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Cross Talk Between O-GlcNAcylation and Phosphorylation: Roles in Signaling, Transcription, and Chronic Disease
Open accessAbstract
O-GlcNAcylation is the addition of β-D-N-acetylglucosamine to serine or threonine residues of nuclear and cytoplasmic proteins. O-linked N-acetylglucosamine (O-GlcNAc) was not discovered until the early 1980s and still remains difficult to detect and quantify. Nonetheless, O-GlcNAc is highly abundant and cycles on proteins with a timescale similar to protein phosphorylation. O-GlcNAc occurs in organisms ranging from some bacteria to protozoans and metazoans, including plants and nematodes up the evolutionary tree to man. O-GlcNAcylation is mostly on nuclear proteins, but it occurs in all intracellular compartments, including mitochondria. Recent glycomic analyses have shown that O-GlcNAcylation has surprisingly extensive cross talk with phosphorylation, where it serves as a nutrient/stress sensor to modulate signaling, transcription, and cytoskeletal functions. Abnormal amounts of O-GlcNAcylation underlie the etiology of insulin resistance and glucose toxicity in diabetes, and this type of modification plays a direct role in neurodegenerative disease. Many oncogenic proteins and tumor suppressor proteins are also regulated by O-GlcNAcylation. Current data justify extensive efforts toward a better understanding of this invisible, yet abundant, modification. As tools for the study of O-GlcNAc become more facile and available, exponential growth in this area of research will eventually take place.
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“there seems to be a limited number of forms of intracellular glycosylation, with a single modi fi cation ( O -GlcNAc) numerically dominating the scene (647 -648).”
From Biological roles of glycans (2017) · cites this paper as [648]
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Cites
The protein kinase complement of the human genome
Manning, G., Whyte, D. B., Martinez, R., Hunter, T., & Sudarsanam, S. (2002) · Science · doi:10.1126/science.1075762 · Cited by 8,145
Lysine acetylation targets protein complexes and co-regulates major cellular functions
Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040
Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
Syka, J. E. P., Coon, J. J., Schroeder, M. J., Shabanowitz, J., & Hunt, D. F. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402700101 · Cited by 2,370
Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins
Hart, G. W., Housley, M. P., & Slawson, C. (2007) · Nature · doi:10.1038/nature05815 · Cited by 1,418
Self-citationLarge-scale characterization of HeLa cell nuclear phosphoproteins
Beausoleil, S. A., Jedrychowski, M. P., Schwartz, D., Elias, J. E., Villén, J., Li, J., Cohn, M. A., Cantley, L. C., & Gygi, S. P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404720101 · Cited by 1,376
Du, X.-L., Edelstein, D., Rossetti, L., Fantus, I. G., Goldberg, H. J., Ziyadeh, F. N., Wu, J., & Brownlee, M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.22.12222 · Cited by 1,152
Torres, C., & Hart, G. W. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43295-9 · Cited by 1,132
Self-citationMarshall, S., Bacote, V., & Traxinger, R. R. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67706-9 · Cited by 1,049
Glycosylation of Nucleocytoplasmic Proteins: Signal Transduction and O-GlcNAc
Wells, L., Vosseller, K., & Hart, G. W. (2001) · Science · doi:10.1126/science.1058714 · Cited by 959
Self-citationProtein phosphatase 1 – targeted in many directions
Cohen, P. T. W. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.2.241 · Cited by 922
Du, X. L., Edelstein, D., Dimmeler, S., Ju, Q., Sui, C., & Brownlee, M. (2001) · Journal of Clinical Investigation · doi:10.1172/jci11235 · Cited by 907
Jackson, S. P., & Tjian, R. (1988) · Cell · doi:10.1016/0092-8674(88)90015-3 · Cited by 901
The Mechanism of Ca2+-Dependent Regulation of Kinesin-Mediated Mitochondrial Motility
Wang, X., & Schwarz, T. L. (2009) · Cell · doi:10.1016/j.cell.2008.11.046 · Cited by 871
Shafi, R., Iyer, S. P. N., Ellies, L. G., O'Donnell, N., Marek, K. W., Chui, D., Hart, G. W., & Marth, J. D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.100471497 · Cited by 796
Self-citationO-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease
Liu, F., Iqbal, K., Grundke-Iqbal, I., Hart, G. W., & Gong, C.-X. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400348101 · Cited by 775
Self-citationDynamic O-Glycosylation of Nuclear and Cytosolic Proteins
Gao, Y., Wells, L., Comer, F. I., Parker, G. J., & Hart, G. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010420200 · Cited by 757
Self-citationDynamic Glycosylation of Nuclear and Cytosolic Proteins
Kreppel, L. K., Blomberg, M. A., & Hart, G. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.14.9308 · Cited by 747
Self-citationA potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo
Yuzwa, S. A., Macauley, M. S., Heinonen, J. E., Shan, X., Dennis, R. J., He, Y., Whitworth, G. E., Stubbs, K. A., McEachern, E. J., Davies, G. J., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.96 · Cited by 717
Recruitment of RNA polymerase III to its target promotersPreprint
Schramm, L., & Hernandez, N. (2002) · Genes & Development · doi:10.1101/gad.1018902 · Cited by 646
Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance
Yang, X., Ongusaha, P. P., Miles, P. D. G., Havstad, J. C., Zhang, F., So, W. V., Kudlow, J. E., Michell, R. H., Olefsky, J. M., Field, S. J., et al. (2008) · Nature · doi:10.1038/nature06668 · Cited by 639
Dynamic O-GlcNAc Modification of Nucleocytoplasmic Proteins in Response to Stress
