O-GlcNAc signaling: a metabolic link between diabetes and cancer?

Slawson, C.; Copeland, R.J.; Hart, G.W.

doi:10.1016/j.tibs.2010.04.005

Cited by 346Glycosylation and Glycoproteins ResearchCarbohydrate Chemistry and SynthesisMetabolism, Diabetes, and Cancer

O-GlcNAc signaling: a metabolic link between diabetes and cancer?

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Slawson, C., Copeland, R.J., Hart, G.W.·2010·Trends in Biochemical Sciences

DOI 10.1016/j.tibs.2010.04.005PMC PMC2949529

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Abstract

O-linked β-N-acetylglucosamine (O-GlcNAc) is a sugar attachment to serine or threonine hydroxyl moieties on nuclear and cytoplasmic proteins. In many ways, O-GlcNAcylation is similar to phosphorylation because both post-translational modifications cycle rapidly in response to internal or environmental cues. O-GlcNAcylated proteins are involved in transcription, translation, cytoskeletal assembly, signal transduction, and many other cellular functions. O-GlcNAc signaling is intertwined with cellular metabolism; indeed, the donor sugar for O-GlcNAcylation (UDP-GlcNAc) is synthesized from glucose, glutamine, and UTP via the hexosamine biosynthetic pathway. Emerging research indicates that O-GlcNAc signaling and its crosstalk with phosphorylation are altered in metabolic diseases, such as diabetes and cancer.

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KRAS promotes the hexosamine biosynthesis pathway, which supplies precursors for lipid and protein glycosylation.
“KRAS also promotes the hexosamine biosynthesis pathway (HBP), which provides precursors for lipid and protein glycosylation34, and the non-oxidative arm of the pentose phosphate pathway (PPP)28, which supplies ribose, the backbone for nucleic acid production35 (Fig 2).”
From The metabolic landscape of RAS-driven cancers from biology to therapy (2021) · cites this paper as [34]

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Antisense glutaminase inhibition modifies the O‐GlcNAc pattern and flux through the hexosamine pathway in breast cancer cells
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Identification of GFAT1-L, a novel splice variant of human glutamine: fructose-6-phosphate amidotransferase (GFAT1) that is expressed abundantly in skeletal muscle
Niimi, M., Ogawara, T., Yamashita, T., Yamamoto, Y., Ueyama, A., Kambe, T., Okamoto, T., Ban, T., Tamanoi, H., Ozaki, K., et al. (2001) · Journal of Human Genetics · doi:10.1007/s100380170022 · Cited by 40 · see citing works
Hyperglycemia and glucosamine-induced mesangial cell cycle arrest and hypertrophy: Common or independent mechanisms?
Masson, E., Lagarde, M., Wiernsperger, N. F., & Bawab, S. E. (2006) · IUBMB Life · doi:10.1080/15216540600755980 · Cited by 37 · see citing works
Hyperammonemia in Multiple Myeloma
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Glucosamine-induced increase in Akt phosphorylation corresponds to increased endoplasmic reticulum stress in astroglial cells
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Increased glutamine:fructose-6-phosphate amidotransferase activity in skeletal muscle of patients with NIDDM
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Understanding the role of aneuploidy in tumorigenesis
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Functional domains and interdomain communication in Candida albicans glucosamine-6-phosphate synthase
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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, R. R., Pouwels, M.-J. J., Span, P. N., Olthaar, A. J., Tack, C. J., Hermus, A. R., & Sweep, F. C. G. J. (2004) · Endocrine · doi:10.1385/endo:23:1:17 · Cited by 17 · see citing works

