ArticleAdvances in bioinformatics2014
Alternate Phosphorylation/O-GlcNAc Modification on Human Insulin IRSs: A Road towards Impaired Insulin Signaling in Alzheimer and Diabetes.
Article in Advances in bioinformatics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
17 citing papers in PubMed, 30 citations in OpenAlex.
- O-GlcNAcylation in Endocrinology: The Sweet Link.Endocrinology · 2025Review
- Glucose enrichment reduces lifespan and promotes tau phosphorylation in human tau-expressing C. elegans, unaffected by O-β-GlcNAcylation induction.Journal of molecular medicine (Berlin, Germany) · 2025Article
- O-GlcNAc participates in the meiosis of aging oocytes by mediating mitochondrial function.Reproduction (Cambridge, England) · 2024Article
- Posttranslational Modifications ofPharmacological reviews · 2024Review
- Observational
- Systematic analysis of cuproptosis-related genes in immunological characterization and predictive drugs in Alzheimer's disease.Frontiers in aging neuroscience · 2023Article
- Regulation of the urea cycle by CPS1 O-GlcNAcylation in response to dietary restriction and aging.Journal of molecular cell biology · 2022Article
- Effect of Selenium Treatment on Central Insulin Sensitivity: A Proteomic Analysis in β-Amyloid Precursor Protein/Presenilin-1 Transgenic Mice.Frontiers in molecular neuroscience · 2022Article
- O-GlcNAcylation of core components of the translation initiation machinery regulates protein synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The Role of Insulin Resistance and Protein O-GlcNAcylation in Neurodegeneration.Frontiers in neuroscience · 2019Review
- Evidence for Compromised Insulin Signaling and Neuronal Vulnerability in Experimental Model of Sporadic Alzheimer's Disease.Molecular neurobiology · 2018Article
- Dihydrolipoamide dehydrogenase suppression induces human tau phosphorylation by increasing whole body glucose levels in a C. elegans model of Alzheimer's Disease.Experimental brain research · 2018Article
- Oxidative toxicity in diabetes and Alzheimer's disease: mechanisms behind ROS/ RNS generation.Journal of biomedical science · 2017Review
- Taming Alzheimer's disease: New perspectives, newer horizons.Iranian journal of neurology · 2017Review
- Modifications and Trafficking of APP in the Pathogenesis of Alzheimer's Disease.Frontiers in molecular neuroscience · 2017Review
- The Role of PTP1B O-GlcNAcylation in Hepatic Insulin Resistance.International journal of molecular sciences · 2015Article
- Prohibitin: a potential therapeutic target in tyrosine kinase signaling.Signal transduction and targeted therapyReview
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Impaired insulin signaling has been thought of as important step in both Alzheimer's disease (AD) and type 2 diabetes mellitus (T2DM). Posttranslational modifications (PTMs) regulate functions and interaction of insulin with insulin receptors substrates (IRSs) and activate insulin signaling downstream pathways via autophosphorylation on several tyrosine (TYR) residues on IRSs. Two important insulin receptor substrates 1 and 2 are widely expressed in human, and alternative phosphorylation on their serine (Ser) and threonine (Thr) residues has been known to block the Tyr phosphorylation of IRSs, thus inhibiting insulin signaling and promoting insulin resistance. Like phosphorylation, O-glycosylation modification is important PTM and inhibits phosphorylation on same or neighboring Ser/Thr residues, often called Yin Yang sites. Both IRS-1 and IRS-2 have been shown to be O-glycosylated; however exact sites are not determined yet. In this study, by using neuronal network based prediction methods, we found more than 50 Ser/Thr residues that have potential to be O-glycosylated and may act as possible sites as well. Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.