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Volumn 85, Issue , 2016, Pages 631-657

The Biochemistry of O-GlcNAc Transferase: Which Functions Make It Essential in Mammalian Cells?

Author keywords

Glycosyltransferase mechanism; HCF 1; Host cell factor 1; Nutrient sensing; O GlcNAcylation; O linked N acetylglucosamine transferase; OGT structure; Tetratricopeptide repeat; TPR

Indexed keywords

CELL PROTEIN; HEXOSAMINE; HOST CELL FACTOR 1; N ACETYLGLUCOSAMINE; N ACETYLGLUCOSAMINE TRANSFERASE; SCAFFOLD PROTEIN; TRANSCRIPTION FACTOR; TRANSFERASE; UNCLASSIFIED DRUG; HCFC1 PROTEIN, HUMAN; HOST CELL FACTOR C1; N ACETYLGLUCOSAMINYLTRANSFERASE; O-GLCNAC TRANSFERASE;

EID: 84974715560     PISSN: 00664154     EISSN: 15454509     Source Type: Book Series    
DOI: 10.1146/annurev-biochem-060713-035344     Document Type: Article
Times cited : (142)

References (152)
  • 1
    • 84918541647 scopus 로고    scopus 로고
    • The making of a sweet modification: Structure and function of O-GlcNAc transferase
    • Janetzko J, Walker S. 2014. The making of a sweet modification: structure and function of O-GlcNAc transferase. J. Biol. Chem. 289(50):34424-32
    • (2014) J. Biol. Chem. , vol.289 , Issue.50 , pp. 34424-34432
    • Janetzko, J.1    Walker, S.2
  • 2
    • 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
    • Kreppel LK, Blomberg MA, Hart GW. 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(14):9308-15
    • (1997) J. Biol. Chem. , vol.272 , Issue.14 , pp. 9308-9315
    • Kreppel, L.K.1    Blomberg, M.A.2    Hart, G.W.3
  • 3
    • 0026795976 scopus 로고
    • Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine: Polypeptide Nacetylglucosaminyltransferase
    • Haltiwanger RS, Blomberg MA, Hart GW. 1992. Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide Nacetylglucosaminyltransferase. J. Biol. Chem. 267(13):9005-13
    • (1992) J. Biol. Chem. , vol.267 , Issue.13 , pp. 9005-9013
    • Haltiwanger, R.S.1    Blomberg, M.A.2    Hart, G.W.3
  • 4
    • 0030944105 scopus 로고    scopus 로고
    • O-linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats
    • Lubas WA, Frank DW, Krause M, Hanover JA. 1997. O-linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats. J. Biol. Chem. 272(14):9316-24
    • (1997) J. Biol. Chem. , vol.272 , Issue.14 , pp. 9316-9324
    • Lubas, W.A.1    Frank, D.W.2    Krause, M.3    Hanover, J.A.4
  • 5
    • 84949108534 scopus 로고    scopus 로고
    • A critical perspective of the diverse roles of O-GlcNAc transferase in chromatin
    • Gambetta MC, Müller J. 2015. A critical perspective of the diverse roles of O-GlcNAc transferase in chromatin. Chromosoma 124(4):429-42
    • (2015) Chromosoma , vol.124 , Issue.4 , pp. 429-442
    • Gambetta, M.C.1    Müller, J.2
  • 6
    • 84860184939 scopus 로고    scopus 로고
    • Bittersweet memories: Linking metabolism to epigenetics through O-GlcNAcylation
    • Hanover JA, Krause MW, Love DC. 2012. Bittersweet memories: linking metabolism to epigenetics through O-GlcNAcylation. Nat. Rev. Mol. Cell Biol. 13(5):312-21
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , Issue.5 , pp. 312-321
    • Hanover, J.A.1    Krause, M.W.2    Love, D.C.3
  • 7
    • 77953713601 scopus 로고    scopus 로고
    • Modulation of transcription factor function by O-GlcNAc modification
    • Ozcan S, Andrali SS, Cantrell JE. 2010. Modulation of transcription factor function by O-GlcNAc modification. Biochim. Biophys. Acta 1799(5-6):353-64
    • (2010) Biochim. Biophys. Acta , vol.1799 , Issue.5 , pp. 353-364
    • Ozcan, S.1    Andrali, S.S.2    Cantrell, J.E.3
  • 8
    • 84865300414 scopus 로고    scopus 로고
    • PFK1 glycosylation is a key regulator of cancer cell growth and central metabolic pathways
    • Yi W, Clark PM, Mason DE, Keenan MC, Hill C, et al. 2012. PFK1 glycosylation is a key regulator of cancer cell growth and central metabolic pathways. Science 337(6097):975-80
    • (2012) Science , vol.337 , Issue.6097 , pp. 975-980
    • Yi, W.1    Clark, P.M.2    Mason, D.E.3    Keenan, M.C.4    Hill, C.5
  • 9
    • 84916878247 scopus 로고    scopus 로고
    • O-GlcNAc transferase enables AgRP neurons to suppress browning of white fat
    • Ruan HB, Dietrich MO, Liu ZW, Zimmer MR, Li MD, et al. 2014. O-GlcNAc transferase enables AgRP neurons to suppress browning of white fat. Cell 159(2):306-17
    • (2014) Cell , vol.159 , Issue.2 , pp. 306-317
    • Ruan, H.B.1    Dietrich, M.O.2    Liu, Z.W.3    Zimmer, M.R.4    Li, M.D.5
  • 10
    • 84864708480 scopus 로고    scopus 로고
    • O-GlcNAc transferase/host cell factor C1 complex regulates gluconeogenesis by modulating PGC-1?stability
    • Ruan H-B, Han X, Li M-D, Singh JP, Qian K, et al. 2012. O-GlcNAc transferase/host cell factor C1 complex regulates gluconeogenesis by modulating PGC-1?stability. Cell Metab. 16(2):226-37
    • (2012) Cell Metab. , vol.16 , Issue.2 , pp. 226-237
    • Ruan, H.-B.1    Han, X.2    Li, M.-D.3    Singh, J.P.4    Qian, K.5
  • 11
    • 40449128605 scopus 로고    scopus 로고
    • Hepatic glucose sensing via the CREB coactivator CRTC2
    • Dentin R, Hedrick S, Xie J, Yates J, Montminy M. 2008. Hepatic glucose sensing via the CREB coactivator CRTC2. Science 319(5868):1402-5
    • (2008) Science , vol.319 , Issue.5868 , pp. 1402-1405
    • Dentin, R.1    Hedrick, S.2    Xie, J.3    Yates, J.4    Montminy, M.5
  • 12
    • 78649894035 scopus 로고    scopus 로고
    • O-linked N-acetylglucosamine (O-GlcNAc) regulates stress-induced heat shock protein expression in a GSK-3 dependent manner
    • Kazemi Z, Chang H, Haserodt S, McKen C, Zachara NE. 2010. O-linked N-acetylglucosamine (O-GlcNAc) regulates stress-induced heat shock protein expression in a GSK-3 dependent manner. J. Biol. Chem. 285(50):39096-107
    • (2010) J. Biol. Chem. , vol.285 , Issue.50 , pp. 39096-39107
    • Kazemi, Z.1    Chang, H.2    Haserodt, S.3    McKen, C.4    Zachara, N.E.5
  • 13
    • 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(1-2):13-28
    • (2004) Biochim. Biophys. Acta , vol.1673 , Issue.1 , pp. 13-28
    • Zachara, N.E.1    Hart, G.W.2
  • 14
    • 39749104251 scopus 로고    scopus 로고
    • Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance
    • Yang X, Ongusaha PP, Miles PD, Havstad JC, Zhang F, et al. 2008. Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance. Nature 451(7181):964-69
    • (2008) Nature , vol.451 , Issue.7181 , pp. 964-969
    • Yang, X.1    Ongusaha, P.P.2    Miles, P.D.3    Havstad, J.C.4    Zhang, F.5
  • 15
    • 84918508564 scopus 로고    scopus 로고
    • Multiple tissue-specific roles for the O-GlcNAc post-translationalmodification in the induction of and complications arising from type II diabetes
    • Vaidyanathan K, Wells L. 2014. Multiple tissue-specific roles for the O-GlcNAc post-translationalmodification in the induction of and complications arising from type II diabetes. J. Biol. Chem. 289(50):34466-71
    • (2014) J. Biol. Chem. , vol.289 , Issue.50 , pp. 34466-34471
    • Vaidyanathan, K.1    Wells, L.2
  • 17
    • 0030907389 scopus 로고    scopus 로고
    • Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility
    • Han I, Kudlow JE. 1997. Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility. Mol. Cell. Biol. 17(5):2550-58
    • (1997) Mol. Cell. Biol. , vol.17 , Issue.5 , pp. 2550-2558
    • Han, I.1    Kudlow, J.E.2
  • 18
    • 0346965700 scopus 로고    scopus 로고
    • O-GlcNAc modification is an endogenous inhibitor of the proteasome
    • Zhang F, Su K, Yang X, Bowe DB, Paterson AJ, Kudlow JE. 2003. O-GlcNAc modification is an endogenous inhibitor of the proteasomE. Cell 115(6):715-25
    • (2003) Cell , vol.115 , Issue.6 , pp. 715-725
    • Zhang, F.1    Su, K.2    Yang, X.3    Bowe, D.B.4    Paterson, A.J.5    Kudlow, J.E.6
  • 19
    • 2442687675 scopus 로고    scopus 로고
    • 70-kDa-heat shock protein presents an adjustable lectinic activity towards O-linked N-acetylglucosamine
    • Guinez C, Lemoine J, Michalski J-C, Lefebvre T. 2004. 70-kDa-heat shock protein presents an adjustable lectinic activity towards O-linked N-acetylglucosamine. Biochem. Biophys. Res. Commun. 319(1):21-26
    • (2004) Biochem. Biophys. Res. Commun. , vol.319 , Issue.1 , pp. 21-26
    • Guinez, C.1    Lemoine, J.2    Michalski, J.-C.3    Lefebvre, T.4
  • 20
    • 84928254126 scopus 로고    scopus 로고
    • A little sugar goes a long way: The cell biology of O-GlcNAc
    • Bond MR, Hanover JA. 2015. A little sugar goes a long way: The cell biology of O-GlcNAc. J. Cell Biol. 208(7):869-80
    • (2015) J. Cell Biol. , vol.208 , Issue.7 , pp. 869-880
    • Bond, M.R.1    Hanover, J.A.2
  • 21
    • 79959381299 scopus 로고    scopus 로고
    • Cross talk between O-GlcNAcylation and phosphorylation: Roles in signaling, transcription, and chronic disease
    • Hart GW, Slawson C, Ramirez-Correa G, Lagerlof O. 2011. Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease. Annu. Rev. Biochem. 80(1):825-58
    • (2011) Annu. Rev. Biochem. , vol.80 , Issue.1 , pp. 825-858