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Glycosylation in cancer: mechanisms and clinical implications
Pinho, S. S., & Reis, C. A. (2015) · Nature reviews. Cancer · doi:10.1038/nrc3982 · Cited by 3,096 · see citing works
Cross Talk Between O-GlcNAcylation and Phosphorylation: Roles in Signaling, Transcription, and Chronic Disease
Hart, G. W., Slawson, C., Ramirez-Correa, G., & Lagerlof, O. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060608-102511 · Cited by 1,317 · see citing works
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KRAS Mutation: From Undruggable to Druggable in Cancer
Huang, L., Guo, Z., Wang, F., & Fu, L. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00780-4 · Cited by 1,127 · see citing works
Endothelial Cell Metabolism in Normal and Diseased Vasculature
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Endothelial Cell Metabolism
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Diabetic cardiomyopathy: Mechanisms and new treatment strategies targeting antioxidant signaling pathways
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A two-way street: reciprocal regulation of metabolism and signalling
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Cellular Metabolic Stress: Considering How Cells Respond to Nutrient Excess
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Signalling by insulin and IGF receptors: supporting acts and new players
Siddle, K. (2011) · Journal of Molecular Endocrinology · doi:10.1530/jme-11-0022 · Cited by 456 · see citing works
O-GlcNAc signalling: implications for cancer cell biology
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Energy Metabolism of the Osteoblast: Implications for Osteoporosis
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N-Acetylglucosamine Functions in Cell Signaling
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Strengthened glycolysis under hypoxia supports tumor symbiosis and hexosamine biosynthesis in pancreatic adenocarcinoma
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Autophagosome maturation: An epic journey from the ER to lysosomes
Zhao, Y. G., & Zhang, H. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201810099 · Cited by 362 · see citing works
Implications of Underlying Mechanisms for the Recognition and Management of Diabetic Cardiomyopathy
Marwick, T. H., Ritchie, R., Shaw, J. E., & Kaye, D. (2018) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2017.11.019 · Cited by 365 · see citing works
Role of O -linked N -acetylglucosamine protein modification in cellular (patho)physiology
Chatham, J. C., Zhang, J., & Wende, A. R. (2020) · Physiological Reviews · doi:10.1152/physrev.00043.2019 · Cited by 359 · see citing works
The Link Between Angiogenesis and Endothelial Metabolism
Potente, M., & Carmeliet, P. (2016) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021115-105134 · Cited by 353 · see citing works
O-GlcNAcylation of PGK1 coordinates glycolysis and TCA cycle to promote tumor growth
Nie, H., Ju, H., Fan, J., Shi, X., Cheng, Y., Cang, X., Zheng, Z., Duan, X., & Yi, W. (2020) · Nature Communications · doi:10.1038/s41467-019-13601-8 · Cited by 349 · see citing works
Endothelial Cell Metabolism in Health and Disease
Rohlenová, K., Veys, K., Santos, I. M., Bock, K. D., & Carmeliet, P. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.10.010 · Cited by 336 · see citing works
Targeting Metabolic Plasticity and Flexibility Dynamics for Cancer Therapy
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The metabolic landscape of RAS-driven cancers from biology to therapy
Mukhopadhyay, S., Vander Heiden, M. G., & McCormick, F. (2021) · Nature Cancer · doi:10.1038/s43018-021-00184-x · Cited by 315 · see citing works
O-GlcNAc-modification of SNAP-29 regulates autophagosome maturation
Guo, B., Liang, Q., Li, L., Hu, Z., Wu, F., Zhang, P., Ma, Y., Zhao, B., Kovács, A. L., Zhang, Z., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb3066 · Cited by 295 · see citing works
