ArticleNature2015
Structure and mechanism of the mammalian fructose transporter GLUT5.
Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 146 papers.
What it found
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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.
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Who cites it
146 citing papers in PubMed, 236 citations in OpenAlex.
- Spatiotemporal heterogeneity and dynamic evolution of microglial glucose metabolic reprogramming in Alzheimer's disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026Review
- Unraveling the Complex Hydrogen-Bonding and Solvation Patterns of Fructose Tautomers via Complementary AIMD and Classical MD Simulations.ACS physical chemistry Au · 2026Article
- Substrate binding reorganizes the energetic landscape of Plasmodium falciparum hexose transporter PfHT1.bioRxiv : the preprint server for biology · 2026Article
- Consumption of Fructose by Cultured Primary Rat Astrocytes.Neurochemical research · 2026Article
- Glucose Transporters: Structure, Trafficking, Physiology, and Disease Relevance.Current issues in molecular biology · 2026Review
- Fructose-Based Single-Chain Polymer Nanoparticles for GLUT1-Mediated Delivery: Impact of Polymer Design on Uptake and In Vivo Performance.Advanced healthcare materials · 2026Article
- A two-step mechanism for sugar translocation.Nature structural & molecular biology · 2026Article
- Microglial fructose metabolism is essential for glioblastoma growth.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Role and mechanism of circ_001024 endogenous competition for miR-145-3p targeting to regulate GLUT5 in RCC.BMC cancer · 2025Article
- Structural and functional insights of AmpG in muropeptide transport and multiple β-lactam antibiotics resistance.Nature communications · 2025Article
- Structural Insights into the Substrate Egress Pathways Explains Specificity and Inhibition of Human Glucose Transporters (GLUT1 and GLUT9).ACS pharmacology & translational science · 2025Article
- The Effect of GLUT-1-XbaI G>T and HaeIII T>C Polymorphisms onMolecular imaging and radionuclide therapy · 2025Article
- Comparative analysis of STP6 and STP10 unravels molecular selectivity in sugar transport proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Do microglia metabolize fructose in Alzheimer's disease?Journal of neuroinflammation · 2025Review
- A structural perspective on insect gustatory receptors.Chemical senses · 2025Review
- AKR1B1-dependent fructose metabolism enhances malignancy of cancer cells.Cell death and differentiation · 2024Article
- Review
- Structural basis for urate recognition and apigenin inhibition of human GLUT9.Nature communications · 2024Article
- Profiling Cell Heterogeneity and Fructose Transporter Expression in the Rat Nephron by Integrating Single-Cell and Microdissected Tubule Segment Transcriptomes.International journal of molecular sciences · 2024Article
- Multiple roles for the cytoplasmic C-terminal domains of the yeast cell surface receptors Rgt2 and Snf3 in glucose sensing and signaling.Scientific reports · 2024Article
86 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
22 authors at 6 institutions in 3 countries.
Funding
Abstract
The altered activity of the fructose transporter GLUT5, an isoform of the facilitated-diffusion glucose transporter family, has been linked to disorders such as type 2 diabetes and obesity. GLUT5 is also overexpressed in certain tumour cells, and inhibitors are potential drugs for these conditions. Here we describe the crystal structures of GLUT5 from Rattus norvegicus and Bos taurus in open outward- and open inward-facing conformations, respectively. GLUT5 has a major facilitator superfamily fold like other homologous monosaccharide transporters. On the basis of a comparison of the inward-facing structures of GLUT5 and human GLUT1, a ubiquitous glucose transporter, we show that a single point mutation is enough to switch the substrate-binding preference of GLUT5 from fructose to glucose. A comparison of the substrate-free structures of GLUT5 with occluded substrate-bound structures of Escherichia coli XylE suggests that, in addition to global rocker-switch-like re-orientation of the bundles, local asymmetric rearrangements of carboxy-terminal transmembrane bundle helices TM7 and TM10 underlie a 'gated-pore' transport mechanism in such monosaccharide transporters.
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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.