    • Hart, G.W.1    Slawson, C.2    Ramirez-Correa, G.3    Lagerlof, O.4
  • 22
    • 79952606829 scopus 로고    scopus 로고
    • Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathway
    • Daou S, Mashtalir N, Hammond-Martel I, Pak H, Yu H, et al. 2011. Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathway. PNAS 108(7):2747-52
    • (2011) PNAS , vol.108 , Issue.7 , pp. 2747-2752
    • Daou, S.1    Mashtalir, N.2    Hammond-Martel, I.3    Pak, H.4    Yu, H.5
  • 23
    • 79551661274 scopus 로고    scopus 로고
    • O-GlcNAc transferase catalyzes site-specific proteolysis of HCF-1
    • Capotosti F, Guernier S, Lammers F, Waridel P, Cai Y, et al. 2011. O-GlcNAc transferase catalyzes site-specific proteolysis of HCF-1. Cell 144(3):376-88
    • (2011) Cell , vol.144 , Issue.3 , pp. 376-388
    • Capotosti, F.1    Guernier, S.2    Lammers, F.3    Waridel, P.4    Cai, Y.5
  • 24
    • 84889246546 scopus 로고    scopus 로고
    • HCF-1 is cleaved in the active site of O-GlcNAc transferase
    • Lazarus MB, Jiang J, Kapuria V, Bhuiyan T, Janetzko J, et al. 2013. HCF-1 is cleaved in the active site of O-GlcNAc transferase. Science 342(6163):1235-39
    • (2013) Science , vol.342 , Issue.6163 , pp. 1235-1239
    • Lazarus, M.B.1    Jiang, J.2    Kapuria, V.3    Bhuiyan, T.4    Janetzko, J.5
  • 25
    • 84942866628 scopus 로고    scopus 로고
    • Distinct OGT-binding sites promote HCF-1 cleavage
    • BhuiyanT, Waridel P, Kapuria V, ZoeteV, HerrW. 2015. Distinct OGT-binding sites promote HCF-1 cleavage. PLOS ONE 10(8):e0136636
    • (2015) PLOS ONE , vol.10 , Issue.8 , pp. e0136636
    • Bhuiyan, T.1    Waridel, P.2    Kapuria, V.3    Zoete, V.4    Herr, W.5
  • 26
    • 0037067659 scopus 로고    scopus 로고
    • Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3a: Coupling protein O-GlcNAcylation to transcriptional repression
    • Yang X, Zhang F, Kudlow JE. 2002. Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3a: coupling protein O-GlcNAcylation to transcriptional repression. Cell 110(1):69-80
    • (2002) Cell , vol.110 , Issue.1 , pp. 69-80
    • Yang, X.1    Zhang, F.2    Kudlow, J.E.3
  • 27
    • 84866467141 scopus 로고    scopus 로고
    • Loss of the tumor suppressor BAP1 causes myeloid transformation
    • Dey A, Seshasayee D, Noubade R, French DM, Liu J, et al. 2012. Loss of the tumor suppressor BAP1 causes myeloid transformation. Science 337(6101):1541-46
    • (2012) Science , vol.337 , Issue.6101 , pp. 1541-1546
    • Dey, A.1    Seshasayee, D.2    Noubade, R.3    French, D.M.4    Liu, J.5
  • 28
    • 84874266225 scopus 로고    scopus 로고
    • TETproteins connect theO-linked N-acetylglucosamine transferase OGT to chromatin in embryonic stem cells
    • Vella P, Scelfo A, Jammula S, Chiacchiera F, WilliamsK, et al. 2013. TETproteins connect theO-linked N-acetylglucosamine transferase OGT to chromatin in embryonic stem cells. Mol. Cell. 49(4):645-56
    • (2013) Mol. Cell. , vol.49 , Issue.4 , pp. 645-656
    • Vella, P.1    Scelfo, A.2    Jammula, S.3    Chiacchiera, F.4    Williams, K.5
  • 29
    • 84875218124 scopus 로고    scopus 로고
    • TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT and Set1/COMPASS
    • Deplus R, Delatte B, Schwinn MK, Defrance M, Méndez J, et al. 2013. TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT and Set1/COMPASS. EMBO J. 32(5):645-55
    • (2013) EMBO J. , vol.32 , Issue.5 , pp. 645-655
    • Deplus, R.1    Delatte, B.2    Schwinn, M.K.3    Defrance, M.4    Méndez, J.5
  • 30
    • 84891153568 scopus 로고    scopus 로고
    • TET3-OGT interaction increases the stability and the presence of OGT in chromatin
    • Ito R, Katsura S, Shimada H, Tsuchiya H, Hada M, et al. 2014. TET3-OGT interaction increases the stability and the presence of OGT in chromatin. Genes Cells 19(1):52-65
    • (2014) Genes Cells , vol.19 , Issue.1 , pp. 52-65
    • Ito, R.1    Katsura, S.2    Shimada, H.3    Tsuchiya, H.4    Hada, M.5
  • 31
    • 84880530231 scopus 로고    scopus 로고
    • Ten-eleven translocation 1 (Tet1) is regulated by O-linked N-acetylglucosamine transferase (Ogt) for target gene repression in mouse embryonic stem cells
    • Shi FT, Kim H, Lu W, He Q, Liu D, et al. 2013. Ten-eleven translocation 1 (Tet1) is regulated by O-linked N-acetylglucosamine transferase (Ogt) for target gene repression in mouse embryonic stem cells. J. Biol. Chem. 288(29):20776-84
    • (2013) J. Biol. Chem. , vol.288 , Issue.29 , pp. 20776-20784
    • Shi, F.T.1    Kim, H.2    Lu, W.3    He, Q.4    Liu, D.5
  • 32
    • 84872953223 scopus 로고    scopus 로고
    • TET2 promotes histone O-GlcNAcylation during gene transcription
    • Chen Q, Chen Y, Bian C, Fujiki R, Yu X. 2013. TET2 promotes histone O-GlcNAcylation during gene transcription. Nature 493(7433):561-64
    • (2013) Nature , vol.493 , Issue.7433 , pp. 561-564
    • Chen, Q.1    Chen, Y.2    Bian, C.3    Fujiki, R.4    Yu, X.5
  • 33
    • 84896858308 scopus 로고    scopus 로고
    • Differential regulation of the ten-eleven translocation (TET) family of dioxygenases by O-linked N-acetylglucosamine transferase (OGT)
    • Zhang Q, Liu X, GaoW, Li P, Hou J, et al. 2014. Differential regulation of the ten-eleven translocation (TET) family of dioxygenases by O-linked N-acetylglucosamine transferase (OGT). J. Biol. Chem. 289(9):5986-96
    • (2014) J. Biol. Chem. , vol.289 , Issue.9 , pp. 5986-5996
    • Zhang, Q.1    Liu, X.2    Gao, W.3    Li, P.4    Hou, J.5
  • 34
    • 45149095784 scopus 로고    scopus 로고
    • AMP-activated protein kinase and p38MAPK activate O-GlcNAcylation of neuronal proteins during glucose deprivation
    • Cheung WD, HartGW. 2008. AMP-activated protein kinase and p38MAPK activate O-GlcNAcylation of neuronal proteins during glucose deprivation. J. Biol. Chem. 283(19):13009-20
    • (2008) J. Biol. Chem. , vol.283 , Issue.19 , pp. 13009-13020
    • Cheung, W.D.1    Hart, G.W.2
  • 35
    • 57749088688 scopus 로고    scopus 로고
    • O-linked N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins
    • Cheung WD, Sakabe K, Housley MP, Dias WB, Hart GW. 2008. O-linked N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins. J. Biol. Chem. 283(49):33935-41
    • (2008) J. Biol. Chem. , vol.283 , Issue.49 , pp. 33935-33941
    • Cheung, W.D.1    Sakabe, K.2    Housley, M.P.3    Dias, W.B.4    Hart, G.W.5
  • 36
    • 64149111641 scopus 로고    scopus 로고
    • A PGC-1 O-GlcNAc transferase complex regulates FoxO transcription factor activity in response to glucose
    • HousleyMP, Udeshi ND, Rodgers JT, Shabanowitz J, Puigserver P, et al. 2009. A PGC-1 O-GlcNAc transferase complex regulates FoxO transcription factor activity in response to glucose. J. Biol. Chem. 284(8):5148-57
    • (2009) J. Biol. Chem. , vol.284 , Issue.8 , pp. 5148-5157
    • Housley, M.P.1    Udeshi, N.D.2    Rodgers, J.T.3    Shabanowitz, J.4    Puigserver, P.5
  • 37
    • 0042090275 scopus 로고    scopus 로고
    • Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity
    • Iyer SPN, Hart GW. 2003. Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity. J. Biol. Chem. 278(27):24608-16
    • (2003) J. Biol. Chem. , vol.278 , Issue.27 , pp. 24608-24616
    • Iyer, S.P.N.1    Hart, G.W.2
  • 38
    • 78650733551 scopus 로고    scopus 로고
    • N-acetylglucosamine transferase is an integral component of a kinesin-directed mitochondrial trafficking complex
    • Brickley K, Pozo K, Stephenson FA. 2011. N-acetylglucosamine transferase is an integral component of a kinesin-directed mitochondrial trafficking complex. Biochim. Biophys. Acta 1813(1):269-81
    • (2011) Biochim. Biophys. Acta , vol.1813 , Issue.1 , pp. 269-281
    • Brickley, K.1    Pozo, K.2    Stephenson, F.A.3
  • 39
    • 57349187712 scopus 로고    scopus 로고
    • A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin
    • Slawson C, Lakshmanan T, Knapp S, Hart GW. 2008. A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin. Mol. Biol. Cell 19(10):4130-40
    • (2008) Mol. Biol. Cell , vol.19 , Issue.10 , pp. 4130-4140
    • Slawson, C.1    Lakshmanan, T.2    Knapp, S.3    Hart, G.W.4
  • 40
    • 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, Iyer SPN, Ellies LG, O'Donnell N, Marek KW, et al. 2000. The O-GlcNAc transferase gene resides on the x chromosome and is essential for embryonic stem cell viability and mouse ontogeny. PNAS 97(11):5735-39
    • (2000) PNAS , vol.97 , Issue.11 , pp. 5735-5739
    • Shafi, R.1    Iyer, S.P.N.2    Ellies, L.G.3    O'Donnell, N.4    Marek, K.W.5
  • 41
    • 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, Zachara NE, Hart GW, Marth JD. 2004. Ogt-dependent X-chromosome-linked protein glycosylation is a requisite modification in somatic cell function and embryo viability. Mol. Cell. Biol. 24(4):1680-90
    • (2004) Mol. Cell. Biol. , vol.24 , Issue.4 , pp. 1680-1690
    • O'Donnell, N.1    Zachara, N.E.2    Hart, G.W.3    Marth, J.D.4
  • 42
    • 84897499290 scopus 로고    scopus 로고