O-GlcNAc Transferase/Host Cell Factor C1 Complex Regulates Gluconeogenesis by Modulating PGC-1α Stability
Ruan, H.-B., Han, X., Li, M.-D., Singh, J. P., Qian, K., Azarhoush, S., Zhao, L., Bennett, A. M., Samuel, V. T., Wu, J., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.07.006 · Cited by 296 · see citing works
Critical Role of O-Linked β-N-Acetylglucosamine Transferase in Prostate Cancer Invasion, Angiogenesis, and Metastasis
Lynch, T. P., Ferrer, C. M., Jackson, S. R., Shahriari, K. S., Vosseller, K., & Reginato, M. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.302547 · Cited by 286 · see citing works
Regulation of the Hippo-YAP Pathway by Glucose Sensor O-GlcNAcylation
Peng, C., Zhu, Y., Zhang, W., Liao, Q., Chen, Y., Zhao, X., Guo, Q., Shen, P., Zhen, B., Qian, X., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.10.010 · Cited by 279 · see citing works
Endothelial cell metabolism in health and disease: impact of hypoxia
Wong, B. W., Marsch, E., Treps, L., Baes, M. I., & Carmeliet, P. (2017) · The EMBO Journal · doi:10.15252/embj.201696150 · Cited by 277 · see citing works
O-GlcNAcylation: A New Cancer Hallmark?
Fardini, Y., Dehennaut, V., Lefebvre, T., & Issad, T. (2013) · Frontiers in Endocrinology · doi:10.3389/fendo.2013.00099 · Cited by 265 · see citing works
O-GlcNAcylation is a novel regulator of lung and colon cancer malignancy
Mi, W., Gu, Y., Han, C., Liu, H., Fan, Q., Zhang, X., Cong, Q., & Yu, W. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.01.009 · Cited by 259 · see citing works
Protein O -GlcNAcylation in diabetes and diabetic complications
Ma, J., & Hart, G. W. (2013) · Expert Review of Proteomics · doi:10.1586/14789450.2013.820536 · Cited by 251 · see citing works
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The myosin phosphatase targeting protein (MYPT) family: A regulated mechanism for achieving substrate specificity of the catalytic subunit of protein phosphatase type 1δ
Grassie, M. E., Moffat, L. D., Walsh, M. P., & MacDonald, J. A. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.01.018 · Cited by 229 · see citing works
The essential role of YAP O-GlcNAcylation in high-glucose-stimulated liver tumorigenesis
Zhang, X., Qiao, Y., Wu, Q., Chen, Y., Zou, S., Liu, X., Zhu, G., Zhao, Y., Chen, Y., Yu, Y., et al. (2017) · Nature Communications · doi:10.1038/ncomms15280 · Cited by 234 · see citing works
Glycotherapy: New Advances Inspire a Reemergence of Glycans in Medicine
Hudak, J. E., & Bertozzi, C. R. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.09.010 · Cited by 228 · see citing works
Cracking the O-GlcNAc code in metabolism
Ruan, H., Singh, J. P., Li, M., Wu, J., & Yang, X. (2013) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2013.02.002 · Cited by 224 · see citing works
Integration of Metabolomics and Transcriptomics Reveals Major Metabolic Pathways and Potential Biomarker Involved in Prostate Cancer
Ren, S., Shao, Y., Zhao, X., Hong, C. S., Wang, F., Lu, X., Li, J., Ye, G., Yan, M., Zhuang, Z., et al. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.052381 · Cited by 212 · see citing works
A Comprehensive View of the Epigenetic Landscape. Part II: Histone Post-translational Modification, Nucleosome Level, and Chromatin Regulation by ncRNAs
Sadakierska−Chudy, A., & Filip, M. (2014) · Neurotoxicity Research · doi:10.1007/s12640-014-9508-6 · Cited by 202 · see citing works
Macropinocytosis confers resistance to therapies targeting cancer anabolism
Jayashankar, V., & Edinger, A. L. (2020) · Nature Communications · doi:10.1038/s41467-020-14928-3 · Cited by 200 · see citing works
Cell signaling, post-translational protein modifications and NMR spectroscopy
Theillet, F., Smet‐Nocca, C., Liokatis, S., Thongwichian, R., Kosten, J., Yoon, M., Kriwacki, R. W., Landrieu, I., Lippens, G. M., & Selenko, P. (2012) · Journal of Biomolecular NMR · doi:10.1007/s10858-012-9674-x · Cited by 188 · see citing works
Linking macrophage metabolism to function in the tumor microenvironment
