ArticleInternational journal of molecular sciences2022
Proteomic Analysis of Methylglyoxal Modifications Reveals Susceptibility of Glycolytic Enzymes to Dicarbonyl Stress.
Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 36 citations in OpenAlex.
- Promoter Hypermethylation-Driven NPHS2 Silencing Promotes Immune Escape and Sunitinib Resistance in Clear Cell Renal Cell Carcinoma.Oncology research · 2026Article
- A Chemical Mechanistic Path Leads the Way to Cellular Argpyrimidine.Journal of the American Chemical Society · 2025Article
- Protein modifications by advanced glycation end products (AGEs) in human clear cell renal cell carcinoma.Journal of translational medicine · 2025Article
- Methylglyoxal mutagenizes single-stranded DNA via Rev1-associated slippage and mispairing.Nucleic acids research · 2025Article
- Alternative Splicing in Tumorigenesis and Cancer Therapy.Biomolecules · 2025Review
- Methylglyoxal mutagenizes single-stranded DNA via Rev1-associated slippage and mispairing.bioRxiv : the preprint server for biology · 2025Article
- TgGloL is an atypical glyoxalase/VOC domain-containing apicoplast protein that is important for the growth ofMolecular biology of the cell · 2025Article
- Global transcriptional analysis of human FHs 74 Int intestinal epithelial cells after exposure to advanced glycation end products.PloS one · 2025Article
- Methylglyoxal-Induced Modifications in Human Triosephosphate Isomerase: Structural and Functional Repercussions of Specific Mutations.Molecules (Basel, Switzerland) · 2024Article
- Endogenous Cellular Metabolite Methylglyoxal Induces DNA-Protein Cross-Links in Living Cells.ACS chemical biology · 2024Article
- Article
- Nordihydroguaiaretic acid inhibits glyoxalase I, and causes the accumulation of methylglyoxal followed by cell-growth inhibition.Molecular biology reports · 2022Article
- Glyoxalase 2: Towards a Broader View of the Second Player of the Glyoxalase System.Antioxidants (Basel, Switzerland) · 2022Review
- An Introduction to the Special Issue "Protein Glycation in Food, Nutrition, Health and Disease".International journal of molecular sciences · 2022Article
- The Glyoxalase System Is a Novel Cargo of Amniotic Fluid Stem-Cell-Derived Extracellular Vesicles.Antioxidants (Basel, Switzerland) · 2022Article
- Methylglyoxal Impairs Sister Chromatid Separation in Lymphocytes.International journal of molecular sciences · 2022Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Methylglyoxal (MGO) is a highly reactive cellular metabolite that glycates lysine and arginine residues to form post-translational modifications known as advanced glycation end products. Because of their low abundance and low stoichiometry, few studies have reported their occurrence and site-specific locations in proteins. Proteomic analysis of WIL2-NS B lymphoblastoid cells in the absence and presence of exogenous MGO was conducted to investigate the extent of MGO modifications. We found over 500 MGO modified proteins, revealing an over-representation of these modifications on many glycolytic enzymes, as well as ribosomal and spliceosome proteins. Moreover, MGO modifications were observed on the active site residues of glycolytic enzymes that could alter their activity. We similarly observed modification of glycolytic enzymes across several epithelial cell lines and peripheral blood lymphocytes, with modification of fructose bisphosphate aldolase being observed in all samples. These results indicate that glycolytic proteins could be particularly prone to the formation of MGO adducts.
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