    • Microarray discovery of newOGTsubstrates: The medulloblastoma oncogene OTX2 is O-GlcNAcylated
    • Ortiz-Meoz RF, Merbl Y, KirschnerMW, Walker S. 2014. Microarray discovery of newOGTsubstrates: The medulloblastoma oncogene OTX2 is O-GlcNAcylated. J. Am. Chem. Soc. 136(13):4845-48
    • (2014) J. Am. Chem. Soc. , vol.136 , Issue.13 , pp. 4845-4848
    • Ortiz-Meoz, R.F.1    Merbl, Y.2    Kirschner, M.W.3    Walker, S.4
  • 43
    • 79953652899 scopus 로고    scopus 로고
    • DbOGAP-an integrated bioinformatics resource for protein O-GlcNAcylation
    • Wang J, Torii M, Liu H, Hart GW, Hu Z-Z. 2011. dbOGAP-an integrated bioinformatics resource for protein O-GlcNAcylation. BMC Bioinform. 12:91
    • (2011) BMC Bioinform. , vol.12 , pp. 91
    • Wang, J.1    Torii, M.2    Liu, H.3    Hart, G.W.4    Hu, Z.-Z.5
  • 44
    • 84898658993 scopus 로고    scopus 로고
    • Global identification of O-GlcNAc transferase (OGT) interactors by a human proteome microarray and the construction of an OGT interactome
    • Deng RP, He X, Guo SJ, Liu WF, Tao Y, Tao SC. 2014. Global identification of O-GlcNAc transferase (OGT) interactors by a human proteome microarray and the construction of an OGT interactome. Proteomics 14(9):1020-30
    • (2014) Proteomics , vol.14 , Issue.9 , pp. 1020-1030
    • Deng, R.P.1    He, X.2    Guo, S.J.3    Liu, W.F.4    Tao, Y.5    Tao, S.C.6
  • 45
    • 84885315910 scopus 로고    scopus 로고
    • O-GlcNAc in cancer biology
    • Ma Z, Vosseller K. 2013. O-GlcNAc in cancer biology. Amino Acids. 45(4):719-33
    • (2013) Amino Acids. , vol.45 , Issue.4 , pp. 719-733
    • Ma, Z.1    Vosseller, K.2
  • 46
    • 84919329062 scopus 로고    scopus 로고
    • Protein O-GlcNAcylation and cardiovascular (patho) physiology
    • Marsh SA, Collins HE, Chatham JC. 2014. Protein O-GlcNAcylation and cardiovascular (patho) physiology. J. Biol. Chem. 289(50):34449-56
    • (2014) J. Biol. Chem. , vol.289 , Issue.50 , pp. 34449-34456
    • Marsh, S.A.1    Collins, H.E.2    Chatham, J.C.3
  • 47
    • 84907200765 scopus 로고    scopus 로고
    • O-GlcNAc and neurodegeneration: Biochemical mechanisms and potential roles in Alzheimer's disease and beyond
    • Yuzwa SA, Vocadlo DJ. 2014. O-GlcNAc and neurodegeneration: biochemical mechanisms and potential roles in Alzheimer's disease and beyond. Chem. Soc. Rev. 43(19):6839-58
    • (2014) Chem. Soc. Rev. , vol.43 , Issue.19 , pp. 6839-6858
    • Yuzwa, S.A.1    Vocadlo, D.J.2
  • 48
    • 84929146685 scopus 로고    scopus 로고
    • The role of hexosamine biosynthesis and signaling in early development
    • ed. HJ Leese, DR Brison. New York: Springer
    • Pantaleon DM. 2015. The role of hexosamine biosynthesis and signaling in early development. In Cell Signaling During Mammalian Early Embryo Development, ed. HJ Leese, DR Brison, pp. 53-76. New York: Springer
    • (2015) Cell Signaling during Mammalian Early Embryo Development , pp. 53-76
    • Pantaleon, D.M.1
  • 49
    • 0034597007 scopus 로고    scopus 로고
    • Decreased UDP-GlcNAc levels abrogate proliferation control in EMeg32-deficient cells
    • Boehmelt G, Wakeham A, Elia A, Sasaki T, Plyte S, et al. 2000. Decreased UDP-GlcNAc levels abrogate proliferation control in EMeg32-deficient cells. EMBO J. 19(19):5092-104
    • (2000) EMBO J. , vol.19 , Issue.19 , pp. 5092-5104
    • Boehmelt, G.1    Wakeham, A.2    Elia, A.3    Sasaki, T.4    Plyte, S.5
  • 50
    • 0025193520 scopus 로고
    • Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins. Identification of a uridine diphospho-N-acetylglucosamine: Peptide Nacetylglucosaminyltransferase
    • Haltiwanger RS, Holt GD, Hart GW. 1990. Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins. Identification of a uridine diphospho-N-acetylglucosamine:peptide Nacetylglucosaminyltransferase. J. Biol. Chem. 265(5):2563-68
    • (1990) J. Biol. Chem. , vol.265 , Issue.5 , pp. 2563-2568
    • Haltiwanger, R.S.1    Holt, G.D.2    Hart, G.W.3
  • 51
    • 0025855139 scopus 로고
    • Discovery of a metabolic pathwaymediating glucose-induced desensitization of the glucose transport system. Role of hexosamine biosynthesis in the induction of insulin resistance
    • Marshall S, Bacote V, Traxinger RR. 1991. Discovery of a metabolic pathwaymediating glucose-induced desensitization of the glucose transport system. Role of hexosamine biosynthesis in the induction of insulin resistance. J. Biol. Chem. 266(8):4706-12
    • (1991) J. Biol. Chem. , vol.266 , Issue.8 , pp. 4706-4712
    • Marshall, S.1    Bacote, V.2    Traxinger, R.R.3
  • 52
    • 0037341310 scopus 로고    scopus 로고
    • Palmitate-induced activation of the hexosamine pathway in human myotubes: Increased expression of glutamine: Fructose-6-phosphate aminotransferase
    • Weigert C, Klopfer K, Kausch C, Brodbeck K, Stumvoll M, et al. 2003. Palmitate-induced activation of the hexosamine pathway in human myotubes: increased expression of glutamine:fructose-6-phosphate aminotransferase. Diabetes 52(3):650-56
    • (2003) Diabetes , vol.52 , Issue.3 , pp. 650-656
    • Weigert, C.1    Klopfer, K.2    Kausch, C.3    Brodbeck, K.4    Stumvoll, M.5
  • 53
    • 4143074732 scopus 로고    scopus 로고
    • Dynamic actions of glucose and glucosamine on hexosamine biosynthesis in isolated adipocytes: Differential effects on glucosamine 6-phosphate, UDP-Nacetylglucosamine, and ATP levels
    • Marshall S, Nadeau O, Yamasaki K. 2004. Dynamic actions of glucose and glucosamine on hexosamine biosynthesis in isolated adipocytes: differential effects on glucosamine 6-phosphate, UDP-Nacetylglucosamine, and ATP levels. J. Biol. Chem. 279(34):35313-19
    • (2004) J. Biol. Chem. , vol.279 , Issue.34 , pp. 35313-35319
    • Marshall, S.1    Nadeau, O.2    Yamasaki, K.3
  • 54
    • 0036181947 scopus 로고    scopus 로고
    • Hexosamines as mediators of nutrient sensing and regulation in diabetes
    • McClain DA. 2002. Hexosamines as mediators of nutrient sensing and regulation in diabetes. J. Diabetes Complicat. 16(1):72-80
    • (2002) J. Diabetes Complicat. , vol.16 , Issue.1 , pp. 72-80
    • McClain, D.A.1
  • 55
    • 2442520383 scopus 로고    scopus 로고
    • Hexosamines are unlikely to function as a nutrient-sensor in 3T3-L1 adipocytes: A comparison of UDP-hexosamine levels after increased glucose flux and glucosamine treatment
    • Bosch RR, Pouwels M-JJM, Span PN, Olthaar AJ, Tack CJ, et al. 2004. Hexosamines are unlikely to function as a nutrient-sensor in 3T3-L1 adipocytes: A comparison of UDP-hexosamine levels after increased glucose flux and glucosamine treatment. Endocrine 23(1):17-24
    • (2004) Endocrine , vol.23 , Issue.1 , pp. 17-24
    • Bosch, R.R.1    Pouwels, M.-J.J.M.2    Span, P.N.3    Olthaar, A.J.4    Tack, C.J.5
  • 56
    • 0021857641 scopus 로고
    • Translocation of UDP-N-acetylglucosamine into vesicles derived from rat liver rough endoplasmic reticulum and Golgi apparatus
    • PerezM, Hirschberg CB. 1985. Translocation of UDP-N-acetylglucosamine into vesicles derived from rat liver rough endoplasmic reticulum and Golgi apparatus. J. Biol. Chem. 260(8):4671-78
    • (1985) J. Biol. Chem. , vol.260 , Issue.8 , pp. 4671-4678
    • Perez, M.1    Hirschberg, C.B.2
  • 57
    • 0037440370 scopus 로고    scopus 로고
    • Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc transferase encoded by a single mammalian gene
    • Hanover JA, Yu S, Lubas WB, Shin S-H, Ragano-Caracciola M, et al. 2003. Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc transferase encoded by a single mammalian gene. Arch. Biochem. Biophys. 409(2):287-97
    • (2003) Arch. Biochem. Biophys. , 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
  • 58
    • 84857933257 scopus 로고    scopus 로고
    • Structural and functional discussion of the tetra-trico-peptide repeat, a protein interaction module
    • Zeytuni N, Zarivach R. 2012. Structural and functional discussion of the tetra-trico-peptide repeat, a protein interaction module. Structure 20(3):397-405
    • (2012) Structure , vol.20 , Issue.3 , pp. 397-405
    • Zeytuni, N.1    Zarivach, R.2
  • 59
    • 0344496513 scopus 로고    scopus 로고
    • The tetratricopeptide repeat: A structural motif mediating protein-protein interactions
    • Blatch GL, Lässle M. 1999. The tetratricopeptide repeat: A structural motif mediating protein-protein interactions. BioEssays 21(11):932-39
    • (1999) BioEssays , vol.21 , Issue.11 , pp. 932-939
    • Blatch, G.L.1    Lässle, M.2
  • 60
    • 80052491229 scopus 로고    scopus 로고
    • Versatile TPR domains accommodate different modes of target protein recognition and function
    • Allan RK, Ratajczak T. 2010. Versatile TPR domains accommodate different modes of target protein recognition and function. Cell Stress Chaperones 16(4):353-67
    • (2010) Cell Stress Chaperones , vol.16 , Issue.4 , pp. 353-367
    • Allan, R.K.1    Ratajczak, T.2
  • 61
    • 4744341309 scopus 로고    scopus 로고
    • The superhelical TPRrepeat domain of O-linkedGlcNAc transferase exhibits structural similarities to importin ?