Jin, R., Neufeld, L. A., & McGaha, T. L. (2025) · Nature Cancer · doi:10.1038/s43018-025-00909-2 · Cited by 173 · see citing works
Analytical and Biochemical Perspectives of Protein O-GlcNAcylation
Ma, J., Wu, C., & Hart, G. W. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00884 · Cited by 171 · see citing works
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Hyperglycemia-associated alterations in cellular signaling and dysregulated mitochondrial bioenergetics in human metabolic disorders
Stefano, G. B., Challenger, S., & Kream, R. M. (2016) · Zeitschrift für Ernährungswissenschaft · doi:10.1007/s00394-016-1212-2 · Cited by 164 · see citing works
FXR in liver physiology: Multiple faces to regulate liver metabolism
Panzitt, K., & Wagner, M. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2021.166133 · Cited by 160 · see citing works
Roles of O-GlcNAc in chronic diseases of aging
Banerjee, P. S., Lagerlöf, O., & Hart, G. W. (2016) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2016.05.005 · Cited by 157 · see citing works
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Role of UDP-N-Acetylglucosamine (GlcNAc) and O-GlcNAcylation of Hyaluronan Synthase 2 in the Control of Chondroitin Sulfate and Hyaluronan Synthesis
Vigetti, D., Deleonibus, S., Moretto, P., Karousou, E., Viola, M., Bartolini, B., Hascall, V., Tammi, M., Luca, G. D., & Passi, A. G. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.402347 · Cited by 154 · see citing works
Molecular Basis of Signaling Specificity of Insulin and IGF Receptors: Neglected Corners and Recent Advances
Siddle, K. (2012) · Frontiers in Endocrinology · doi:10.3389/fendo.2012.00034 · Cited by 154 · see citing works
Biosynthetic Machinery Involved in Aberrant Glycosylation: Promising Targets for Developing of Drugs Against Cancer
Vasconcelos-dos-Santos, A., Oliveira, I. D. A., Lucena, M. C., Mantuano, N. R., Whelan, S. A., Dias, W. B., & Todeschini, A. R. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2015.00138 · Cited by 149 · see citing works
Down-regulation of OGT promotes cisplatin resistance by inducing autophagy in ovarian cancer
Zhou, F., Yang, X., Zhao, H., Liu, Y., Yang, F., An, R. F., Lv, X., Li, J., & Chen, B. (2018) · Theranostics · doi:10.7150/thno.27806 · Cited by 148 · see citing works
Conditional Knock-out Reveals a Requirement for O-Linked N-Acetylglucosaminase (O-GlcNAcase) in Metabolic Homeostasis
Keembiyehetty, C. N., Love, D. C., Harwood, K. R., Gavrilova, O., Comly, M. E., & Hanover, J. A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.617779 · Cited by 145 · see citing works
Common errors in mass spectrometry‐based analysis of post‐translational modifications
Kim, M., Zhong, J., & Pandey, A. (2015) · PROTEOMICS · doi:10.1002/pmic.201500355 · Cited by 146 · see citing works
O-GlcNAc in cancer: An Oncometabolism-fueled vicious cycle
Hanover, J. A., Chen, W., & Bond, M. R. (2018) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-018-9751-2 · Cited by 144 · see citing works
Dynamic O-GlcNAcylation and its roles in the cellular stress response and homeostasis
Groves, J. A., Lee, A., Yildirir, G., & Zachara, N. E. (2013) · Cell Stress and Chaperones · doi:10.1007/s12192-013-0426-y · Cited by 143 · see citing works
The hexosamine biosynthesis pathway is a targetable liability in KRAS/LKB1 mutant lung cancer
Kim, J., Lee, H. M., Cai, F., Ko, B., Yang, C., Lieu, E. L., Muhammad, N., Rhyne, S., Li, K., Haloul, M., et al. (2020) · Nature Metabolism · doi:10.1038/s42255-020-00316-0 · Cited by 143 · see citing works
O-GlcNAcylation in health and neurodegenerative diseases
Lee, B. E., Suh, P., & Kim, J. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00709-5 · Cited by 143 · see citing works
Glycosylation Changes in Brain Cancer
Veillon, L. J., Fakih, C., Abou‐El‐Hassan, H., Kobeissy, F. H., & Mechref, Y. S. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00271 · Cited by 141 · see citing works
O-GlcNAc signaling in cancer metabolism and epigenetics
