2    Staron, M.M.3
  • 20
    • 34247583996 scopus 로고    scopus 로고
    • Cycling of O-linked beta-Nacetylglucosamine on nucleocytoplasmic proteins
    • Hart, G. W., M. P. Housley, and C. Slawson. 2007. Cycling of O-linked beta-Nacetylglucosamine 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
  • 21
    • 72449187655 scopus 로고    scopus 로고
    • The intersections between O-GlcNAcylation and phosphorylation: Implications for multiple signaling pathways
    • Zeidan, Q., and G. W. Hart. 2010. The intersections between O-GlcNAcylation and phosphorylation: implications for multiple signaling pathways. J. Cell Sci. 123: 13-22.
    • (2010) J. Cell Sci. , vol.123 , pp. 13-22
    • Zeidan, Q.1    Hart, G.W.2
  • 22
    • 79959381299 scopus 로고    scopus 로고
    • Cross talk between O-GlcNAcylation and phosphorylation: Roles in signaling, transcription, and chronic disease
    • Hart, G. W., C. Slawson, G. Ramirez-Correa, and O. Lagerlof. 2011. Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease. Annu. Rev. Biochem. 80: 825-858.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 825-858
    • Hart, G.W.1    Slawson, C.2    Ramirez-Correa, G.3    Lagerlof, O.4
  • 23
    • 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
    • Shafi, R., S. P. Iyer, L. G. Ellies, N. O'Donnell, K. W. Marek, D. Chui, G. W. Hart, and J. D. Marth. 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. USA 97: 5735-5739.
    • (2000) Proc. Natl. Acad. Sci. USA , 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    Hart, G.W.7    Marth, J.D.8
  • 25
    • 0842347416 scopus 로고    scopus 로고
    • Ogt-dependent X-chromosome-linked protein glycosylation is a requisite modification in somatic cell function and embryo viability
    • O'Donnell, N., N. E. Zachara, G. W. Hart, and J. D. Marth. 2004. Ogt-dependent X-chromosome-linked protein glycosylation is a requisite modification in somatic cell function and embryo viability. Mol. Cell. Biol. 24: 1680-1690.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1680-1690
    • O'Donnell, N.1    Zachara, N.E.2    Hart, G.W.3    Marth, J.D.4
  • 27
    • 77949295164 scopus 로고    scopus 로고
    • The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine
    • Hanover, J. A., M. W. Krause, and D. C. Love. 2010. The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine. Biochim. Biophys. Acta 1800: 80-95.
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 80-95
    • Hanover, J.A.1    Krause, M.W.2    Love, D.C.3
  • 28
    • 84860184939 scopus 로고    scopus 로고
    • Bittersweet memories: Linking metabolism to epigenetics through O-GlcNAcylation
    • Hanover, J. A., M. W. Krause, and D. C. Love. 2012. Bittersweet memories: linking metabolism to epigenetics through O-GlcNAcylation. Nat. Rev. Mol. Cell Biol. 13: 312-321.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 312-321
    • Hanover, J.A.1    Krause, M.W.2    Love, D.C.3
  • 29
    • 84870731979 scopus 로고    scopus 로고
    • Exploring leukocyte O-GlcNAcylation as a novel diagnostic tool for the earlier detection of type 2 diabetes mellitus
    • Springhorn, C., T. E. Matsha, R. T. Erasmus, and M. F. Essop. 2012. Exploring leukocyte O-GlcNAcylation as a novel diagnostic tool for the earlier detection of type 2 diabetes mellitus. J. Clin. Endocrinol. Metab. 97: 4640-4649.
    • (2012) J. Clin. Endocrinol. Metab. , vol.97 , pp. 4640-4649
    • Springhorn, C.1    Matsha, T.E.2    Erasmus, R.T.3    Essop, M.F.4
  • 30
    • 67650072530 scopus 로고    scopus 로고
    • Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer's disease
    • Liu, F., J. Shi, H. Tanimukai, J. Gu, J. Gu, I. Grundke-Iqbal, K. Iqbal, and C. X. Gong. 2009. Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer's disease. Brain 132: 1820-1832.