    • Jnek M, Rehwinkel J, Lazarus BD, Izaurralde E, Hanover JA, Conti E. 2004. The superhelical TPRrepeat domain of O-linkedGlcNAc transferase exhibits structural similarities to importin ?. Nat. Struct. Mol. Biol. 11(10):1001-7
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , Issue.10 , pp. 1001-1007
    • Jnek, M.1    Rehwinkel, J.2    Lazarus, B.D.3    Izaurralde, E.4    Hanover, J.A.5    Conti, E.6
  • 62
    • 79251611901 scopus 로고    scopus 로고
    • Structure of human O-GlcNAc transferase and its complex with a peptide substrate
    • Lazarus MB, Nam Y, Jiang J, Sliz P, Walker S. 2011. Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature 469(7331):564-67
    • (2011) Nature , vol.469 , Issue.7331 , pp. 564-567
    • Lazarus, M.B.1    Nam, Y.2    Jiang, J.3    Sliz, P.4    Walker, S.5
  • 63
    • 0035976715 scopus 로고    scopus 로고
    • Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily
    • Wrabl JO, Grishin NV. 2001. Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily. J. Mol. Biol. 314(3):365-74
    • (2001) J. Mol. Biol. , vol.314 , Issue.3 , pp. 365-374
    • Wrabl, J.O.1    Grishin, N.V.2
  • 64
    • 0033623762 scopus 로고    scopus 로고
    • The 1. 9 a crystal structure of Escherichia coli MurG, a membraneassociated glycosyltransferase involved in peptidoglycan biosynthesis
    • Ha S, Walker D, Shi Y, Walker S. 2000. The 1. 9 a crystal structure of Escherichia coli MurG, a membraneassociated glycosyltransferase involved in peptidoglycan biosynthesis. Protein Sci. 9:1045-52
    • (2000) Protein Sci. , vol.9 , pp. 1045-1052
    • Ha, S.1    Walker, D.2    Shi, Y.3    Walker, S.4
  • 65
    • 0015834475 scopus 로고
    • Comparison of super-secondary structures in proteins
    • Rao ST, Rossmann MG. 1973. Comparison of super-secondary structures in proteins. J. Mol. Biol. 76(2):241-56
    • (1973) J. Mol. Biol. , vol.76 , Issue.2 , pp. 241-256
    • Rao, S.T.1    Rossmann, M.G.2
  • 69
    • 0037417869 scopus 로고    scopus 로고
    • Crystal structure of the MurG: UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases
    • Hu Y, Chen L, Ha S, Gross B, Falcone B, et al. 2003. Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases. PNAS 100(3):845-49
    • (2003) PNAS , vol.100 , Issue.3 , pp. 845-849
    • Hu, Y.1    Chen, L.2    Ha, S.3    Gross, B.4    Falcone, B.5
  • 71
    • 84870384002 scopus 로고    scopus 로고
    • O-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysis
    • SchimplM, Zheng X, Borodkin VS, Blair DE, Ferenbach AT, et al. 2012. O-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysis. Nat. Chem. Biol. 8(12):969-74
    • (2012) Nat. Chem. Biol. , vol.8 , Issue.12 , pp. 969-974
    • Schimpl, M.1    Zheng, X.2    Borodkin, V.S.3    Blair, D.E.4    Ferenbach, A.T.5
  • 72
    • 84941024243 scopus 로고    scopus 로고
    • The active site of O-GlcNAc transferase imposes constraints on substrate sequence
    • Pathak S, Alonso J, Schimpl M, Rafie K, Blair DE, et al. 2015. The active site of O-GlcNAc transferase imposes constraints on substrate sequence. Nat. Struct. Mol. Biol. 22(9):744-50
    • (2015) Nat. Struct. Mol. Biol. , vol.22 , Issue.9 , pp. 744-750
    • Pathak, S.1    Alonso, J.2    Schimpl, M.3    Rafie, K.4    Blair, D.E.5
  • 73
    • 84905216760 scopus 로고    scopus 로고
    • A peptide panel investigation reveals the acceptor specificity of O-GlcNAc transferase
    • Liu X, Li L, Wang Y, Yan H, Ma X, et al. 2014. A peptide panel investigation reveals the acceptor specificity of O-GlcNAc transferase. FASEB J. 28(8):3362-72
    • (2014) FASEB J. , vol.28 , Issue.8 , pp. 3362-3372
    • Liu, X.1    Li, L.2    Wang, Y.3    Yan, H.4    Ma, X.5
  • 74
    • 34250309514 scopus 로고    scopus 로고
    • A high-throughput assay for O-GlcNAc transferase detects primary sequence preferences in peptide substrates
    • Leavy TM, Bertozzi CR. 2007. A high-throughput assay for O-GlcNAc transferase detects primary sequence preferences in peptide substrates. Bioorg. Med. Chem. Lett. 17(14):3851-54
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , Issue.14 , pp. 3851-3854
    • Leavy, T.M.1    Bertozzi, C.R.2
  • 75
    • 84866522320 scopus 로고    scopus 로고
    • Substrate-assisted catalytic mechanism of O-GlcNAc transferase discovered by quantum mechanics/molecular mechanics investigation
    • Tvaro?ska I, Kozmon S, Wimmerová M, Ko?ca J. 2012. Substrate-assisted catalytic mechanism of O-GlcNAc transferase discovered by quantum mechanics/molecular mechanics investigation. J. Am. Chem. Soc. 134(37):15563-71
    • (2012) J. Am. Chem. Soc. , vol.134 , Issue.37 , pp. 15563-15571
    • Tvaroska, I.1    Kozmon, S.2    Wimmerová, M.3    Koca, J.4
  • 76
    • 84905366680 scopus 로고    scopus 로고
    • Substrateguided front-face reaction revealed by combined structural snapshots andmetadynamics for the polypeptide N-acetylgalactosaminyltransferase 2
    • Lira-Navarrete E, Iglesias-Fernández J, Zandberg WF, Compañón I, Kong Y, et al. 2014. Substrateguided front-face reaction revealed by combined structural snapshots andmetadynamics for the polypeptide N-acetylgalactosaminyltransferase 2. Angew. Chem. Int. Ed. Engl. 53(31):8206-10
    • (2014) Angew. Chem. Int. Ed. Engl. , vol.53 , Issue.31 , pp. 8206-8210
    • Lira-Navarrete, E.1    Iglesias-Fernández, J.2    Zandberg, W.F.3    Compañón, I.4    Kong, Y.5
  • 77
    • 84866984440 scopus 로고    scopus 로고
    • Acid dissociation constants of uridine-5-diphosphate compounds determined by 31phosphorus nuclear magnetic resonance spectroscopy and internal pH referencing
    • Jancan I, Macnaughtan MA. 2012. Acid dissociation constants of uridine-5-diphosphate compounds determined by 31phosphorus nuclear magnetic resonance spectroscopy and internal pH referencing. Anal. Chim. Acta 749:63-69
    • (2012) Anal. Chim. Acta , vol.749 , pp. 63-69
    • Jancan, I.1    Macnaughtan, M.A.2
  • 78
    • 84860389788 scopus 로고    scopus 로고
    • Mechanistic evidence for a front-side, SNi-type reaction in a retaining glycosyltransferase
    • Lee SS, Hong SY, Errey JC, Izumi A, Davies GJ, Davis BG. 2011. Mechanistic evidence for a front-side, SNi-type reaction in a retaining glycosyltransferase. Nat. Chem. Biol. 7(9):631-38
    • (2011) Nat. Chem. Biol. , vol.7 , Issue.9 , pp. 631-638
