ArticleCurrent protocols in protein science2011
Detection and analysis of proteins modified by O-linked N-acetylglucosamine.
Article in Current protocols in protein science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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
29 citing papers in PubMed, 92 citations in OpenAlex.
- Article
- Advances in chemical probing of proteinChemical Society reviews · 2021Review
- The Hitchhiker's guide to glycoproteomics.Biochemical Society transactions · 2021Review
- Allelic polymorphisms in a glycosyltransferase gene shape glycan repertoire in the O-linked protein glycosylation system of Neisseria.Glycobiology · 2021Article
- Role ofPhysiological reviews · 2021Review
- Methods for Enrichment and Assignment of N-Acetylglucosamine Modification Sites.Molecular & cellular proteomics : MCP · 2021Review
- Hyperglycemia Acutely Increases Cytosolic Reactive Oxygen Species viaCirculation research · 2020Article
- New Insights Into the Biology of Protein O-GlcNAcylation: Approaches and Observations.Frontiers in aging · 2020Article
- Article
- O-GlcNAc Site Mapping by Using a Combination of Chemoenzymatic Labeling, Copper-Free Click Chemistry, Reductive Cleavage, and Electron-Transfer Dissociation Mass Spectrometry.Analytical chemistry · 2019Article
- Nutrient regulation of signaling and transcription.The Journal of biological chemistry · 2019Review
- Investigation of post-translational modifications in type 2 diabetes.Clinical proteomics · 2018Review
- Antrodia cinnamomea Oligosaccharides Suppress Lipopolysaccharide-Induced Inflammation through Promoting O-GlcNAcylation and Repressing p38/Akt Phosphorylation.Molecules (Basel, Switzerland) · 2017Article
- A Putative O-Linked β-Journal of bacteriology · 2017Article
- Analysis of Protein O-GlcNAcylation by Mass Spectrometry.Current protocols in protein science · 2017Article
- Chemical Glycoproteomics.Chemical reviews · 2016Review
- Mitochondrial ATP synthase activity is impaired by suppressed O-GlcNAcylation in Alzheimer's disease.Human molecular genetics · 2015Article
- Article
- 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
- In vivo putative O-GlcNAcylation of human SCP1 and evidence for possible role of its N-terminal disordered structure.BMB reports · 2014Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
O-GlcNAc is a common post-translational modification of nuclear, mitochondrial, and cytoplasmic proteins that is implicated in the etiology of type II diabetes and Alzheimer's disease, as well as cardioprotection. This unit covers simple and comprehensive techniques for identifying proteins modified by O-GlcNAc, studying the enzymes that add and remove O-GlcNAc, and mapping O-GlcNAc modification sites.
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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.