    • (2009) Brain , vol.132 , pp. 1820-1832
    • Liu, F.1    Shi, J.2    Tanimukai, H.3    Gu, J.4    Gu, J.5    Grundke-Iqbal, I.6    Iqbal, K.7    Gong, C.X.8
  • 32
    • 77949332132 scopus 로고    scopus 로고
    • Regulation of insulin receptor substrate 1 (IRS-1)/AKT kinase-mediated insulin signaling by O-Linked beta-N-acetylglucosamine in 3T3-L1 adipocytes
    • Whelan, S. A., W. B. Dias, L. Thiruneelakantapillai, M. D. Lane, and G.W. Hart. 2010. Regulation of insulin receptor substrate 1 (IRS-1)/AKT kinase-mediated insulin signaling by O-Linked beta-N-acetylglucosamine in 3T3-L1 adipocytes. J. Biol. Chem. 285: 5204-5211.
    • (2010) J. Biol. Chem. , vol.285 , pp. 5204-5211
    • Whelan, S.A.1    Dias, W.B.2    Thiruneelakantapillai, L.3    Lane, M.D.4    Hart, G.W.5
  • 36
    • 84877921283 scopus 로고    scopus 로고
    • A correlation between altered O-GlcNAcylation, migration and with changes in E-cadherin levels in ovarian cancer cells
    • Jin, F. Z., C. Yu, D. Z. Zhao, M. J.Wu, and Z. Yang. 2013. A correlation between altered O-GlcNAcylation, migration and with changes in E-cadherin levels in ovarian cancer cells. Exp. Cell Res. 319: 1482-1490.
    • (2013) Exp. Cell Res. , vol.319 , pp. 1482-1490
    • Jin, F.Z.1    Yu, C.2    Zhao, D.Z.3    Wu, M.J.4    Yang, Z.5
  • 37
    • 0026030545 scopus 로고
    • Lymphocyte activation induces rapid changes in nuclear and cytoplasmic glycoproteins
    • Kearse, K. P., and G. W. Hart. 1991. Lymphocyte activation induces rapid changes in nuclear and cytoplasmic glycoproteins. Proc. Natl. Acad. Sci. USA 88: 1701-1705.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1701-1705
    • Kearse, K.P.1    Hart, G.W.2
  • 38
    • 35348836064 scopus 로고    scopus 로고
    • Requirement for O-linked N-acetylglucosaminyltransferase in lymphocytes activation
    • Golks, A., T. T. Tran, J. F. Goetschy, and D. Guerini. 2007. Requirement for O-linked N-acetylglucosaminyltransferase in lymphocytes activation. EMBO J. 26: 4368-4379.
    • (2007) EMBO J. , vol.26 , pp. 4368-4379
    • Golks, A.1    Tran, T.T.2    Goetschy, J.F.3    Guerini, D.4
  • 40
    • 34848896594 scopus 로고    scopus 로고
    • Mild performic acid oxidation enhances chromatographic and top down mass spectrometric analyses of histones
    • Pesavento, J. J., B. A. Garcia, J. A. Streeky, N. L. Kelleher, and C. A. Mizzen. 2007. Mild performic acid oxidation enhances chromatographic and top down mass spectrometric analyses of histones. Mol. Cell. Proteomics 6: 1510-1526.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1510-1526
    • Pesavento, J.J.1    Garcia, B.A.2    Streeky, J.A.3    Kelleher, N.L.4    Mizzen, C.A.5
  • 41
    • 0001607910 scopus 로고    scopus 로고
    • Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications
    • Wells, L., K. Vosseller, R. N. Cole, J. M. Cronshaw, M. J. Matunis, and G. W. Hart. 2002. Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications. Mol. Cell. Proteomics 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
  • 42
    • 13844313887 scopus 로고    scopus 로고
    • Quantitative analysis of both protein expression and serine/threonine post-translational modifications through stable isotope labeling with dithiothreitol
    • Vosseller, K., K. C. Hansen, R. J. Chalkley, J. C. Trinidad, L. Wells, G. W. Hart, and A. L. Burlingame. 2005. Quantitative analysis of both protein expression and serine/threonine post-translational modifications through stable isotope labeling with dithiothreitol. Proteomics 5: 388-398.
    • (2005) Proteomics , vol.5 , 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
  • 43
    • 3543072968 scopus 로고    scopus 로고
    • Purification of biotinylated proteins on streptavidin resin: A protocol for quantitative elution
    • Rybak, J., S. B. Scheurer, D. Neri, and G. Elia. 2004. Purification of biotinylated proteins on streptavidin resin: A protocol for quantitative elution. Proteomics 4: 2296-2299.