Zachara, N. E., O'Donnell, N., Cheung, W. D., Mercer, J. J., Marth, J. D., & Hart, G. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403773200 · Cited by 568
Self-citationLubas, W. A., Frank, D. W., Krause, M., & Hanover, J. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.14.9316 · Cited by 551
Alexander, G. E., Chen, K., Pietrini, P., Rapoport, S. I., & Reiman, E. M. (2002) · American Journal of Psychiatry · doi:10.1176/appi.ajp.159.5.738 · Cited by 532
Hexosamines, insulin resistance, and the complications of diabetes: current status
Buse, M. G. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00329.2005 · Cited by 528
Evidence for Genetic Linkage of Alzheimer's Disease to Chromosome 10q
Bertram, L., Blacker, D., Mullin, K., Keeney, D. B., Jones, J., Basu, S., Yhu, S., McInnis, M. G., Go, R. C. P., Vekrellis, K., et al. (2000) · Science · doi:10.1126/science.290.5500.2302 · Cited by 519
Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability
Yang, W. H., Kim, J. E., Nam, H. W., Ju, J., Kim, H. S., Kim, Y. S., & Cho, J. W. (2006) · Nature Cell Biology · doi:10.1038/ncb1470 · Cited by 510
Dong, D. L., & Hart, G. W. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32170-1 · Cited by 508
Self-citationDYNAMIC O-LINKED GLYCOSYLATION OF NUCLEAR AND CYTOSKELETAL PROTEINS
Hart, G. W. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.315 · Cited by 503
Self-citationHolt, G. D., & Hart, G. W. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)57510-x · Cited by 498
Self-citationVosseller, K., Wells, L., Lane, M. D., & Hart, G. W. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.072072399 · Cited by 494
Self-citationThe Hexosamine Signaling Pathway: Deciphering the "O-GlcNAc Code"
Love, D. C., & Hanover, J. A. (2005) · Science s STKE · doi:10.1126/stke.3122005re13 · Cited by 481
Chou, T.-Y., Hart, G. W., & Dang, C. V. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.18961 · Cited by 453
Self-citationHaltiwanger, R. S., Blomberg, M. A., & Hart, G. W. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50380-5 · Cited by 444
Self-citationNuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine.
Holt, G. D., Snow, C. M., Senior, A., Haltiwanger, R. S., Gerace, L., & Hart, G. W. (1987) · The Journal of Cell Biology · doi:10.1083/jcb.104.5.1157 · Cited by 444
Self-citationLiu, F., Shi, J., Tanimukai, H., Gu, J., Gu, J., Grundke-Iqbal, I., Iqbal, K., & Gong, C.-X. (2009) · Brain · doi:10.1093/brain/awp099 · Cited by 439
Zachara, N. E., & Hart, G. W. (2004) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2004.03.016 · Cited by 438
Self-citationO-GlcNAc Modification Is an Endogenous Inhibitor of the Proteasome
Zhang, F., Su, K., Yang, X., Bowe, D. B., Paterson, A. J., & Kudlow, J. E. (2003) · Cell · doi:10.1016/s0092-8674(03)00974-7 · Cited by 432
Ohn, T., Kedersha, N., Hickman, T. T., Tisdale, S., & Anderson, P. (2008) · Nature Cell Biology · doi:10.1038/ncb1783 · Cited by 431
O'Donnell, N., Zachara, N. E., Hart, G. W., & Marth, J. D. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.4.1680-1690.2004 · Cited by 431
Self-citationRegulation of a Cytosolic and Nuclear O-GlcNAc Transferase
Kreppel, L. K., & Hart, G. W. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.45.32015 · Cited by 425
Self-citationWells, L., Vosseller, K., Cole, R. N., Cronshaw, J. M., Matunis, M. J., & Hart, G. W. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200048-mcp200 · Cited by 421
Self-citationRNA polymerase II is a glycoprotein. Modification of the COOH-terminal domain by O-GlcNAc
Kelly, W. G., Dahmus, M. E., & Hart, G. W. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82216-5 · Cited by 407
Self-citationCaldwell, S. A., Jackson, S. R., Shahriari, K. S., Lynch, T. P., Sethi, G., Walker, S., Vosseller, K., & Reginato, M. J. (2010) · Oncogene · doi:10.1038/onc.2010.41 · Cited by 406
Cell signaling, the essential role of O-GlcNAc
Zachara, N. E., & Hart, G. W. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2006.04.007 · Cited by 386
GLYCOSYLATION IN THE NUCLEUS AND CYTOPLASM
Hart, G. W., Haltiwanger, R. S., Holt, G. D., & Kelly, W. G. (1989) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.58.070189.004205 · Cited by 386
Self-citationO-GlcNAcase Uses Substrate-assisted Catalysis
Macauley, M. S., Whitworth, G. E., Debowski, A. W., Chin, D., & Vocadlo, D. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413819200 · Cited by 385
Clark, R. J., McDonough, P. M., Swanson, E., Trost, S. U., Suzuki, M., Fukuda, M., & DILLMANN, W. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303810200 · Cited by 382
Haltiwanger, R. S., Holt, G. D., & Hart, G. W. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39838-2 · Cited by 372
Self-citationThe Microtubule-associated Protein Tau Is Extensively Modified with O-linked N-acetylglucosamine
Arnold, C. S., Johnson, G. W., Cole, R. N., Dong, D. L.-Y., Lee, M., & Hart, G. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.46.28741 · Cited by 361
Self-citationThe Cellular Fate of Glucose and Its Relevance in Type 2 Diabetes
Bouché, C., Serdy, S., Kahn, C. R., & Goldfine, A. B. (2004) · Endocrine Reviews · doi:10.1210/er.2003-0026 · Cited by 361
The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine
Hanover, J. A., Krause, M., & Love, D. C. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.07.017 · Cited by 352
O-GlcNAc Regulates FoxO Activation in Response to Glucose
Housley, M. P., Rodgers, J. T., Udeshi, N. D., Kelly, T. J., Shabanowitz, J., Hunt, D. F., Puigserver, P., & Hart, G. W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802240200 · Cited by 349
Self-citationO-GlcNAc signaling: a metabolic link between diabetes and cancer?