Singh, J. P., Zhang, K., Wu, J., & Yang, X. (2014) · Cancer Letters · doi:10.1016/j.canlet.2014.04.014 · Cited by 133 · see citing works
Natural Antisense Transcript for Hyaluronan Synthase 2 (HAS2-AS1) Induces Transcription of HAS2 via Protein O-GlcNAcylation
Vigetti, D., Deleonibus, S., Moretto, P., Bowen, T., Fischer, J. W., Grandoch, M., Oberhuber, A., Love, D. C., Hanover, J. A., Cinquetti, R., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.597401 · Cited by 131 · see citing works
Cytoskeletal keratin glycosylation protects epithelial tissue from injury
Ku, N., Toivola, D. M., Strnad, P., & Omary, M. B. (2010) · Nature Cell Biology · doi:10.1038/ncb2091 · Cited by 121 · see citing works
Shear Stress Regulation of Endothelial Glycocalyx Structure Is Determined by Glucobiosynthesis
Wang, G., Kostidis, S., Tiemeier, G. L., Sol, W. M. P. J., de Vries, M. R., Giera, M. A., Carmeliet, P., van den Berg, B. M., & Rabelink, T. J. (2019) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.119.313399 · Cited by 122 · see citing works
Targeting cancer cell metabolism in pancreatic adenocarcinoma
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β-N-Acetylglucosamine (O-GlcNAc) Is a Novel Regulator of Mitosis-specific Phosphorylations on Histone H3
Fong, J. J., Nguyen, B. L., Bridger, R., Medrano, E. E., Wells, L., Pan, S., & Sifers, R. N. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.315804 · Cited by 119 · see citing works
The complex landscape of pancreatic cancer metabolism
Sousa, C. M., & Kimmelman, A. C. (2014) · Carcinogenesis · doi:10.1093/carcin/bgu097 · Cited by 123 · see citing works
Regulation of hyaluronan biosynthesis and clinical impact of excessive hyaluronan production
Heldin, P., Lin, C., Kolliopoulos, C., Chen, Y., & Skandalis, S. S. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.01.017 · Cited by 120 · see citing works
Three Decades of Research on O-GlcNAcylation – A Major Nutrient Sensor That Regulates Signaling, Transcription and Cellular Metabolism
Hart, G. W. (2014) · Frontiers in Endocrinology · doi:10.3389/fendo.2014.00183 · Cited by 119 · see citing works
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Snapin Mediates Incretin Action and Augments Glucose-Dependent Insulin Secretion
Song, W., Seshadri, M. R., Ashraf, U., Mdluli, T., Mondal, P., Keil, M. F., Azevedo, M. F., Kirschner, L. S., Stratakis, C. A., & Hussain, M. A. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.02.002 · Cited by 113 · see citing works
Impact of SGLT2 Inhibitors on Heart Failure: From Pathophysiology to Clinical Effects
Palmiero, G., Cesaro, A., Vetrano, E., Pafundi, P. C., Galiero, R., Caturano, A., Moscarella, E., Gragnano, F., Salvatore, T., Rinaldi, L., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115863 · Cited by 120 · see citing works
Gene expression of O-GlcNAc cycling enzymes in human breast cancers
Krześlak, A., Forma, E., Bernaciak, M., Romanowicz, H., & Bryś, M. (2011) · Clinical and Experimental Medicine · doi:10.1007/s10238-011-0138-5 · Cited by 109 · see citing works
dbOGAP - An Integrated Bioinformatics Resource for Protein O-GlcNAcylation
Wang, J., Torii, M., Liu, H., Hart, G. W., & Hu, Z. (2011) · BMC Bioinformatics · doi:10.1186/1471-2105-12-91 · Cited by 107 · see citing works
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O-GlcNAcylation and O-GlcNAc Cycling Regulate Gene Transcription: Emerging Roles in Cancer
Parker, M. P., Peterson, K. R., & Slawson, C. M. (2021) · Cancers · doi:10.3390/cancers13071666 · Cited by 104 · see citing works
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A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase
Jiang, J., Lazarus, M. B., Pasquina, L. W., Piotr Sliz, A., & Walker, S. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.711 · Cited by 104 · see citing works
Eaten alive: novel insights into autophagy from multicellular model systems
Zhang, H., & Baehrecke, E. H. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.03.001 · Cited by 102 · see citing works