    • (2004) Proteomics , vol.4 , pp. 2296-2299
    • Rybak, J.1    Scheurer, S.B.2    Neri, D.3    Elia, G.4
  • 44
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J. K., A. L. McCormack, and J. R. Yates. 1994. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 5: 976-989.
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 45
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias, J. E., and S. P. Gygi. 2007. Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat. Methods 4: 207-214.
    • (2007) Nat. Methods , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 49
    • 77949769388 scopus 로고    scopus 로고
    • O-linked beta-Nacetylglucosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress
    • Butkinaree, C., K. Park, and G. W. Hart. 2010. O-linked beta-Nacetylglucosamine (O-GlcNAc): extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress. Biochim. Biophys. Acta 1800: 96-106.
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 96-106
    • Butkinaree, C.1    Park, K.2    Hart, G.W.3
  • 50
    • 27744519400 scopus 로고    scopus 로고
    • Fuel feeds function: Energy metabolism and the T-cell response
    • Fox, C. J., P. S. Hammerman, and C. B. Thompson. 2005. Fuel feeds function: energy metabolism and the T-cell response. Nat. Rev. Immunol. 5: 844-852.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 844-852
    • Fox, C.J.1    Hammerman, P.S.2    Thompson, C.B.3
  • 51
    • 44449165597 scopus 로고    scopus 로고
    • Glucose uptake is limiting in T cell activation and requires CD28-mediated Akt-dependent and independent pathways
    • Jacobs, S. R., C. E. Herman, N. J. Maciver, J. A. Wofford, H. L. Wieman, J. J. Hammen, and J. C. Rathmell. 2008. Glucose uptake is limiting in T cell activation and requires CD28-mediated Akt-dependent and independent pathways. J. Immunol. 180: 4476-4486.
    • (2008) J. Immunol. , vol.180 , pp. 4476-4486
    • Jacobs, S.R.1    Herman, C.E.2    Maciver, N.J.3    Wofford, J.A.4    Wieman, H.L.5    Hammen, J.J.6    Rathmell, J.C.7
  • 52
    • 54249141095 scopus 로고    scopus 로고
    • Glucose metabolism in lymphocytes is a regulated process with significant effects on immune cell function and survival
    • Maciver, N. J., S. R. Jacobs, H. L. Wieman, J. A. Wofford, J. L. Coloff, and J. C. Rathmell. 2008. Glucose metabolism in lymphocytes is a regulated process with significant effects on immune cell function and survival. J. Leukoc. Biol. 84: 949-957.
    • (2008) J. Leukoc. Biol. , vol.84 , pp. 949-957
    • Maciver, N.J.1    Jacobs, S.R.2    Wieman, H.L.3    Wofford, J.A.4    Coloff, J.L.5    Rathmell, J.C.6
  • 53
    • 79952747341 scopus 로고    scopus 로고
    • Metabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the Nacetylgalactosamine salvage pathway
    • Boyce, M., I. S. Carrico, A. S. Ganguli, S. H. Yu, M. J. Hangauer, S. C. Hubbard, J. J. Kohler, and C. R. Bertozzi. 2011. Metabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the Nacetylgalactosamine salvage pathway. Proc. Natl. Acad. Sci. USA 108: 3141-3146.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 3141-3146
    • Boyce, M.1    Carrico, I.S.2    Ganguli, A.S.3    Yu, S.H.4    Hangauer, M.J.5    Hubbard, S.C.6    Kohler, J.J.7    Bertozzi, C.R.8
  • 54
    • 0034677879 scopus 로고    scopus 로고
    • Cell surface engineering by a modified Staudinger reaction
    • Saxon, E., and C. R. Bertozzi. 2000. Cell surface engineering by a modified Staudinger reaction. Science 287: 2007-2010.
    • (2000) Science , vol.287 , pp. 2007-2010
    • Saxon, E.1    Bertozzi, C.R.2
  • 55
    • 84873350431 scopus 로고    scopus 로고
    • Proteome wide purification and identification of O-GlcNAc-modified proteins using click chemistry and mass spectrometry
    • Hahne, H., N. Sobotzki, T. Nyberg, D. Helm, V. S. Borodkin, D. M. van Aalten, B. Agnew, and B. Kuster. 2013. Proteome wide purification and identification of O-GlcNAc-modified proteins using click chemistry and mass spectrometry. J. Proteome Res. 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
  • 56
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang, D. W., B. T. Sherman, and R. A. Lempicki. 2009. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat. Protoc. 4: 44-57.