Slawson, C., Copeland, R. J., & Hart, G. W. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.005 · Cited by 346
Self-citationVosseller, K., Trinidad, J. C., Chalkley, R. J., Specht, C. G., Thalhammer, A., Lynn, A. J., Snedecor, J., Guan, S., Medzihradszky, K. F., Maltby, D. A., et al. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t500040-mcp200 · Cited by 346
Wang, Z., Guček, M., & Hart, G. W. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806216105 · Cited by 341
Self-citationHebert, L. F., Daniels, M. C., Zhou, J., Crook, E. D., Turner, R. L., Simmons, S. T., Neidigh, J. L., Zhu, J. S., Baron, A., & McClain, D. A. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118876 · Cited by 334
Extensive Crosstalk Between O-GlcNAcylation and Phosphorylation Regulates Cytokinesis
Wang, Z., Udeshi, N. D., Slawson, C. M., Compton, P. D., Sakabe, K., Cheung, W. D., Shabanowitz, J., Hunt, D. F., & Hart, G. W. (2010) · Science Signaling · doi:10.1126/scisignal.2000526 · Cited by 328
Self-citationHexosamines and Insulin Resistance
McClain, D. A., & Crook, E. D. (1996) · Diabetes · doi:10.2337/diab.45.8.1003 · Cited by 325
Essential Role of the Glycosyltransferase Sxc/Ogt in Polycomb Repression
Gambetta, M. C., Oktaba, K., & Müller, J. (2009) · Science · doi:10.1126/science.1169727 · Cited by 315
Zeidan, Q., & Hart, G. W. (2009) · Journal of Cell Science · doi:10.1242/jcs.053678 · Cited by 312
Self-citationFunctional Expression of O-linked GlcNAc Transferase
Lubas, W. A., & Hanover, J. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.15.10983 · Cited by 311
Ghosh, S., Blumenthal, H. J., Davidson, E. A., et al. (1960) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69397-4 · Cited by 295
Slawson, C. M., Zachara, N. E., Vosseller, K., Cheung, W. D., Lane, M. D., & Hart, G. W. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503396200 · Cited by 291
Self-citationReciprocity between O-GlcNAc and O-Phosphate on the Carboxyl Terminal Domain of RNA Polymerase II
Comer, F. I., & Hart, G. W. (2001) · Biochemistry · doi:10.1021/bi0027480 · Cited by 290
Self-citationKhidekel, N., Arndt, S., Lamarre-Vincent, N., et al. (2003) · Journal of the American Chemical Society · doi:10.1021/ja038545r · Cited by 289
Glycan-dependent signaling: O-linked N-acetylglucosamine
HANOVER, J. A. (2001) · The FASEB Journal · doi:10.1096/fj.01-0094rev · Cited by 283
Hanover, J. A., Cohen, C. K., Willingham, M. C., & Park, M. K. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48017-9 · Cited by 280
Wang, Z., Udeshi, N. D., O’Malley, M. M., Shabanowitz, J., Hunt, D. F., & Hart, G. W. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900268-mcp200 · Cited by 269
Self-citationHu, Y., Suárez, J., Fricovsky, E. S., Wang, H., Scott, B. T., Trauger, S. A., Han, W., Hu, Y., Oyeleye, M. O., & DILLMANN, W. H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m808518200 · Cited by 258
Cardioprotection by N -Acetylglucosamine Linkage to Cellular Proteins
Jones, S. P., Zachara, N. E., Ngoh, G. A., Hill, B. G., Teshima, Y., Bhatnagar, A., Hart, G. W., & Marbán, E. (2008) · Circulation · doi:10.1161/circulationaha.107.730515 · Cited by 258
Self-citationCopeland, R. J., Bullen, J. W., & Hart, G. W. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90281.2008 · Cited by 253
Self-citationO -GlcNAc modification in diabetes and Alzheimer's disease
Dias, W. B., & Hart, G. W. (2007) · Molecular BioSystems · doi:10.1039/b704905f · Cited by 253
Self-citationDiscovery of O- GlcNAc Transferase Inhibitors
Gross, B. J., Kraybill, B. C., & Walker, S. (2005) · Journal of the American Chemical Society · doi:10.1021/ja0555217 · Cited by 249
Cheung, W. D., & Hart, G. W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801222200 · Cited by 248
Self-citationHanover, J. A., Yu, S. D., Lubas, W. B., Shin, S., Ragano‐Caracciolo, M., Kochran, J., & Love, D. C. (2002) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(02)00578-7 · Cited by 246
The relationship between Alzheimer's disease and diabetes: Type 3 diabetes?
