ReviewProteomics. Clinical applications2013
O-GlcNAcomics--Revealing roles of O-GlcNAcylation in disease mechanisms and development of potential diagnostics.
Review in Proteomics. Clinical applications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed.
- β-cell neogenesis: A rising star to rescue diabetes mellitus.Journal of advanced research · 2024Review
- Nutrient sensitive proteinLife science alliance · 2022Article
- O-GlcNAcylation regulation of cellular signaling in cancer.Cellular signalling · 2022Review
- The molecular imprinting of magnetic nanoparticles with boric acid affinity for the selective recognition and isolation of glycoproteins.RSC advances · 2021Article
- O-GlcNAcylation in early stages of chronic lymphocytic leukemia: Protocol development for flow cytometry.Cancer biomarkers : section A of Disease markers · 2021Article
- Regulation of pancreatic cancer TRAIL resistance by protein O-GlcNAcylation.Laboratory investigation; a journal of technical methods and pathology · 2020Article
- Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance.Chemical reviews · 2019Article
- Hyper-O-GlcNAcylation promotes epithelial-mesenchymal transition in endometrial cancer cells.Oncotarget · 2019Article
- Human and rodent temporal lobe epilepsy is characterized by changes in O-GlcNAc homeostasis that can be reversed to dampen epileptiform activity.Neurobiology of disease · 2019Article
- Article
- LW-AFC Effects onAging and disease · 2017Article
- Post-translational modifications of the cardiac proteome in diabetes and heart failure.Proteomics. Clinical applications · 2016Review
- Activity Based High-Throughput Screening for Novel O-GlcNAc Transferase Substrates Using a Dynamic Peptide Microarray.PloS one · 2016Article
- Transition from identity to bioactivity-guided proteomics for biomarker discovery with focus on the PF2D platform.Proteomics. Clinical applications · 2016Review
- Natural history of β-cell adaptation and failure in type 2 diabetes.Molecular aspects of medicine · 2015Review
- The putative eukaryote-like O-GlcNAc transferase of the cyanobacterium Synechococcus elongatus PCC 7942 hydrolyzes UDP-GlcNAc and is involved in multiple cellular processes.Journal of bacteriology · 2015Article
- O-GlcNAcylation as a novel ammonia-induced posttranslational protein modification in cultured rat astrocytes.Metabolic brain disease · 2014Article
- Role for high-glucose-induced protein O-GlcNAcylation in stimulating cardiac fibroblast collagen synthesis.American journal of physiology. Cell physiology · 2014Article
- O-GlcNAc profiling: from proteins to proteomes.Clinical proteomics · 2014Article
- The challenge and promise of glycomics.Chemistry & biology · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
O-linked-β-N-acetylglucosamine (O-GlcNAc) is a dynamic PTM of the 3'-hydroxyl groups of serine or threonine residues of nuclear, cytoplasmic, and mitochondrial proteins. The cycling of this modification is regulated in response to nutrients, stress, and other extracellular stimuli by the catalytic activities of O-GlcNAc transferase and O-GlcNAcase. O-GlcNAc is functionally similar to phosphorylation and has been demonstrated to play critical roles in numerous biological processes, including cell signaling, transcription, and disease etiology. Since its discovery nearly 30 years ago, studies have demonstrated that the O-GlcNAc is highly abundant and widespread, like phosphorylation however, the development of methodologies to study O-GlcNAc at the site level has been challenging. Recently, a number of studies have overcome these challenges and describe new tagging, enrichment, and mass spectrometric-based approaches to study O-GlcNAc in terms of its site identification, stoichiometry, and dynamics on proteins. The development of these methods are key for elucidation of O-GlcNAc's functional crosstalk with phosphorylation and other PTMs, and will serve to provide the necessary information for the development of site-specific antibodies, which will aid in the determination of a particular protein's site-specific function. In this review, we describe these methods and summarize results obtained from them demonstrating the roles of O-GlcNAc in diabetes, cancer, Alzheimer's, and in learning and memory, while also describing how these new strategies have implicated O-GlcNAc as a potential diagnostic for the screening of patients for prediabetes.
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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.