    • (2009) Nat. Protoc. , vol.4 , pp. 44-57
    • Huang, D.W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 57
    • 58549112996 scopus 로고    scopus 로고
    • Bioinformatics enrichment tools: Paths toward the comprehensive functional analysis of large gene lists
    • Huang, D. W., B. T. Sherman, and R. A. Lempicki. 2009. Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists. Nucleic Acids Res. 37: 1-13.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1-13
    • Huang, D.W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 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, S. A., S. Daou, B. Affar, and A. Burlingame. 2013. 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 13: 982-991.
    • (2013) Proteomics , vol.13 , pp. 982-991
    • Myers, S.A.1    Daou, S.2    Affar, B.3    Burlingame, A.4
  • 61
    • 57349187712 scopus 로고    scopus 로고
    • A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin
    • Slawson, C., T. Lakshmanan, S. Knapp, and G. W. Hart. 2008. A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin. Mol. Biol. Cell 19: 4130-4140.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4130-4140
    • Slawson, C.1    Lakshmanan, T.2    Knapp, S.3    Hart, G.W.4
  • 62
    • 77955865876 scopus 로고    scopus 로고
    • Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags
    • Rexach, J. E., C. J. Rogers, S. H. Yu, J. Tao, Y. E. Sun, and L. C. Hsieh-Wilson. 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
  • 63
    • 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
    • Ranuncolo, S. M., S. Ghosh, J. A. Hanover, G. W. Hart, and B. A. Lewis. 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.
    • (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
  • 64
    • 84905723395 scopus 로고    scopus 로고
    • Nutrient regulation of signaling, transcription, and cell physiology by O-GlcNAcylation
    • Hardivillé, S., and G. W. Hart. 2014. Nutrient regulation of signaling, transcription, and cell physiology by O-GlcNAcylation. Cell Metab. 20: 208-213.
    • (2014) Cell Metab. , vol.20 , pp. 208-213
    • Hardivillé, S.1    Hart, G.W.2
  • 66
    • 77952429792 scopus 로고    scopus 로고
    • Nutrient sensor O-GlcNAc transferase regulates breast cancer tumorigenesis through targeting of the oncogenic transcription factor FoxM1
    • Caldwell, S. A., S. R. Jackson, K. S. Shahriari, T. P. Lynch, G. Sethi, S. Walker, K. Vosseller, and M. J. Reginato. 2010. Nutrient sensor O-GlcNAc transferase regulates breast cancer tumorigenesis through targeting of the oncogenic transcription factor FoxM1. Oncogene 29: 2831-2842.
    • (2010) Oncogene , vol.29 , pp. 2831-2842
    • Caldwell, S.A.1    Jackson, S.R.2    Shahriari, K.S.3    Lynch, T.P.4    Sethi, G.5    Walker, S.6    Vosseller, K.7    Reginato, M.J.8
  • 67
    • 84859484538 scopus 로고    scopus 로고
    • Critical role of O-linked b-N-acetylglucosamine transferase in prostate cancer invasion, angiogenesis, and metastasis
    • Lynch, T. P., C. M. Ferrer, S. R. Jackson, K. S. Shahriari, K. Vosseller, and M. J. Reginato. 2012. Critical role of O-linked b-N-acetylglucosamine transferase in prostate cancer invasion, angiogenesis, and metastasis. J. Biol. Chem. 287: 11070-11081.
    • (2012) J. Biol. Chem. , vol.287 , pp. 11070-11081
    • Lynch, T.P.1    Ferrer, C.M.2    Jackson, S.R.3    Shahriari, K.S.4    Vosseller, K.5    Reginato, M.J.6
  • 70
    • 79251611901 scopus 로고    scopus 로고
    • Structure of human O-GlcNAc transferase and its complex with a peptide substrate
    • Lazarus, M. B., Y. Nam, J. Jiang, P. Sliz, and S. Walker. 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
  • 71
    • 0036853106 scopus 로고    scopus 로고
    • Sustained and dynamic inositol lipid metabolism inside and outside the immunological synapse
    • Costello, P. S., M. Gallagher, and D. A. Cantrell. 2002. Sustained and dynamic inositol lipid metabolism inside and outside the immunological synapse. Nat. Immunol. 3: 1082-1089.
