ArticleNature communications2021
Synergistic sequence contributions bias glycation outcomes.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 24 citations in OpenAlex.
- Rational Design of an Electronically Gated Dicyano-BODIPY Platform for Reversible-Covalent Imaging of Methylglyoxal.JACS Au · 2026Article
- Profiling Selectivity for theBiochemistry · 2026Article
- Psoriasis Is Accompanied by Low Serum Levels of MG-H1, GOLD and MOLD: LC-Orbitrap-MS/MS Analysis of Chosen Glycation Products.Molecules (Basel, Switzerland) · 2026Article
- Discovery of Glycation-Derived Cross-links at Arginine.Journal of the American Chemical Society · 2026Article
- Article
- Identification of Methylglyoxal Reactive Proteins with Photocaged Glycating Agents.Chembiochem : a European journal of chemical biology · 2025Article
- A Chemical Mechanistic Path Leads the Way to Cellular Argpyrimidine.Journal of the American Chemical Society · 2025Article
- Predictable Modulation of a Spontaneous Post-translational Modification in Living Cells.Angewandte Chemie (International ed. in English) · 2025Article
- Mechanisms of metabolism-coupled protein modifications.Nature chemical biology · 2025Review
- The chemical language of protein glycation.Nature chemical biology · 2025Review
- Glyoxalase I is a novel target for the prevention of metabolic derangement.Pharmacology & therapeutics · 2023Review
- A global view of the human post-translational modification landscape.The Biochemical journal · 2023Review
- Parkinsonism-Associated Protein DJ-1 Is an Antagonist, Not an Eraser, for Protein Glycation.Biochemistry · 2023Article
- Comparison of Color Development Kinetics of Tanning Reactions of Dihydroxyacetone with Free and Protected Basic Amino Acids.ACS omega · 2022Article
- Methylglyoxal and Its Adducts: Induction, Repair, and Association with Disease.Chemical research in toxicology · 2022Review
- Is dietary intake of advanced glycation end products associated with mortality among adults with diabetes?Nutrition, metabolism, and cardiovascular diseases : NMCD · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The methylglyoxal-derived hydroimidazolone isomer, MGH-1, is an abundant advanced glycation end-product (AGE) associated with disease and age-related disorders. As AGE formation occurs spontaneously and without an enzyme, it remains unknown why certain sites on distinct proteins become modified with specific AGEs. Here, we use a combinatorial peptide library to determine the chemical features that favor MGH-1. When properly positioned, tyrosine is found to play an active mechanistic role that facilitates MGH-1 formation. This work offers mechanistic insight connecting multiple AGEs, including MGH-1 and carboxyethylarginine (CEA), and reconciles the role of negative charge in influencing glycation outcomes. Further, this study provides clear evidence that glycation outcomes can be influenced through long- or medium-range cooperative interactions. This work demonstrates that these chemical features also predictably template selective glycation on full-length protein targets expressed in mammalian cells. This information is vital for developing methods that control glycation in living cells and will enable the study of glycation as a functional post-translational modification.
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.