    • Lee, S.S.1    Hong, S.Y.2    Errey, J.C.3    Izumi, A.4    Davies, G.J.5    Davis, B.G.6
  • 79
    • 84858218497 scopus 로고    scopus 로고
    • Retaining glycosyltransferase mechanism studied by QM/MM methods: Lipopolysaccharyl- 1, 4-galactosyltransferase C transfers galactose via an oxocarbenium ion-like transition state
    • Gómez H, Polyak I, Thiel W, Lluch JM, Masgrau L. 2012. Retaining glycosyltransferase mechanism studied by QM/MM methods: Lipopolysaccharyl- 1, 4-galactosyltransferase C transfers galactose via an oxocarbenium ion-like transition state. J. Am. Chem. Soc. 134(10):4743-52
    • (2012) J. Am. Chem. Soc. , vol.134 , Issue.10 , pp. 4743-4752
    • Gómez, H.1    Polyak, I.2    Thiel, W.3    Lluch, J.M.4    Masgrau, L.5
  • 80
    • 76349106696 scopus 로고    scopus 로고
    • Mechanistic insight into enzymatic glycosyl transfer with retention of configuration through analysis of glycomimetic inhibitors
    • Errey JC, Lee SS, Gibson RP, Martinez Fleites C, Barry CS, et al. 2010. Mechanistic insight into enzymatic glycosyl transfer with retention of configuration through analysis of glycomimetic inhibitors. Angew. Chem. Int. Ed. Engl. 49(7):1234-37
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , Issue.7 , pp. 1234-1237
    • Errey, J.C.1    Lee, S.S.2    Gibson, R.P.3    Martinez Fleites, C.4    Barry, C.S.5
  • 81
    • 80855133537 scopus 로고    scopus 로고
    • The molecular mechanism of enzymatic glycosyl transfer with retention of configuration: Evidence for a short-lived oxocarbenium-like species
    • Ardèvol A, Rovira C. 2011. The molecular mechanism of enzymatic glycosyl transfer with retention of configuration: evidence for a short-lived oxocarbenium-like species. Angew. Chem. Int. Ed. Engl. 50(46):10897-901
    • (2011) Angew. Chem. Int. Ed. Engl. , vol.50 , Issue.46 , pp. 10897-10901
    • Ardèvol, A.1    Rovira, C.2
  • 82
    • 84925945606 scopus 로고    scopus 로고
    • Exploring reaction pathways for O-GlcNAc transferase catalysis. A string method study
    • Kumari M, Kozmon S, Kulhánek P, ? Stepán J, Tvaro?ska I, Ko?ca J. 2015. Exploring reaction pathways for O-GlcNAc transferase catalysis. A string method study. J. Phys. Chem. B 119(12):4371-81
    • (2015) J. Phys. Chem. B , vol.119 , Issue.12 , pp. 4371-4381
    • Kumari, M.1    Kozmon, S.2    Kulhánek, P.3    Stepán, J.4    Tvaroska, I.5    Koca, J.6
  • 83
    • 0034646669 scopus 로고    scopus 로고
    • Functional expression of O-linkedGlcNAc transferase. Domain structure and substrate specificity
    • LubasWA, Hanover JA. 2000. Functional expression of O-linkedGlcNAc transferase. Domain structure and substrate specificity. J. Biol. Chem. 275(15):10983-88
    • (2000) J. Biol. Chem. , vol.275 , Issue.15 , pp. 10983-10988
    • Lubas, W.A.1    Hanover, J.A.2
  • 84
    • 84860871127 scopus 로고    scopus 로고
    • Insights into O-linked N-acetylglucosamine (O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and OGlcNAcase activity on protein substrates
    • Shen DL, Gloster TM, Yuzwa SA, Vocadlo DJ. 2012. Insights into O-linked N-acetylglucosamine (O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and OGlcNAcase activity on protein substrates. J. Biol. Chem. 287(19):15395-408
    • (2012) J. Biol. Chem. , vol.287 , Issue.19 , pp. 15395-15408
    • Shen, D.L.1    Gloster, T.M.2    Yuzwa, S.A.3    Vocadlo, D.J.4
  • 85
    • 0033527739 scopus 로고    scopus 로고
    • Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats
    • Kreppel LK, Hart GW. 1999. Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats. J. Biol. Chem. 274(45):32015-22
    • (1999) J. Biol. Chem. , vol.274 , Issue.45 , pp. 32015-32022
    • Kreppel, L.K.1    Hart, G.W.2
  • 86
    • 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 RP, Geisler TS, Chambers JH, McClain DA. 2009. Up-regulation of O-GlcNAc transferase with glucose deprivation in HepG2 cells is mediated by decreased hexosamine pathway flux. J. Biol. Chem. 284(6):3425-32
    • (2009) J. Biol. Chem. , vol.284 , Issue.6 , pp. 3425-3432
    • Taylor, R.P.1    Geisler, T.S.2    Chambers, J.H.3    McClain, D.A.4
  • 87
    • 0020469152 scopus 로고
    • Activation by dolichol phosphate-mannose of the biosynthesis of N-acetylglucosaminylpyrophosphoryl polyprenols by the retina
    • Kean EL. 1982. Activation by dolichol phosphate-mannose of the biosynthesis of N-acetylglucosaminylpyrophosphoryl polyprenols by the retina. J. Biol. Chem. 257(14):7952-54
    • (1982) J. Biol. Chem. , vol.257 , Issue.14 , pp. 7952-7954
    • Kean, E.L.1
  • 88
    • 79955475591 scopus 로고    scopus 로고
    • Denitrosylation of S-nitrosylated OGT is triggered in LPS-stimulated innate immune response
    • Ryu I-H, Do S-I. 2011. Denitrosylation of S-nitrosylated OGT is triggered in LPS-stimulated innate immune response. Biochem. Biophys. Res. Commun. 408(1):52-57
    • (2011) Biochem. Biophys. Res. Commun. , vol.408 , Issue.1 , pp. 52-57
    • Ryu, I.-H.1    Do, S.-I.2
  • 89
    • 84901313642 scopus 로고    scopus 로고
    • AMPK regulates histone H2B O-GlcNAcylation
    • Xu Q, Yang C, Du Y, Chen Y, Liu H, et al. 2014. AMPK regulates histone H2B O-GlcNAcylation. Nucleic Acids Res. 42(9):5594-604
    • (2014) Nucleic Acids Res. , vol.42 , Issue.9 , pp. 5594-5604
    • Xu, Q.1    Yang, C.2    Du, Y.3    Chen, Y.4    Liu, H.5
  • 90
    • 84873351364 scopus 로고    scopus 로고
    • Glucose sensor O-GlcNAcylation coordinates with phosphorylation to regulate circadian clock
    • Kaasik K, Kivimäe S, Allen JJ, Chalkley RJ, Huang Y, et al. 2013. Glucose sensor O-GlcNAcylation coordinates with phosphorylation to regulate circadian clock. Cell Metab. 17(2):291-302
    • (2013) Cell Metab. , vol.17 , Issue.2 , pp. 291-302
    • Kaasik, K.1    Kivimäe, S.2    Allen, J.J.3    Chalkley, R.J.4    Huang, Y.5
  • 91
    • 84898613353 scopus 로고    scopus 로고
    • Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK)
    • Bullen JW, Balsbaugh JL, Chanda D, Shabanowitz J, Hunt DF, et al. 2014. Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK). J. Biol. Chem. 289(15):10592-606
    • (2014) J. Biol. Chem. , vol.289 , Issue.15 , pp. 10592-10606
    • Bullen, J.W.1    Balsbaugh, J.L.2    Chanda, D.3    Shabanowitz, J.4    Hunt, D.F.5
  • 92
    • 84919337950 scopus 로고    scopus 로고
    • O-GlcNAcase: Promiscuous hexosaminidase or key regulator of O-GlcNAc signaling?
