(2022) 2022 Alzheimer’s disease facts and figures. Alzheimers Dement 18(4):700-789
Tiwari S et al (2019) Alzheimer’s disease: pathogenesis, diagnostics, and therapeutics. Int J Nanomedicine 14:5541–5554
Article CAS PubMed PubMed Central Google Scholar
Khan S, Barve KH, Kumar MS (2020) Recent advancements in pathogenesis, diagnostics and treatment of Alzheimer’s disease. Curr Neuropharmacol 18(11):1106–1125
Article CAS PubMed PubMed Central Google Scholar
Bakota L, Brandt R (2016) Tau biology and tau-directed therapies for Alzheimer’s disease. Drugs 76(3):301–313
Article CAS PubMed PubMed Central Google Scholar
Wegmann S, Biernat J, Mandelkow E (2021) A current view on Tau protein phosphorylation in Alzheimer’s disease. Curr Opin Neurobiol 69:131–138
Article CAS PubMed Google Scholar
Vu LD, Gevaert K, De Smet I (2018) Protein language: post-translational modifications talking to each other. Trends Plant Sci 23(12):1068–1080
Article CAS PubMed Google Scholar
Alquezar C, Arya S, Kao AW (2020) Tau post-translational modifications: dynamic transformers of Tau function, degradation, and aggregation. Front Neurol 11:595532
Gong CX, Iqbal K (2008) Hyperphosphorylation of microtubule-associated protein tau: a promising therapeutic target for Alzheimer disease. Curr Med Chem 15(23):2321–2328
Article CAS PubMed PubMed Central Google Scholar
Hanger DP, Anderton BH, Noble W (2009) Tau phosphorylation: the therapeutic challenge for neurodegenerative disease. Trends Mol Med 15(3):112–119
Article CAS PubMed Google Scholar
Yuzwa SA, Vocadlo DJ (2009) O-GlcNAc modification and the tauopathies: insights from chemical biology. Curr Alzheimer Res 6(5):451–454
Article CAS PubMed Google Scholar
Iqbal K, Gong CX, Liu F (2014) Microtubule-associated protein tau as a therapeutic target in Alzheimer’s disease. Expert Opin Ther Targets 18(3):307–318
Article CAS PubMed Google Scholar
Smet-Nocca C et al (2011) Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation. Mol Biosyst 7(5):1420–1429
Article CAS PubMed Google Scholar
Lazarus MB et al (2011) Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature 469(7331):564–567
Article CAS PubMed PubMed Central Google Scholar
Butkinaree C, Park K, Hart GW (2010) O-linked beta-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
Article CAS PubMed Google Scholar
Bond MR et al (2014) Conserved nutrient sensor O-GlcNAc transferase is integral to C. elegans pathogen-specific immunity. PLoS One 9(12):e113231
Article PubMed PubMed Central Google Scholar
Rahman MM et al (2010) Intracellular protein glycosylation modulates insulin mediated lifespan in C.elegans. Aging (Albany NY). 2(10):678–90.
Yuzwa SA et al (2008) A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo. Nat Chem Biol 4(8):483–490
Article CAS PubMed Google Scholar
Ahmad WD, Shabbiri KD, Ahmad I (2020) Prediction of human tau 3D structure, and interplay between O-beta-GlcNAc and phosphorylation modifications in Alzheimer’s disease: C. elegans as a suitable model to study these interactions in vivo. Biochem Biophys Res Commun 528(3):466–472
Article CAS PubMed Google Scholar
Jahangir Z, Ahmad W, Shabbiri K (2014) Alternate phosphorylation/O-GlcNAc modification on human insulin IRSs: a road towards impaired insulin signaling in Alzheimer and diabetes. Adv Bioinformatics 2014:324753
Article PubMed PubMed Central Google Scholar
Kenyon C (2005) The plasticity of aging: insights from long-lived mutants. Cell 120(4):449–460
Article CAS PubMed Google Scholar
Mosconi L et al (2007) Early detection of Alzheimer’s disease using neuroimaging. Exp Gerontol 42(1–2):129–138
Mosconi L (2005) Brain glucose metabolism in the early and specific diagnosis of Alzheimer’s disease. FDG-PET studies in MCI and AD. Eur J Nucl Med Mol Imaging 32(4):486–510
Article CAS PubMed Google Scholar
Hunt A et al (2007) Reduced cerebral glucose metabolism in patients at risk for Alzheimer’s disease. Psychiatry Res 155(2):147–154
Article CAS PubMed Google Scholar
Hoyer S (2000) Brain glucose and energy metabolism abnormalities in sporadic Alzheimer disease. Causes and consequences: an update. Exp Gerontol 35(9–10):1363–1372
Article CAS PubMed Google Scholar
Hoyer S (1991) Abnormalities of glucose metabolism in Alzheimer’s disease. Ann N Y Acad Sci 640:53–58
Article CAS PubMed Google Scholar
Costantini LC et al (2008) Hypometabolism as a therapeutic target in Alzheimer’s disease. BMC Neurosci 9(Suppl 2):S16
Article PubMed PubMed Central Google Scholar
Liu F et al (2004) O-GlcNAcylation regulates phosphorylation of tau: a mechanism involved in Alzheimer’s disease. Proc Natl Acad Sci U S A 101(29):10804–10809
Article CAS PubMed PubMed Central Google Scholar
Liu F et al (2009) Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer’s disease. Brain 132(Pt 7):1820–1832
Article PubMed PubMed Central Google Scholar
Goldberg HJ et al (2006) Posttranslational, reversible O-glycosylation is stimulated by high glucose and mediates plasminogen activator inhibitor-1 gene expression and Sp1 transcriptional activity in glomerular mesangial cells. Endocrinology 147(1):222–231
Article CAS PubMed Google Scholar
Beharry C et al (2014) Tau-induced neurodegeneration: mechanisms and targets. Neurosci Bull 30(2):346–358
Article CAS PubMed PubMed Central Google Scholar
Baudoin L, Issad T (2014) O-GlcNAcylation and Inflammation: a vast territory to explore. Front Endocrinol (Lausanne) 5:235
Aguilar H et al (2014) Role for high-glucose-induced protein O-GlcNAcylation in stimulating cardiac fibroblast collagen synthesis. Am J Physiol Cell Physiol 306(9):C794-804
Article CAS PubMed PubMed Central Google Scholar
Lee SJ, Murphy CT, Kenyon C (2009) Glucose shortens the life span of C. elegans by downregulating DAF-16/FOXO activity and aquaporin gene expression. Cell Metab 10(5):379–391
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