Kroner, Z. (2009) · PubMed · Cited by 246
Deng, Y., Li, B., Liu, Y. M., Iqbal, K., Grundke, I., & Gong, C. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.090157 · Cited by 233
Hu, Y., Belke, D. D., Suárez, J., Swanson, E., Clark, R., Hoshijima, M., & DILLMANN, W. H. (2005) · Circulation Research · doi:10.1161/01.res.0000165478.06813.58 · Cited by 228
Sinclair, D. A. R., Syrzycka, M., Macauley, M. S., Rastgardani, T., Komljenovic, I., Vocadlo, D. J., Brock, H. W., & Honda, B. M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904638106 · Cited by 227
Glycosylation of the c-Myc transactivation domain.
Chou, T., Dang, C. V., & Hart, G. W. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.10.4417 · Cited by 225
Self-citationHousley, M. P., Udeshi, N. D., Rodgers, J. T., Shabanowitz, J., Puigserver, P., Hunt, D. F., & Hart, G. W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m808890200 · Cited by 223
Self-citationToleman, C. A., Paterson, A. J., Whisenhunt, T. R., & Kudlow, J. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410406200 · Cited by 222
Hanover, J. A., Forsythe, M. E., Hennessey, P. T., Brodigan, T. M., Love, D. C., Ashwell, G., & Krause, M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408771102 · Cited by 218
A role for N-acetylglucosamine as a nutrient sensor and mediator of insulin resistance
Wells, L., Vosseller, K., & Hart, G. W. (2003) · Cellular and Molecular Life Sciences · doi:10.1007/s000180300017 · Cited by 217
Self-citationWang, Z., Pandey, A., & Hart, G. W. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600453-mcp200 · Cited by 217
Self-citationDynamic Interplay between O-Glycosylation and O-Phosphorylation of Nucleocytoplasmic Proteins
Kamemura, K., Hayes, B. K., Comer, F. I., & Hart, G. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201729200 · Cited by 216
Self-citationMitochondrial and nucleocytoplasmic targeting of O-linked GlcNAc transferase
Love, D. C., Kochran, J., Cathey, R. L., Shin, S., & Hanover, J. A. (2003) · Journal of Cell Science · doi:10.1242/jcs.00246 · Cited by 213
Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18.
Chou, C.-F., Smith, A. J., & Omary, M. B. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50611-1 · Cited by 212
Wells, L., & Hart, G. W. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00641-0 · Cited by 205
Self-citationDong, D. L., Xu, Z. S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., & Hart, G. W. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85471-6 · Cited by 204
Self-citationStructural insights into the mechanism and inhibition of eukaryotic O‐GlcNAc hydrolysis
Rao, F. V., Dorfmueller, H. C., Villa, F., Allwood, M. B., Eggleston, I. M., & van Aalten, D. M. F. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601026 · Cited by 202
Cytosolic O‐glycosylation is abundant in nerve terminals
Cole, R. N., & Hart, G. W. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00655.x · Cited by 201
Self-citationIyer, S. P. N., & Hart, G. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300036200 · Cited by 200
Self-citationLoss of p53 enhances catalytic activity of IKKβ through O-linked β-N-acetyl glucosamine modification
Kawauchi, K., Araki, K., Tobiume, K., & Tanaka, N. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0813210106 · Cited by 200
Hexosamines as mediators of nutrient sensing and regulation in diabetes
McClain, D. A. (2002) · Journal of Diabetes and its Complications · doi:10.1016/s1056-8727(01)00188-x · Cited by 196
Structure and mechanism of a bacterial β-glucosaminidase having O-GlcNAcase activity
Dennis, R. J., Taylor, E. J., Macauley, M. S., Stubbs, K. A., Turkenburg, J. P., Hart, S., Black, G. N., Vocadlo, D. J., & Davies, G. J. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1079 · Cited by 195
AlternativeO-Glycosylation/O-Phosphorylation of Serine-16 in Murine Estrogen Receptor β
Cheng, X., & Hart, G. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010411200 · Cited by 190
Self-citationPromoter Selectivity of Escherichia coli RNA Polymerase Eσ70 and Eσ38 Holoenzymes
Kusano, S., Ding, Q., Fujita, N., et al. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.4.1998 · Cited by 189
Regulation of the O-Linked β-N-Acetylglucosamine Transferase by Insulin Signaling
Whelan, S. A., Lane, M. D., & Hart, G. W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800677200 · Cited by 186
Self-citationThe Biosynthesis of Hyaluronic Acid by Group A Streptococcus
Markovitz, A., Cifonelli, J. A., & Dorfman, A. (1959) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69812-6 · Cited by 186
Slawson, C. M., Lakshmanan, T., Knapp, S., & Hart, G. W. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-11-1146 · Cited by 184
Self-citationO-GlcNAc and the control of gene expression
Comer, F. I., & Hart, G. W. (1999) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(99)00176-2 · Cited by 183
Self-citationGlucose and glucosamine regulate growth factor gene expression in vascular smooth muscle cells.
McClain, D. A., Paterson, A. J., Roos, M. D., Wei, X., & Kudlow, J. E. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.17.8150 · Cited by 182
Keratin modifications and solubility properties in epithelial cells and in vitro.
