ArticleMolecules (Basel, Switzerland)2023
Identification of Structural Determinants of the Transport of the Dehydroascorbic Acid Mediated by Glucose Transport GLUT1.
Article in Molecules (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 7 citations in OpenAlex.
- Ascorbic Acid Modulates Collagen Properties in Glucocorticoid-Induced Osteoporotic Bone: Insights into Chemical, Mechanical, and Biological Regulation.Advanced healthcare materials · 2026Article
- TET2 downregulation limits oxidative stress-induced cytotoxicity of high dose ascorbate in dabrafenib-resistant melanoma cells.Cancer drug resistance (Alhambra, Calif.) · 2026Article
- A Comprehensive Review of Vitamin C for Cancer Therapy: Anti-Tumor Mechanisms and Nano-Formulation Strategies.International journal of nanomedicine · 2026Review
- Glut1 Deficiency Syndrome: Novel Pathomechanisms, Current Concepts, and Challenges.Journal of inherited metabolic disease · 2025Review
- Modulation of transmembrane domain architecture by the intracellular C-terminal domain in yeast glucose transporter-receptor divergence.Frontiers in molecular biosciences · 2025Review
- Relevance of Sugar Transport across the Cell Membrane.International journal of molecular sciences · 2023Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
GLUT1 is a facilitative glucose transporter that can transport oxidized vitamin C (i.e., dehydroascorbic acid) and complements the action of reduced vitamin C transporters. To identify the residues involved in human GLUT1's transport of dehydroascorbic acid, we performed docking studies in the 5 Å grid of the glucose-binding cavity of GLUT1. The interactions of the bicyclic hemiacetal form of dehydroascorbic acid with GLUT1 through hydrogen bonds with the -OH group of C3 and C5 were less favorable than the interactions with the sugars transported by GLUT1. The eight most relevant residues in such interactions (i.e., F26, Q161, I164, Q282, Y292, and W412) were mutated to alanine to perform functional studies for dehydroascorbic acid and the glucose analog, 2-deoxiglucose, in
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Registered trials
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