ReviewACS chemical biology2017
Deciphering the Functions of Protein O-GlcNAcylation with Chemistry.
Review in ACS chemical biology, 2017. 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
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
17 citing papers in PubMed, 30 citations in OpenAlex.
- Dissecting the Mechanisms Underlying Substrate Recognition and Functional Regulation of O-GlcNAc Cycling Enzymes.ACS chemical biology · 2025Review
- A tale of two sugars: O-GlcNAc and O-fucose orchestrate growth, development, and acclimation in plants.Trends in biochemical sciences · 2025Review
- In Situ Imaging of O-Linked β-N-Acetylglucosamine Using On-Tissue Hydrolysis and MALDI Mass Spectrometry.Cancers · 2023Article
- Advances in Optical Sensors ofBioconjugate chemistry · 2022Review
- The Beginner's Guide toFrontiers in immunology · 2022Review
- Advances in chemical probing of proteinChemical Society reviews · 2021Review
- Photocrosslinking O-GlcNAcylated Proteins to Neighboring Biomolecules.Current protocols · 2021Article
- O-GlcNAcylation in Hyperglycemic Pregnancies: Impact on Placental Function.Frontiers in endocrinology · 2021Review
- The Metabolic Chemical Reporter AcFrontiers in chemistry · 2021Article
- Precision Mapping of O-LinkedJournal of the American Chemical Society · 2020Article
- O-Acetylated Chemical Reporters of Glycosylation Can Display Metabolism-Dependent Background Labeling of Proteins but Are Generally Reliable Tools for the Identification of Glycoproteins.Frontiers in chemistry · 2020Article
- Recent advances in mass spectrometry (MS)-based glycoproteomics in complex biological samples.Trends in analytical chemistry : TRAC · 2019Article
- Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance.Chemical reviews · 2019Article
- Chemical and Biochemical Strategies To Explore the Substrate Recognition of O-GlcNAc-Cycling Enzymes.Chembiochem : a European journal of chemical biology · 2019Review
- Evaluation of a PET Radioligand to ImageJournal of nuclear medicine : official publication, Society of Nuclear Medicine · 2019Article
- New use for CETSA: monitoring innate immune receptor stability via post-translational modification by OGT.Journal of bioenergetics and biomembranes · 2018Article
- Glycolysis-Derived Compounds From Astrocytes That Modulate Synaptic Communication.Frontiers in neuroscience · 2018Review
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 at 1 institution in 1 country.
Funding
Abstract
O-GlcNAcylation is the modification of serine and threonine residues with β-N-acetylglucosamine (O-GlcNAc) on intracellular proteins. This dynamic modification is attached by O-GlcNAc transferase (OGT) and removed by O-GlcNAcase (OGA) and is a critical regulator of various cellular processes. Furthermore, O-GlcNAcylation is dysregulated in many diseases, such as diabetes, cancer, and Alzheimer's disease. However, the precise role of this modification and its cycling enzymes (OGT and OGA) in normal and disease states remains elusive. This is partially due to the difficulty in studying O-GlcNAcylation with traditional genetic and biochemical techniques. In this review, we will summarize recent progress in chemical approaches to overcome these obstacles. We will cover new inhibitors of OGT and OGA, advances in metabolic labeling and cellular imaging, synthetic approaches to access homogeneous O-GlcNAcylated proteins, and cross-linking methods to identify O-GlcNAc-protein interactions. We will also discuss remaining gaps in our toolbox for studying O-GlcNAcylation and questions of high interest that are yet to be answered.
Indexed as
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.