Omary, M. B., Ku, N., Liao, J. C., et al. (1998) · PubMed · Cited by 181
Slawson, C. M., Housley, M. P., & Hart, G. W. (2005) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20676 · Cited by 181
Self-citationComtesse, N., Maldener, E., & Meese, E. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4815 · Cited by 177
Hartweck, L. M., Scott, C. L., & Olszewski, N. E. (2002) · Genetics · doi:10.1093/genetics/161.3.1279 · Cited by 177
Jackson, S. P., & Tjian, R. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.6.1781 · Cited by 176
Alternative O-Glycosylation/O-Phosphorylation of the Murine Estrogen Receptor β
Cheng, X., Cole, R. N., Zaia, J., & Hart, G. W. (2000) · Biochemistry · doi:10.1021/bi000755i · Cited by 175
Self-citationGreis, K. D., Hayes, B. K., Comer, F. I., KIRK, M. C., Barnes, S., Lowary, T. L., & Hart, G. W. (1996) · Analytical Biochemistry · doi:10.1006/abio.1996.0047 · Cited by 175
Self-citationSite‐specific interplay between O‐GlcNAcylation and phosphorylation in cellular regulation
Hu, P., Shimoji, S., & Hart, G. W. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.04.044 · Cited by 170
Self-citationO-Linked N-Acetylglucosamine Is Present on the Extracellular Domain of Notch Receptors
Matsuura, A., Ito, M., Sakaidani, Y., Kondo, T., Murakami, K., Furukawa, K., Nadano, D., Matsuda, T., & Okajima, T. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806202200 · Cited by 168
Liu, J., Pang, Y., CHANG, T., Bounelis, P., Chatham, J. C., & Marchase, R. B. (2005) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2005.11.003 · Cited by 168
Fülöp, N., Marchase, R. B., & Chatham, J. C. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2006.07.018 · Cited by 168
Whitworth, G. E., Macauley, M. S., Stubbs, K. A., Dennis, R. J., Taylor, E. J., Davies, G. J., Greig, I. R., & Vocadlo, D. J. (2006) · Journal of the American Chemical Society · doi:10.1021/ja065697o · Cited by 166
Kelly, W. G., & Hart, G. W. (1989) · Cell · doi:10.1016/0092-8674(89)90962-8 · Cited by 166
Self-citationRegulation of Calcium/Calmodulin-dependent Kinase IV by O-GlcNAc Modification
Dias, W. B., Cheung, W. D., Wang, Z., & Hart, G. W. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.007310 · Cited by 165
Self-citationCytoplasmic O‐glycosylation prevents cell surface transport of E‐cadherin during apoptosis
Zhu, W., Leber, B. F., & Andrews, D. W. (2001) · The EMBO Journal · doi:10.1093/emboj/20.21.5999 · Cited by 165
Methods in Enzymology: O‐Glycosylation of Proteins
Peter‐Katalinić, J. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)05007-x · Cited by 164
Forsythe, M. E., Love, D. C., Lazarus, B. D., Kim, E. J., Prinz, W. A., Ashwell, G., Krause, M., & Hanover, J. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601931103 · Cited by 164
Iyer, S. P. N., Akimoto, Y., & Hart, G. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209384200 · Cited by 163
Self-citationErythrocytes contain cytoplasmic glycoproteins. O-linked GlcNAc on Band 4.1.
Holt, G. D., Haltiwanger, R. S., Torres, C., & Hart, G. W. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48100-8 · Cited by 162
Self-citationCheung, W. D., Sakabe, K., Housley, M. P., Dias, W. B., & Hart, G. W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806199200 · Cited by 162
Self-citationO-GlcNAc protein modification in plants: Evolution and function
Olszewski, N. E., West, C. M., Sassi, S. O., & Hartweck, L. M. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.11.016 · Cited by 160
O-GlcNAc Transferase Is in a Functional Complex with Protein Phosphatase 1 Catalytic Subunits
Wells, L., Kreppel, L. K., Comer, F. I., Wadzinski, B. E., & Hart, G. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406481200 · Cited by 158
Self-citationHigh glucose and insulin promote O- GlcNAc modification of proteins, including α-tubulin
Walgren, J., Vincent, T. S., Schey, K. L., & Buse, M. G. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00382.2002 · Cited by 158
Dorfmueller, H. C., Borodkin, V. S., Schimpl, M., Shepherd, S. M., Shpiro, N., & van Aalten, D. M. F. (2006) · Journal of the American Chemical Society · doi:10.1021/ja066743n · Cited by 157
β‐Amyloid precursor protein is modified with O‐linked N‐acetylglucosamine
Griffith, L. S., Mathes, M., & Schmitz, B. (1995) · Journal of Neuroscience Research · doi:10.1002/jnr.490410214 · Cited by 154
Aberrant O-GlcNAcylation characterizes chronic lymphocytic leukemia
Shi, Y., Tomic, J., Wen, F., Shaha, S., Bahlo, A., Harrison, R., Dennis, J. W., Williams, R., Gross, B. J., Walker, S., et al. (2010) · Leukemia · doi:10.1038/leu.2010.152 · Cited by 146
Self-citationLoops Govern SH2 Domain Specificity by Controlling Access to Binding Pockets
Kaneko, T., Huang, H., Zhao, B., Li, L., Liu, H., Voss, C. K., Wu, C., Schiller, M. R., & Li, S. S.-C. (2010) · Science Signaling · doi:10.1126/scisignal.2000796 · Cited by 146
Ramirez-Correa, G. A., Jin, W., Wang, Z., Zhong, X., Gao, W. D., Dias, W. B., Vecoli, C., Hart, G. W., & Murphy, A. M. (2008) · Circulation Research · doi:10.1161/circresaha.108.184978 · Cited by 145
Self-citationHart, G. W., Kreppel, L. K., Comer, F. I., Arnold, C. S., Snow, D. M., Ye, Z., Cheng, X., Manna, D. L. D., Caine, D. S., Earles, B. J., et al. (1996) · Glycobiology · doi:10.1093/glycob/6.7.711 · Cited by 140
Self-citationGibberellin signal transduction presents …the SPY who O-GlcNAc'd me