    • Alonso J, Schimpl M, van Aalten DMF. 2014. O-GlcNAcase: Promiscuous hexosaminidase or key regulator of O-GlcNAc signaling? J. Biol. Chem. 289(50):34433-39
    • (2014) J. Biol. Chem. , vol.289 , Issue.50 , pp. 34433-34439
    • Alonso, J.1    Schimpl, M.2    Van Aalten, D.M.F.3
  • 93
    • 0026662974 scopus 로고
    • Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18
    • Chou CF, Smith AJ, Omary MB. 1992. Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18. J. Biol. Chem. 267(6):3901-6
    • (1992) J. Biol. Chem. , vol.267 , Issue.6 , pp. 3901-3906
    • Chou, C.F.1    Smith, A.J.2    Omary, M.B.3
  • 94
    • 0029670515 scopus 로고    scopus 로고
    • Dynamic O-GlcNAcylation of the small heat shock protein ?B-crystallin
    • Roquemore EP, Chevrier MR, Cotter RJ, Hart GW. 1996. Dynamic O-GlcNAcylation of the small heat shock protein ?B-crystallin. Biochemistry 35(11):3578-86
    • (1996) Biochemistry , vol.35 , Issue.11 , pp. 3578-3586
    • Roquemore, E.P.1    Chevrier, M.R.2    Cotter, R.J.3    Hart, G.W.4
  • 98
    • 84942321625 scopus 로고    scopus 로고
    • MTOR/MYC axis regulates O-GlcNAc transferase expression and O-GlcNAcylation in breast cancer
    • Sodi VL, Khaku S, Krutilina R, Schwab LP, Vocadlo DJ, et al. 2015. mTOR/MYC axis regulates O-GlcNAc transferase expression and O-GlcNAcylation in breast cancer. Mol. Cancer Res. 13(5):923-33
    • (2015) Mol. Cancer Res. , vol.13 , Issue.5 , pp. 923-933
    • Sodi, V.L.1    Khaku, S.2    Krutilina, R.3    Schwab, L.P.4    Vocadlo, D.J.5
  • 100
    • 77949273931 scopus 로고    scopus 로고
    • Control of herpesvirus IE gene expression by HCF-1 coupled chromatin modification activities
    • Kristie TM, Liang Y, Vogel JL. 2010. Control of herpesvirus IE gene expression by HCF-1 coupled chromatin modification activities. Biochim. Biophys. Acta 1799(3-4):257-65
    • (2010) Biochim. Biophys. Acta , vol.1799 , Issue.3 , pp. 257-265
    • Kristie, T.M.1    Liang, Y.2    Vogel, J.L.3
  • 101
    • 84864088377 scopus 로고    scopus 로고
    • Role of host cell factor-1 in cell cycle regulation
    • Zargar ZU, Tyagi S. 2012. Role of host cell factor-1 in cell cycle regulation. Transcription 3(4):187-92
    • (2012) Transcription , vol.3 , Issue.4 , pp. 187-192
    • Zargar, Z.U.1    Tyagi, S.2
  • 102
    • 0027328280 scopus 로고
    • The VP16 accessory protein HCF is a family of polypeptides processed from a large precursor protein
    • Wilson AC, LaMarco K, Peterson MG, HerrW. 1993. The VP16 accessory protein HCF is a family of polypeptides processed from a large precursor protein. Cell 74(1):115-25
    • (1993) Cell , vol.74 , Issue.1 , pp. 115-125
    • Wilson, A.C.1    LaMarco, K.2    Peterson, M.G.3    Herr, W.4
  • 103
    • 0028904801 scopus 로고
    • The cellular C1 factor of the herpes simplex virus enhancer complex is a family of polypeptides
    • Kristie TM, Pomerantz JL, Twomey TC, Parent SA, Sharp PA. 1995. The cellular C1 factor of the herpes simplex virus enhancer complex is a family of polypeptides. J. Biol. Chem. 270(9):4387-94
    • (1995) J. Biol. Chem. , vol.270 , Issue.9 , pp. 4387-4394
    • Kristie, T.M.1    Pomerantz, J.L.2    Twomey, T.C.3    Parent, S.A.4    Sharp, P.A.5
  • 104
    • 0038434062 scopus 로고    scopus 로고
    • The herpes simplex virus VP16-induced complex: Themakings of a regulatory switch
    • Wysocka J, HerrW. 2003. The herpes simplex virus VP16-induced complex: Themakings of a regulatory switch. Trends Biochem. Sci. 28(6):294-304
    • (2003) Trends Biochem. Sci. , vol.28 , Issue.6 , pp. 294-304
    • Wysocka, J.1    Herr, W.2
  • 105
    • 0038242360 scopus 로고    scopus 로고
    • Proteolytic processing is necessary to separate and ensure proper cell growth and cytokinesis functions of HCF-1
    • Julien E, Herr W. 2003. Proteolytic processing is necessary to separate and ensure proper cell growth and cytokinesis functions of HCF-1. EMBO J. 22(10):2360-69
    • (2003) EMBO J. , vol.22 , Issue.10 , pp. 2360-2369
    • Julien, E.1    Herr, W.2
  • 106
    • 0032563246 scopus 로고    scopus 로고
    • Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin ?
    • Conti E, Uy M, Leighton L, Blobel G, Kuriyan J. 1998. Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin ?. Cell 94(2):193-204
    • (1998) Cell , vol.94 , Issue.2 , pp. 193-204
    • Conti, E.1    Uy, M.2    Leighton, L.3    Blobel, G.4    Kuriyan, J.5
  • 107
    • 0033664345 scopus 로고    scopus 로고
    • Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5
    • Gatto GJ, Geisbrecht BV, Gould SJ, Berg JM. 2000. Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5. Nat. Struct. Mol. Biol. 7(12):1091-95
    • (2000) Nat. Struct. Mol. Biol. , vol.7 , Issue.12 , pp. 1091-1095
    • Gatto, G.J.1    Geisbrecht, B.V.2    Gould, S.J.3    Berg, J.M.4
  • 108
    • 0037648473 scopus 로고    scopus 로고
    • Identification and cloning of a novel family of coiled-coil domain proteins that interact with O-GlcNAc transferase
    • Iyer SPN, Akimoto Y, HartGW. 2003. Identification and cloning of a novel family of coiled-coil domain proteins that interact with O-GlcNAc transferase. J. Biol. Chem. 278(7):5399-409
    • (2003) J. Biol. Chem. , vol.278 , Issue.7 , pp. 5399-5409
    • Iyer, S.P.N.1    Akimoto, Y.2    Hart, G.W.3
  • 109
    • 84903975888 scopus 로고    scopus 로고
    • Glucose regulates mitochondrial motility via Milton modification by O-GlcNAc transferase
    • Pekkurnaz G, Trinidad JC, Wang X, Kong D, Schwarz TL. 2014. Glucose regulates mitochondrial motility via Milton modification by O-GlcNAc transferasE. Cell 158(1):54-68
    • (2014) Cell , vol.158 , Issue.1 , pp. 54-68
    • Pekkurnaz, G.1    Trinidad, J.C.2    Wang, X.3    Kong, D.4    Schwarz, T.L.5
  • 110
    • 23844481789 scopus 로고    scopus 로고
    • A Caenorhabditis elegans model of insulin resistance: Altered macronutrient storage and dauer formation in an OGT-1 knockout
    • Hanover JA, Forsythe ME, Hennessey PT, Brodigan TM, Love DC, et al. 2005. A Caenorhabditis elegans model of insulin resistance: Altered macronutrient storage and dauer formation in an OGT-1 knockout. PNAS 102(32):11266-71
    • (2005) PNAS , vol.102 , Issue.32 , pp. 11266-11271
    • Hanover, J.A.1    Forsythe, M.E.2    Hennessey, P.T.3    Brodigan, T.M.4    Love, D.C.5
  • 111
    • 0021670304 scopus 로고
    • A gene that regulates the bithorax complex differentially in larval and adult cells of Drosophila
    • Ingham PW. 1984. A gene that regulates the bithorax complex differentially in larval and adult cells of Drosophila. Cell 37(3):815-23
    • (1984) Cell , vol.37 , Issue.3 , pp. 815-823
    • Ingham, P.W.1
  • 112
    • 67650076327 scopus 로고    scopus 로고
    • Essential role of the glycosyltransferase Sxc/Ogt in polycomb repression
    • Gambetta MC, Oktaba K, Müller J. 2009. Essential role of the glycosyltransferase Sxc/Ogt in polycomb repression. Science 325(5936):93-96
    • (2009) Science , vol.325 , Issue.5936 , pp. 93-96
    • Gambetta, M.C.1    Oktaba, K.2    Müller, J.3
  • 113
    • 69449092638 scopus 로고    scopus 로고
    • Drosophila O-GlcNAc transferase (OGT) is encoded by the Polycomb group (PcG) gene, super sex combs (sxc)
    • Sinclair DA, Syrzycka M, MacauleyMS, RastgardaniT, Komljenovic I, et al. 2009. Drosophila O-GlcNAc transferase (OGT) is encoded by the Polycomb group (PcG) gene, super sex combs (sxc). PNAS 106(32):13427-32
    • (2009) PNAS , vol.106 , Issue.32 , pp. 13427-13432
    • Sinclair, D.A.1    Syrzycka, M.2    Macauley, M.S.3    Rastgardani, T.4    Komljenovic, I.5
  • 114
    • 84898778602 scopus 로고    scopus 로고
    • O-GlcNAc reports ambient temperature and confers heat resistance on ectotherm development
    • Radermacher PT, Myachina F, Bosshardt F, Pandey R, Mariappa D, et al. 2014. O-GlcNAc reports ambient temperature and confers heat resistance on ectotherm development. PNAS 111(15):5592-97
    • (2014) PNAS , vol.111 , Issue.15 , pp. 5592-5597
    • Radermacher, P.T.1    Myachina, F.2    Bosshardt, F.3    Pandey, R.4    Mariappa, D.5
  • 115
    • 79954500148 scopus 로고    scopus 로고
    • Intracellular protein glycosylation modulates insulin mediated lifespan in C. Elegans
    • Rahman MM, Stuchlick O, El-Karim EG, Stuart R, Kipreos ET, Wells L. 2010. Intracellular protein glycosylation modulates insulin mediated lifespan in C. Elegans. Aging 2(10):678-90
    • (2010) Aging , vol.2 , Issue.10 , pp. 678-690
    • Rahman, M.M.1    Stuchlick, O.2    El-Karim, E.G.3    Stuart, R.4    Kipreos, E.T.5    Wells, L.6