Regulation of OGT by URI in Response to Glucose Confers c-MYC-Dependent Survival Mechanisms
Burén, S., Gomes, A. L., Teijeiro, A., Fawal, M.-A., Yilmaz, M., Tummala, K. S., Pérez‐Martínez, M., Rodriguez‐Justo, M., Campos‐Olivas, R., Megı́as, D., et al. (2016) · Cancer Cell · doi:10.1016/j.ccell.2016.06.023 · Cited by 101 · see citing works
Curcumin Ameliorates Nonalcoholic Fatty Liver Disease through Inhibition of O-GlcNAcylation
Lee, D. E., Lee, S. J., Kim, S. J., Lee, H., & Kwon, O. (2019) · Nutrients · doi:10.3390/nu11112702 · Cited by 101 · see citing works
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., Sui, G., Vogel, J. L., Kristie, T. M., & Affar, E. B. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1013822108 · Cited by 98 · see citing works
UAP1 is overexpressed in prostate cancer and is protective against inhibitors of N-linked glycosylation
Itkonen, H. M., Engedal, N., Babaie, E., Luhr, M., Guldvik, I. J., Minner, S. J. P., Hohloch, J., Tsourlakis, M., Schlomm, T., & Mills, I. G. (2014) · Oncogene · doi:10.1038/onc.2014.307 · Cited by 97 · see citing works
The Increase in O-Linked N-Acetylglucosamine Protein Modification Stimulates Chondrogenic Differentiation Both in Vitro and in Vivo
Andrés-Bergós, J., Tardio, L., Larranaga‐Vera, A., Gómez, R., Herrero‐Beaumont, G., & Largo, R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.354241 · Cited by 97 · see citing works
O-GlcNAc elevation through activation of the hexosamine biosynthetic pathway enhances cancer cell chemoresistance
Liu, Y., Cao, Y., Pan, X., Shi, M., Wu, Q., Huang, T., Jiang, H., Li, W., & Zhang, J. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0522-0 · Cited by 94 · see citing works
N-Acetylglucosamine (GlcNAc) Induction of Hyphal Morphogenesis and Transcriptional Responses in Candida albicans Are Not Dependent on Its Metabolism
Naseem, S., Gunasekera, A. H., Araya, E., & Konopka, J. B. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.249854 · Cited by 93 · see citing works
Delineating metabolic signatures of head and neck squamous cell carcinoma: Phospholipase A, a potential therapeutic target
Tripathi, P., Kamarajan, P., Somashekar, B. S., MacKinnon, N., Chinnaiyan, A. M., Kapila, Y. L., Rajendiran, T. M., & Ramamoorthy, A. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.06.025 · Cited by 93 · see citing works
High Glucose-induced O-GlcNAcylated Carbohydrate Response Element-binding Protein (ChREBP) Mediates Mesangial Cell Lipogenesis and Fibrosis
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Authors: Slawson, C., Copeland, R. J., & Hart, G. W.
Affiliations: Johns Hopkins University (US)
ORCID: Slawson, C.
Hart, G.W.
Venue: Trends in Biochemical Sciences
Publisher: Elsevier BV
Published: 2010-10
Volume: 35
Issue: 10
Pages: 547-555
ISSN: 0968-0004 (ISSN-L)
DOI: 10.1016/j.tibs.2010.04.005
PMC: PMC2949529
OpenAlex: W1982409123
Cited by: 346
References: 86
Citations by year: 2026: 9 · 2025: 19 · 2024: 17 · 2023: 11 · 2022: 18 · 2021: 22 · 2020: 21 · 2019: 17 · 2018: 34 · 2017: 30 · 2016: 23 · 2015: 25 · 2014: 30 · 2013: 24 · 2012: 27
FWCI: 1.92
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Trends in Biochemical Sciences (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health
National Cancer Institute (R01CA042486)
National Institute of Diabetes and Digestive and Kidney Diseases (R01DK061671, P30DK079637)
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 › Metabolism, Diabetes, and Cancer
Keywords: O-GlcNAcylation, UDP-GlcNAc, hexosamine biosynthetic pathway, post-translational modification, cellular metabolism, diabetes mellitus, cancer, metabolic disorders
MeSH terms: Acetylglucosamine, Animals, Diabetes Mellitus, Hexosamines, Humans, Insulin, Neoplasms, Signal Transduction

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O-GlcNAc signaling: a metabolic link between diabetes and cancer?

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