Thornton, T. (1999) · Trends in Plant Science · doi:10.1016/s1360-1385(99)01485-5 · Cited by 140
Novel immunogenic antigen homologous to hyaluronidase in meningioma
Heckel, D., Comtesse, N., Brass, N., Blin, N., Zang, K. D., & Meese, E. (1998) · Human Molecular Genetics · doi:10.1093/hmg/7.12.1859 · Cited by 140
Wrabl, J. O., & Grishin, N. V. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5151 · Cited by 139
[26] Detection of O-Linked N-acetylglucosamine (O-GlcNAc) on cytoplasmic and nuclear proteins
Roquemore, E. P., Chou, T., & Hart, G. W. (1994) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(94)30028-3 · Cited by 136
Self-citationO-GlcNAc Transferase Regulates Mitotic Chromatin Dynamics
Sakabe, K., & Hart, G. W. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.158170 · Cited by 136
Self-citationSolomon, S. S., Majumdar, G., Martinez-Hernandez, A., & Raghow, R. (2008) · Life Sciences · doi:10.1016/j.lfs.2008.06.024 · Cited by 132
Localization of O-GlcNAc modification on the serum response transcription factor.
Reason, A. J., Morris, H. R., Panico, M., Marais, R., Treisman, R., Haltiwanger, R. S., Hart, G. W., Kelly, W. G., & Dell, A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41871-6 · Cited by 131
Self-citationIncreasing O-GlcNAc levels: An overview of small-molecule inhibitors of O-GlcNAcase
Macauley, M. S., & Vocadlo, D. J. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.07.028 · Cited by 131
Structural insights into mechanism and specificity of O‐GlcNAc transferase
Clarke, A., Hurtado‐Guerrero, R., Pathak, S., Schüttelkopf, A. W., Borodkin, V. S., Shepherd, S. M., Ibrahim, A. F. M., & van Aalten, D. M. F. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.186 · Cited by 130
Fülöp, N., Mason, M. M., Dutta, K., Wang, P., Davidoff, A. J., Marchase, R. B., & Chatham, J. C. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00422.2006 · Cited by 130
Poised Polymerases: On Your Mark…Get Set…Go!
Price, D. H. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.001 · Cited by 128
Tallent, M. K., Varghis, N., Skorobogatko, Y. V., Hernandez‐Cuebas, L., Whelan, K. A., Vocadlo, D. J., & Vosseller, K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807431200 · Cited by 128
Macauley, M. S., Bubb, A. K., Martinez-Fleites, C., Davies, G. J., & Vocadlo, D. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804525200 · Cited by 127
Characterization of β-N-Acetylglucosaminidase Cleavage by Caspase-3 during Apoptosis
Butkinaree, C., Cheung, W. D., Park, S. J., Park, K., Barber, M., & Hart, G. W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804116200 · Cited by 126
Self-citationZeidan, Q., Wang, Z., Maio, A. D., & Hart, G. W. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-11-0941 · Cited by 126
Self-citationWhelan, S. A., & Hart, G. W. (2003) · Circulation Research · doi:10.1161/01.res.0000103190.20260.37 · Cited by 126
Self-citationKamemura, K., & Hart, G. W. (2003) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(03)01004-3 · Cited by 125
Self-citationNgoh, G. A., Watson, L. J., Facundo, H. T., DILLMANN, W. H., & Jones, S. P. (2008) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2008.04.009 · Cited by 122
Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation
Martinez-Fleites, C., Macauley, M. S., He, Y., Shen, D. L., Vocadlo, D. J., & Davies, G. J. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1443 · Cited by 122
Flagellin fromListeria monocytogenesIs Glycosylated with β-O-LinkedN-Acetylglucosamine
Schirm, M., Kalmokoff, M. L., Aubry, A. J., Thibault, P., Sandoz, M., & Logan, S. M. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.20.6721-6727.2004 · Cited by 121
A bifunctional O-GlcNAc transferase governs flagellar motility through anti-repressionPreprint
Shen, A., Kamp, H. D., Gründling, A., et al. (2006) · Genes & Development · doi:10.1101/gad.1492606 · Cited by 120
Lefebvre, T., Dehennaut, V., Guinez, C., Stichelen, S. O.-V., Drougat, L., Mir, A., Mortuaire, M., Vercoutter‐Edouart, A., & Michalski, J. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.08.008 · Cited by 119
O-GlcNAc modulation at Akt1 Ser473 correlates with apoptosis of murine pancreatic β cells
Kang, E., Han, D., Park, J., Kwak, T., Oh, M.-A., Lee, S.-A., Choi, S., Park, Z., Kim, Y., & Lee, S. E. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.04.014 · Cited by 118
O-GlcNAc cycling: Emerging roles in development and epigenetics
Love, D. C., Krause, M., & Hanover, J. A. (2010) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2010.05.001 · Cited by 113
O-GlcNAc modifications regulate cell survival and epiboly during zebrafish development
Webster, D. M., Teo, C. F., Sun, Y., Włoga, D., Gay, S., Klonowski, K. D., Wells, L., & Dougan, S. T. (2009) · BMC Developmental Biology · doi:10.1186/1471-213x-9-28 · Cited by 112
Luo, B., Soesanto, Y., & McClain, D. A. (2008) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.107.159533 · Cited by 112
Fülöp, N., Zhang, Z., Marchase, R. B., et al. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01091.2006 · Cited by 112
Dong, D. L.-Y., Xu, Z.-S., Hart, G. W., & Cleveland, D. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.34.20845 · Cited by 112
Self-citationCooksey, R. C., Hebert, L. F., Zhu, J.-H., Wofford, P., Garvey, W. T., & McClain, D. A. (1999) · Endocrinology · doi:10.1210/endo.140.3.6563 · Cited by 111