  • 116
    • 77952171341 scopus 로고    scopus 로고
    • Dynamic O-GlcNAc cycling at promoters of Caenorhabditis elegans genes regulating longevity, stress, and immunity
    • Love DC, Ghosh S, Mondoux MA, Fukushige T, Wang P, et al. 2010. Dynamic O-GlcNAc cycling at promoters of Caenorhabditis elegans genes regulating longevity, stress, and immunity. PNAS 107(16):7413-18
    • (2010) PNAS , vol.107 , Issue.16 , pp. 7413-7418
    • Love, D.C.1    Ghosh, S.2    Mondoux, M.A.3    Fukushige, T.4    Wang, P.5
  • 117
    • 84877358993 scopus 로고    scopus 로고
    • Nutrient-driven O-GlcNAc cycling influences autophagic flux and neurodegenerative proteotoxicity
    • Wang P, Hanover JA. 2013. Nutrient-driven O-GlcNAc cycling influences autophagic flux and neurodegenerative proteotoxicity. Autophagy 9(4):604-6
    • (2013) Autophagy , vol.9 , Issue.4 , pp. 604-606
    • Wang, P.1    Hanover, J.A.2
  • 118
    • 84925284243 scopus 로고    scopus 로고
    • O-GlcNAc-modification of SNAP-29 regulates autophagosome maturation
    • Guo B, Liang Q, Li L, Hu Z, Wu F, et al. 2014. O-GlcNAc-modification of SNAP-29 regulates autophagosome maturation. Nat. Cell Biol. 16(12):1215-26
    • (2014) Nat. Cell Biol. , vol.16 , Issue.12 , pp. 1215-1226
    • Guo, B.1    Liang, Q.2    Li, L.3    Hu, Z.4    Wu, F.5
  • 119
    • 84956657857 scopus 로고    scopus 로고
    • Conserved nutrient sensor O-GlcNAc transferase is integral to C. Elegans pathogen-specific immunity
    • Bond MR, Ghosh SK, Wang P, Hanover JA. 2014. Conserved nutrient sensor O-GlcNAc transferase is integral to C. Elegans pathogen-specific immunity. PlOS ONE 9(12):e113231
    • (2014) PlOS ONE , vol.9 , Issue.12 , pp. e113231
    • Bond, M.R.1    Ghosh, S.K.2    Wang, P.3    Hanover, J.A.4
  • 120
    • 0019731694 scopus 로고
    • Staging the metamorphosis of Drosophila melanogaster
    • Bainbridge SP, Bownes M. 1981. Staging the metamorphosis of Drosophila melanogaster. Development 66(1):57-80
    • (1981) Development , vol.66 , Issue.1 , pp. 57-80
    • Bainbridge, S.P.1    Bownes, M.2
  • 121
    • 0022521845 scopus 로고
    • Spatial regulation of antennapedia and bithorax gene expression by the Polycomb locus in Drosophila
    • Wedeen C, HardingK, Levine M. 1986. Spatial regulation of antennapedia and bithorax gene expression by the Polycomb locus in Drosophila. Cell 44(5):739-48
    • (1986) Cell , vol.44 , Issue.5 , pp. 739-748
    • Wedeen, C.1    Harding, K.2    Levine, M.3
  • 122
    • 84876871047 scopus 로고    scopus 로고
    • Occupying chromatin: Polycomb mechanisms for getting to genomic targets, stopping transcriptional traffic, and staying put
    • Simon JA, Kingston RE. 2013. Occupying chromatin: polycomb mechanisms for getting to genomic targets, stopping transcriptional traffic, and staying put. Mol. Cell. 49(5):808-24
    • (2013) Mol. Cell. , vol.49 , Issue.5 , pp. 808-824
    • Simon, J.A.1    Kingston, R.E.2
  • 123
    • 84962310803 scopus 로고    scopus 로고
    • Dual functionality ofO-GlcNAc transferase is required for Drosophila development
    • Mariappa D, Zheng X, Schimpl M, RaimiO, Ferenbach AT, et al. 2015. Dual functionality ofO-GlcNAc transferase is required for Drosophila development. Open Biol. 5(12):150234
    • (2015) Open Biol. , vol.5 , Issue.12 , pp. 150234
    • Mariappa, D.1    Zheng, X.2    Schimpl, M.3    Raimi, O.4    Ferenbach, A.T.5
  • 124
    • 84918582083 scopus 로고    scopus 로고
    • O-GlcNAcylation prevents aggregation of the Polycomb group repressor Polyhomeotic
    • Gambetta MC, Müller J. 2014. O-GlcNAcylation prevents aggregation of the Polycomb group repressor Polyhomeotic. Dev. Cell 31(5):629-39
    • (2014) Dev. Cell , vol.31 , Issue.5 , pp. 629-639
    • Gambetta, M.C.1    Müller, J.2
  • 125
    • 84863337963 scopus 로고    scopus 로고
    • The growth-suppressive function of the Polycomb group protein Polyhomeotic is mediated by polymerization of its sterile alpha motif (SAM) domain
    • Robinson AK, Leal BZ, Chadwell LV, Wang R, Ilangovan U, et al. 2012. The growth-suppressive function of the Polycomb group protein Polyhomeotic is mediated by polymerization of its sterile alpha motif (SAM) domain. J. Biol. Chem. 287(12):8702-13
    • (2012) J. Biol. Chem. , vol.287 , Issue.12 , pp. 8702-8713
    • Robinson, A.K.1    Leal, B.Z.2    Chadwell, L.V.3    Wang, R.4    Ilangovan, U.5
  • 126
    • 84884725454 scopus 로고    scopus 로고
    • SAMdomain polymerization links subnuclear clustering of PRC1 to gene silencing
    • Isono K, Endo TA, KuM, YamadaD, SuzukiR, et al. 2013. SAMdomain polymerization links subnuclear clustering of PRC1 to gene silencing. Dev. Cell 26(6):565-77
    • (2013) Dev. Cell , vol.26 , Issue.6 , pp. 565-577
    • Isono, K.1    Endo, T.A.2    Ku, M.3    Yamada, D.4    Suzuki, R.5
  • 127
    • 0027321548 scopus 로고
    • Derivation of completely cell culture-derived mice from early-passage embryonic stem cells
    • Nagy A, Rossant J, Nagy R, Abramow-Newerly W, Roder JC. 1993. Derivation of completely cell culture-derived mice from early-passage embryonic stem cells. PNAS 90(18):8424-28
    • (1993) PNAS , vol.90 , Issue.18 , pp. 8424-8428
    • Nagy, A.1    Rossant, J.2    Nagy, R.3    Abramow-Newerly, W.4    Roder, J.C.5
  • 128
    • 84888617099 scopus 로고    scopus 로고
    • Organizing principles ofmammalian nonsense-mediatedmRNAdecay
    • Popp MW-L, Maquat LE. 2013. Organizing principles ofmammalian nonsense-mediatedmRNAdecay. Annu. Rev. Genet. 47:139-65
    • (2013) Annu. Rev. Genet. , vol.47 , pp. 139-165
    • Popp , M.W.L.1    Maquat, L.E.2
  • 129
    • 0011032639 scopus 로고    scopus 로고
    • Spermatogenesis
    • Sunderland, MA: Sinauer Associates. 6th ed.
    • Gilbert SF. 2000. Spermatogenesis. In Developmental Biology. Sunderland, MA: Sinauer Associates. 6th ed.
    • (2000) Developmental Biology
    • Gilbert, S.F.1
  • 130
    • 0031443874 scopus 로고    scopus 로고
    • Protamine-Cre recombinase transgenes efficiently recombine target sequences in themale germ line ofmice, but not in embryonic stem cells
    • O'Gorman S, Dagenais NA, Qian M, Marchuk Y. 1997. Protamine-Cre recombinase transgenes efficiently recombine target sequences in themale germ line ofmice, but not in embryonic stem cells. PNAS 94(26):14602-7
    • (1997) PNAS , vol.94 , Issue.26 , pp. 14602-14607
    • O'Gorman, S.1    Dagenais, N.A.2    Qian, M.3    Marchuk, Y.4
  • 131
    • 84875500069 scopus 로고    scopus 로고
    • O-GlcNAc transferase (OGT) as a placental biomarker of maternal stress and reprogramming of CNS gene transcription in development
    • Howerton CL, Morgan CP, Fischer DB, Bale TL. 2013. O-GlcNAc transferase (OGT) as a placental biomarker of maternal stress and reprogramming of CNS gene transcription in development. PNAS 110(13):5169-74
    • (2013) PNAS , vol.110 , Issue.13 , pp. 5169-5174
    • Howerton, C.L.1    Morgan, C.P.2    Fischer, D.B.3    Bale, T.L.4
  • 132
    • 84903721712 scopus 로고    scopus 로고
    • Targeted placental deletion of OGT recapitulates the prenatal stress phenotype including hypothalamic mitochondrial dysfunction
    • Howerton CL, Bale TL. 2014. Targeted placental deletion of OGT recapitulates the prenatal stress phenotype including hypothalamic mitochondrial dysfunction. PNAS 111(26):9639-44
    • (2014) PNAS , vol.111 , Issue.26 , pp. 9639-9644
    • Howerton, C.L.1    Bale, T.L.2
  • 133
    • 0016692463 scopus 로고
    • Preferential inactivation of the paternally derived X chromosome in the extraembryonic membranes of the mouse
    • Takagi N, Sasaki M. 1975. Preferential inactivation of the paternally derived X chromosome in the extraembryonic membranes of the mouse. Nature 256(5519):640-42
    • (1975) Nature , vol.256 , Issue.5519 , pp. 640-642
    • Takagi, N.1    Sasaki, M.2
  • 134
    • 18944397611 scopus 로고    scopus 로고
    • Selective expression of the Cre recombinase in late-stage thymocytes using the distal promoter of the Lck gene
    • Zhang DJ, Wang Q, Wei J, Baimukanova G, Buchholz F, et al. 2005. Selective expression of the Cre recombinase in late-stage thymocytes using the distal promoter of the Lck gene. J. Immunol. 174(11):6725-31
    • (2005) J. Immunol. , vol.174 , Issue.11 , pp. 6725-6731
    • Zhang, D.J.1    Wang, Q.2    Wei, J.3    Baimukanova, G.4    Buchholz, F.5
  • 136
    • 0030878260 scopus 로고    scopus 로고
