ArticleJournal of inherited metabolic disease2019
Low catalytic activity is insufficient to induce disease pathology in triosephosphate isomerase deficiency.
Article in Journal of inherited metabolic disease, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- The return of metabolism: biochemistry and physiology of glycolysis.Biological reviews of the Cambridge Philosophical Society · 2026Review
- Discovery and validation of small molecule stabilizers of mutant triose phosphate isomerase (TPI) as potential lead candidates for TPI deficiency.SLAS discovery : advancing life sciences R & D · 2025Article
- Dihydroxyacetone phosphate accumulation leads to podocyte pyroptosis in diabetic kidney disease.Journal of cellular and molecular medicine · 2024Article
- Newly discovered roles of triosephosphate isomerase including functions within the nucleus.Molecular medicine (Cambridge, Mass.) · 2023Review
- Itavastatin and resveratrol increase triosephosphate isomerase protein in a newly identified variant of TPI deficiency.Disease models & mechanisms · 2022Article
- Murine model of triosephosphate isomerase deficiency with anemia and severe neuromuscular dysfunction.Current research in neurobiology · 2022Article
- Identification of protein quality control regulators using a Drosophila model of TPI deficiency.Neurobiology of disease · 2021Article
- Low catalytic activity is insufficient to induce disease pathology in triosephosphate isomerase deficiency.Journal of inherited metabolic disease · 2019Article
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Authors and funding
32 authors at 8 institutions in 2 countries.
Funding
Abstract
Triosephosphate isomerase (TPI) deficiency is a fatal genetic disorder characterized by hemolytic anemia and neurological dysfunction. Although the enzyme defect in TPI was discovered in the 1960s, the exact etiology of the disease is still debated. Some aspects indicate the disease could be caused by insufficient enzyme activity, whereas other observations indicate it could be a protein misfolding disease with tissue-specific differences in TPI activity. We generated a mouse model in which exchange of a conserved catalytic amino acid residue (isoleucine to valine, Ile170Val) reduces TPI specific activity without affecting the stability of the protein dimer. TPI
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