The THAP-Zinc Finger Protein THAP1 Associates with Coactivator HCF-1 and O-GlcNAc Transferase
Mazars, R., de Peredo, A. G., Cayrol, C., Lavigne, A.-C., Vogel, J. L., Ortéga, N., Lacroix, C., Gautier, V., Huet, G., Ray, A. A., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.072579 · Cited by 107
Cieniewski‐Bernard, C., Bastide, B., Lefebvre, T., Lemoine, J., Mounier, Y., & Michalski, J. (2004) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400024-mcp200 · Cited by 106
Xing, D., Feng, W., Nöt, L. G., et al. (2008) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01259.2007 · Cited by 104
Glycosylation Sites Flank Phosphorylation Sites on Synapsin I
Cole, R. N., & Hart, G. W. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0730418.x · Cited by 103
Self-citationRotavirus NS26 is modified by addition of single O-linked residues of N-acetylglucosamine
González, S. A., & Burrone, Ó. R. (1991) · Virology · doi:10.1016/0042-6822(91)90642-o · Cited by 102
Ball, L. E., Berkaw, M. N., & Buse, M. G. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m500314-mcp200 · Cited by 101
Goldberg, H. J., Scholey, J. W., & Fantus, I. G. (2000) · Diabetes · doi:10.2337/diabetes.49.5.863 · Cited by 101
Detection and Analysis of Proteins Modified by O‐Linked N‐Acetylglucosamine
Zachara, N. E., Vosseller, K., & Hart, G. W. (2011) · Current Protocols in Protein Science · doi:10.1002/0471140864.ps1208s66 · Cited by 100
Self-citationThe hybridoma revolution: an offshoot of basic research
Milstein, C. (1999) · BioEssays · doi:10.1002/(sici)1521-1878(199911)21:11 · Cited by 97
Ray, M. K., Datta, B., Chakraborty, A., Chattopadhyay, A., Meza-Keuthen, S., & Gupta, N. K. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.2.539 · Cited by 94
O-GlcNAc-glycosylation of β-catenin regulates its nuclear localization and transcriptional activity
Sayat, R., Leber, B. F., Grubac, V., Wiltshire, L., & Persad, S. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.05.017 · Cited by 94
Lüdemann, N., Clement, A. M., Hans, V., Leschik, J., Behl, C., & Brandt, R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504395200 · Cited by 92
Du, X. L., Edelstein, D., Dimmeler, S., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci200111235 · Cited by 91
26S proteasome subunits are O-linked N-acetylglucosamine-modified in Drosophila melanogaster
Sümegi, M., Hunyadi‐Gulyás, É., Medzihradszky, K. F., & Udvardy, A. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.11.074 · Cited by 89
Whitford, M. F., & Faulkner, P. (1992) · Journal of Virology · doi:10.1128/jvi.66.6.3324-3329.1992 · Cited by 88
Starr, C. M., & Hanover, J. A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39229-4 · Cited by 87
Chen, Y., Du, J., Zhou, L., Liu, X.-H., Zhao, Y., Nakanishi, H., & Li, Y. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2006.06.017 · Cited by 86
Klein, A., Berkaw, M. N., Buse, M. G., & Ball, L. E. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900207-mcp200 · Cited by 86
Reduction of O-LinkedN-Acetylglucosamine-Modified Assembly Protein-3 in Alzheimer’s Disease
Yao, P. J., & Coleman, P. D. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-07-02399.1998 · Cited by 85
Gandy, J. C., Rountree, A. E., & Bijur, G. N. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.04.051 · Cited by 85
GLUCOSAMINE ADMINISTRATION DURING RESUSCITATION IMPROVES ORGAN FUNCTION AFTER TRAUMA HEMORRHAGE
Yang, S., Zou, L., Bounelis, P., et al. (2006) · Shock · doi:10.1097/01.shk.0000209563.07693.db · Cited by 84
A Subpopulation of Estrogen Receptors Are Modified by O-Linked N-Acetylglucosamine
Jiang, M.-S., & Hart, G. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.4.2421 · Cited by 83
Self-citationBudnar, S., Vaidya, M. M., & Kalraiya, R. D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.098996 · Cited by 83
Daniels, M. C., Ciaraldi, T. P., Nikoulina, S. E., Henry, R. R., & McClain, D. A. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118538 · Cited by 81
Characterisation of human N‐acetyl‐β‐hexosaminadase C
Braidman, I. P., Carroll, M., Dance, N., & Robinson, D. (1974) · FEBS Letters · doi:10.1016/0014-5793(74)81206-8 · Cited by 80
Hexosamines and insulin resistance
McClain, D. A., & Crook, E. D. (1996) · Diabetes · doi:10.2337/diabetes.45.8.1003 · Cited by 79
Greis, K. D., Gibson, W., & Hart, G. W. (1994) · Journal of Virology · doi:10.1128/jvi.68.12.8339-8349.1994 · Cited by 78
Self-citationSong, M., Kim, H.-S., Park, J.-M., Kim, S.-H., Kim, I.-H., Ryu, S. H., & Suh, P. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.09.002 · Cited by 78
Medina, L., Grove, K., & Haltiwanger, R. S. (1998) · Glycobiology · doi:10.1093/glycob/8.4.383 · Cited by 71
Schroeder, M. J., Webb, D. J., Shabanowitz, J., Horwitz, A. F., & Hunt, D. F. (2005) · Journal of Proteome Research · doi:10.1021/pr0502020 · Cited by 69
The role of protein O-linked β-N-acetylglucosamine in mediating cardiac stress responses
Chatham, J. C., & Marchase, R. B. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.07.004 · Cited by 69
Hédou, J., Cieniewski‐Bernard, C., Leroy, Y., Michalski, J., Mounier, Y., & Bastide, B. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m606787200 · Cited by 67
Virion basic phosphoprotein from human cytomegalovirus contains O-linked N-acetylglucosamine.