    • Gene recombination in postmitotic cells. Targeted expression of Cre recombinase provokes cardiac-restricted, site-specific rearrangement in adult ventricular muscle in vivo
    • Agah R, Frenkel PA, French BA, Michael LH, Overbeek PA, Schneider MD. 1997. Gene recombination in postmitotic cells. Targeted expression of Cre recombinase provokes cardiac-restricted, site-specific rearrangement in adult ventricular muscle in vivo. J. Clin. Invest. 100(1):169-79
    • (1997) J. Clin. Invest. , vol.100 , Issue.1 , pp. 169-179
    • Agah, R.1    Frenkel, P.A.2    French, B.A.3    Michael, L.H.4    Overbeek, P.A.5    Schneider, M.D.6
  • 137
    • 78049279413 scopus 로고    scopus 로고
    • O-linked Nacetylglucosamine transferase is indispensable in the failing heart
    • Watson LJ, Facundo HT, Ngoh GA, Ameen M, Brainard RE, et al. 2010. O-linked Nacetylglucosamine transferase is indispensable in the failing heart. PNAS 107(41):17797-802
    • (2010) PNAS , vol.107 , Issue.41 , pp. 17797-17802
    • Watson, L.J.1    Facundo, H.T.2    Ngoh, G.A.3    Ameen, M.4    Brainard, R.E.5
  • 138
    • 84952876590 scopus 로고    scopus 로고
    • Disruption ofO-linked N-acetylglucosamine signaling induces ER stress and ?cell failure
    • Alejandro EU, Bozadjieva N, KumusogluD, Abdulhamid S, Levine H, et al. 2015. Disruption ofO-linked N-acetylglucosamine signaling induces ER stress and ?cell failurE. Cell Rep. 13(11):2527-38
    • (2015) Cell Rep. , vol.13 , Issue.11 , pp. 2527-2538
    • Alejandro, E.U.1    Bozadjieva, N.2    Kumusoglu, D.3    Abdulhamid, S.4    Levine, H.5
  • 139
    • 84901946068 scopus 로고    scopus 로고
    • O-GlcNAcylation regulates cancer metabolism and survival stress signaling via regulation of the HIF-1 pathway
    • FerrerCM, LynchTP, Sodi VL, Falcone JN, Schwab LP, et al. 2014. O-GlcNAcylation regulates cancer metabolism and survival stress signaling via regulation of the HIF-1 pathway. Mol. Cell 54(5):820-31
    • (2014) Mol. Cell , vol.54 , Issue.5 , pp. 820-831
    • Ferrer, C.M.1    Lynch, T.P.2    Sodi, V.L.3    Falcone, J.N.4    Schwab, L.P.5
  • 140
    • 78649640325 scopus 로고    scopus 로고
    • Blocking O-linkedGlcNAc cycling in Drosophila insulin-producing cells perturbs glucose-insulin homeostasis
    • Sekine O, Love DC, Rubenstein DS, Hanover JA. 2010. Blocking O-linkedGlcNAc cycling in Drosophila insulin-producing cells perturbs glucose-insulin homeostasis. J. Biol. Chem. 285(49):38684-91
    • (2010) J. Biol. Chem. , vol.285 , Issue.49 , pp. 38684-38691
    • Sekine, O.1    Love, D.C.2    Rubenstein, D.S.3    Hanover, J.A.4
  • 141
    • 0037117511 scopus 로고    scopus 로고
    • Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes
    • Vosseller K, Wells L, Lane MD, Hart GW. 2002. Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes. PNAS 99(8):5313-18
    • (2002) PNAS , vol.99 , Issue.8 , pp. 5313-5318
    • Vosseller, K.1    Wells, L.2    Lane, M.D.3    Hart, G.W.4
  • 142
    • 0036679303 scopus 로고    scopus 로고
    • Altered glycan-dependent signaling induces insulin resistance and hyperleptinemia
    • McClain DA, Lubas WA, Cooksey RC, Hazel M, Parker GJ, et al. 2002. Altered glycan-dependent signaling induces insulin resistance and hyperleptinemia. PNAS 99(16):10695-99
    • (2002) PNAS , vol.99 , Issue.16 , pp. 10695-10699
    • McClain, D.A.1    Lubas, W.A.2    Cooksey, R.C.3    Hazel, M.4    Parker, G.J.5
  • 143
    • 9544226451 scopus 로고    scopus 로고
    • Overexpression of glutamine: Fructose-6-phosphate amidotransferase in transgenic mice leads to insulin resistance
    • Hebert LF, Daniels MC, Zhou J, Crook ED, Turner RL, et al. 1996. Overexpression of glutamine:fructose-6-phosphate amidotransferase in transgenic mice leads to insulin resistance. J. Clin. Invest. 98(4):930-36
    • (1996) J. Clin. Invest. , vol.98 , Issue.4 , pp. 930-936
    • Hebert, L.F.1    Daniels, M.C.2    Zhou, J.3    Crook, E.D.4    Turner, R.L.5
  • 144
    • 77949769388 scopus 로고    scopus 로고
    • O-linked N-acetylglucosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress
    • Butkinaree C, Park K, Hart GW. 2010. O-linked N-acetylglucosamine (O-GlcNAc): extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress. Biochim. Biophys. Acta 1800(2):96-106
    • (2010) Biochim. Biophys. Acta , vol.1800 , Issue.2 , pp. 96-106
    • Butkinaree, C.1    Park, K.2    Hart, G.W.3
  • 145
    • 3042534011 scopus 로고    scopus 로고
    • Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress. A survival response of mammalian cells
    • Zachara NE, O'Donnell N, Cheung WD, Mercer JJ, Marth JD, Hart GW. 2004. Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress. A survival response of mammalian cells. J. Biol. Chem. 279(29):30133-42
    • (2004) J. Biol. Chem. , vol.279 , Issue.29 , pp. 30133-30142
    • Zachara, N.E.1    O'Donnell, N.2    Cheung, W.D.3    Mercer, J.J.4    Marth, J.D.5    Hart, G.W.6
  • 146
    • 84867908726 scopus 로고    scopus 로고
    • O-GlcNAc cycling mutants modulate proteotoxicity in Caenorhabditis elegans models of human neurodegenerative diseases
    • Wang P, Lazarus BD, Forsythe ME, Love DC, Krause MW, Hanover JA. 2012. O-GlcNAc cycling mutants modulate proteotoxicity in Caenorhabditis elegans models of human neurodegenerative diseases. PNAS 109(43):17669-74
    • (2012) PNAS , vol.109 , Issue.43 , pp. 17669-17674
    • Wang, P.1    Lazarus, B.D.2    Forsythe, M.E.3    Love, D.C.4    Krause, M.W.5    Hanover, J.A.6
  • 147
    • 84975275158 scopus 로고    scopus 로고
    • Post-translational O-GlcNAcylation is essential for nuclear pore integrity and maintenance of the pore selectivity filter
    • Zhu Y, Liu T-W, Madden Z, Yuzwa SA, Murray K, et al. 2016. Post-translational O-GlcNAcylation is essential for nuclear pore integrity and maintenance of the pore selectivity filter. J. Mol. Cell Biol. 8(1):2-16
    • (2016) J. Mol. Cell Biol. , vol.8 , Issue.1 , pp. 2-16
    • Zhu, Y.1    Liu, T.-W.2    Madden, Z.3    Yuzwa, S.A.4    Murray, K.5
  • 148
    • 84860872762 scopus 로고    scopus 로고
    • O-GlcNAcase is essential for embryonic development and maintenance of genomic stability
    • Yang YR, Song M, Lee H, Jeon Y, Choi EJ, et al. 2012. O-GlcNAcase is essential for embryonic development and maintenance of genomic stability. Aging Cell 11(3):439-48
    • (2012) Aging Cell , vol.11 , Issue.3 , pp. 439-448
    • Yang, Y.R.1    Song, M.2    Lee, H.3    Jeon, Y.4    Choi, E.J.5
  • 149
    • 84924898037 scopus 로고    scopus 로고
    • Conditional knock-out reveals a requirement for O-linked N-Acetylglucosaminase (O-GlcNAcase) in metabolic homeostasis
    • Keembiyehetty C, Love DC, Harwood KR, Gavrilova O, Comly ME, Hanover JA. 2015. Conditional knock-out reveals a requirement for O-linked N-Acetylglucosaminase (O-GlcNAcase) in metabolic homeostasis. J. Biol. Chem. 290(11):7097-113
    • (2015) J. Biol. Chem. , vol.290 , Issue.11 , pp. 7097-7113
    • Keembiyehetty, C.1    Love, D.C.2    Harwood, K.R.3    Gavrilova, O.4    Comly, M.E.5    Hanover, J.A.6
  • 150
    • 0032961174 scopus 로고    scopus 로고
    • Selected elements of herpes simplex virus accessory factor HCF are highly conserved in Caenorhabditis elegans
    • Liu Y, HengartnerMO, Herr W. 1999. Selected elements of herpes simplex virus accessory factor HCF are highly conserved in Caenorhabditis elegans. Mol. Cell. Biol. 19(1):909-15
    • (1999) Mol. Cell. Biol. , vol.19 , Issue.1 , pp. 909-915
    • Liu, Y.1    Hengartner, M.O.2    Herr, W.3
  • 151
    • 0030667738 scopus 로고    scopus 로고
    • Concerted activity of host cell factor subregions in promoting stable VP16 complex assembly and preventing interference by the acidic activation domain
    • LaBoissière S, Walker S, O'Hare P. 1997. Concerted activity of host cell factor subregions in promoting stable VP16 complex assembly and preventing interference by the acidic activation domain. Mol. Cell. Biol. 17(12):7108-18
    • (1997) Mol. Cell. Biol. , vol.17 , Issue.12 , pp. 7108-7118
    • LaBoissière, S.1    Walker, S.2    O'Hare, P.3
  • 152
    • 35148901465 scopus 로고    scopus 로고
    • Species selectivity of mixed-lineage leukemia/trithorax and HCF proteolytic maturation pathways
    • Capotosti F, Hsieh JJ-D, Herr W. 2007. Species selectivity of mixed-lineage leukemia/trithorax and HCF proteolytic maturation pathways. Mol. Cell. Biol. 27(20):7063-72
    • (2007) Mol. Cell. Biol. , vol.27 , Issue.20 , pp. 7063-7072
    • Capotosti, F.1    Hsieh, J.J.-D.2    Herr, W.3


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