    • (2002) Nat. Immunol. , vol.3 , pp. 1082-1089
    • Costello, P.S.1    Gallagher, M.2    Cantrell, D.A.3
  • 72
    • 0036852243 scopus 로고    scopus 로고
    • Imaging antigen-induced PI3K activation in T cells
    • Harriague, J., and G. Bismuth. 2002. Imaging antigen-induced PI3K activation in T cells. Nat. Immunol. 3: 1090-1096.
    • (2002) Nat. Immunol. , vol.3 , pp. 1090-1096
    • Harriague, J.1    Bismuth, G.2
  • 74
    • 33646159532 scopus 로고    scopus 로고
    • Recombinant O-GlcNAc transferase isoforms: Identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates
    • Lazarus, B. D., D. C. Love, and J. A. Hanover. 2006. Recombinant O-GlcNAc transferase isoforms: identification of O-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
  • 78
    • 84930181837 scopus 로고    scopus 로고
    • Isotope-targeted glycoproteomics (IsoTaG): A massindependent platform for intact N-and O-glycopeptide discovery and analysis
    • Woo, C. M., A. T. Iavarone, D. R. Spiciarich, K. K. Palaniappan, and C. R. Bertozzi. 2015. Isotope-targeted glycoproteomics (IsoTaG): a massindependent platform for intact N-and O-glycopeptide discovery and analysis. Nat. Methods 12: 561-567.
    • (2015) Nat. Methods , vol.12 , pp. 561-567
    • Woo, C.M.1    Iavarone, A.T.2    Spiciarich, D.R.3    Palaniappan, K.K.4    Bertozzi, C.R.5
  • 82
    • 84918836270 scopus 로고    scopus 로고
    • Knockdown of ubiquitin associated protein 2-like inhibits the growth and migration of prostate cancer cells
    • Li, D., and Y. Huang. 2014. Knockdown of ubiquitin associated protein 2-like inhibits the growth and migration of prostate cancer cells. Oncol. Rep. 32: 1578-1584.
    • (2014) Oncol. Rep. , vol.32 , pp. 1578-1584
    • Li, D.1    Huang, Y.2
  • 83
    • 70350462371 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions
    • Mayya, V., D. H. Lundgren, S. I. Hwang, K. Rezaul, L. Wu, J. K. Eng, V. Rodionov, and D. K. Han. 2009. Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci. Signal. 2: ra46.
    • (2009) Sci. Signal. , vol.2 , pp. ra46
    • Mayya, V.1    Lundgren, D.H.2    Hwang, S.I.3    Rezaul, K.4    Wu, L.5    Eng, J.K.6    Rodionov, V.7    Han, D.K.8
  • 84
    • 0023225084 scopus 로고
    • Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine
    • Holt, G. D., C. M. Snow, A. Senior, R. S. Haltiwanger, L. Gerace, and G. W. Hart. 1987. Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine. J. Cell Biol. 104: 1157-1164.
    • (1987) J. Cell Biol. , vol.104 , pp. 1157-1164
    • Holt, G.D.1    Snow, C.M.2    Senior, A.3    Haltiwanger, R.S.4    Gerace, L.5    Hart, G.W.6
  • 85
    • 84975275158 scopus 로고    scopus 로고
    • Post-translational O-GlcNAcylation is essential for nuclear pore integrity and maintenance of the pore selectivity filter
    • Zhu, Y., T. W. Liu, Z. Madden, S. A. Yuzwa, K. Murray, S. Cecioni, N. Zachara, and D. J. Vocadlo. 2016. Post-translational O-GlcNAcylation is essential for nuclear pore integrity and maintenance of the pore selectivity filter. J. Mol. Cell Biol. 8: 2-16.
    • (2016) J. Mol. Cell Biol. , vol.8 , pp. 2-16
    • Zhu, Y.1    Liu, T.W.2    Madden, Z.3    Yuzwa, S.A.4    Murray, K.5    Cecioni, S.6    Zachara, N.7    Vocadlo, D.J.8
  • 86


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.