Benko, D. M., Haltiwanger, R. S., Hart, G. W., & Gibson, W. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.8.2573 · Cited by 66
Self-citationSterne‐Marr, R., Blevitt, J. M., & Gerace, L. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.116.2.271 · Cited by 65
High Molecular Weight Microtubule-associated Proteins Contain O-Linked N-Acetylglucosamine
Ding, M., & Vandré, D. D. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.21.12555 · Cited by 64
Alzheimer's disease could be “type 3 diabetes”
Pilcher, H. R. (2006) · The Lancet Neurology · doi:10.1016/s1474-4422(06)70434-3 · Cited by 63
Zhang, X., & Bennett, V. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.49.31391 · Cited by 63
Mullis, K. G., Haltiwanger, R. S., Hart, G. W., et al. (1990) · Journal of Virology · doi:10.1128/jvi.64.11.5317-5323.1990 · Cited by 62
Self-citationSugar-Dependent Nuclear Import of Glycoconjugates from the Cytosol
Duverger, E., Carpentier, V., Roche, A., & Monsigny, M. L. P. (1993) · Experimental Cell Research · doi:10.1006/excr.1993.1181 · Cited by 62
Research works printed but not linked: 12
- 10.1074/mcp.M400024-MCP200 · DOI
- 10.1074/jbc.M806199200 · DOI
- 10.1074/jbc.M808890200 · DOI
- Zachara NE, 2004, Methods Mol. Biol., 284, 175
- Greis KD, 1998, Methods Mol. Biol., 76, 19
- 10.1126/scisignal.2000526 · DOI
- Omary MB, 1998, Subcell. Biochem., 31, 105
- 10.1074/jbc.M406481200 · DOI
- 10.1161/CIRCRESAHA.108.184978 · DOI · Paper page
- 10.1210/en.140.3.1151 · DOI
- Kroner Z., 2009, Altern. Med. Rev., 14, 373
- 10.1074/jbc.271.46.28741 · DOI · Paper page
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Metadata
- Authors
- Hart, G. W., Slawson, C., Ramirez-Correa, G., & Lagerlof, O.
- Affiliations
- Johns Hopkins University (US)
- Departments of Biological Chemistry, Johns Hopkins University, School of Medicine, Baltimore, Maryland 21205;, cslawso1@jhmi.edu, gramire2@jhmi.edu, olof.lagerlof@gmail.com
- Departments of Biological Chemistry and Pediatrics, Johns Hopkins University, School of Medicine, Baltimore, Maryland 21205;
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2011-07-07
- Volume
- 80
- Issue
- 1
- Pages
- 825-858
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- PMC
- PMC3294376
- OpenAlex
- W2140409722
- Cited by
- 1,317
- References
- 235
- Citations by year
- 2026: 65 · 2025: 75 · 2024: 88 · 2023: 73 · 2022: 92 · 2021: 121 · 2020: 83 · 2019: 78 · 2018: 90 · 2017: 87 · 2016: 88 · 2015: 91 · 2014: 122 · 2013: 95 · 2012: 53
- FWCI
- 8.27
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Annual Review of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- ScholarWorks @ UTRGV (The University of Texas Rio Grande Valley) (submittedVersion)
- Funders
- National Institutes of Health (4r33dk071280-03)
- National Cancer Institute (R01CA42486, R01CA042486)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK061671, R33-DK-071280, R24DK084949, P30DK079637, R33 DK071280-04, R01-DK61671)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (R37HD013563)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- O-GlcNAcylation, protein phosphorylation, post-translational modification, O-GlcNAc transferase, O-GlcNAcase, protein glycosylation, nutrient sensing, stress sensing, signal transduction, transcriptional regulation, cytoskeleton, mitochondria, insulin resistance, glucotoxicity, diabetes mellitus, neurodegenerative diseases, oncoprotein, tumor suppressor proteins, chronic disease
- MeSH terms
- Acetylglucosamine, Animals, Chronic Disease, Diabetes Mellitus, Glycosylation, Humans, Models, Molecular, Neoplasms, Phosphorylation, Protein Conformation, Transcription, Genetic, Molecular Structure, Signal Transduction, N-Acetylglucosaminyltransferases, Neurodegenerative Diseases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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