ArticleNature communications2023
Structural basis of vitamin C recognition and transport by mammalian SVCT1 transporter.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 33 citations in OpenAlex.
- Plant-dependent and pH-responsive FeRSC advances · 2026Article
- Artificial Transmembrane Channels for Selective Ascorbic Acid Transport and Bioorthogonal Signal Transduction.Angewandte Chemie (International ed. in English) · 2026Article
- Gut Microbiota Remodeling Mediates the Therapeutic Effects of a Plant-Based Medicine on DSS-Induced Ulcerative Colitis in Mice via the Butyrate-SVCT1-Vitamin C Axis.International journal of molecular sciences · 2026Article
- Selection for Molecularly Complementary Modules (MCMs) Drives the Origins and Evolution of Pleiofunctional, Epistatic Interactomes (PEIs).Life (Basel, Switzerland) · 2026Review
- The SLC-ome of membrane transport: From molecular discovery to physiology and clinical applications.Physiological reviews · 2025Review
- Molecular basis for substrate recognition and transport of mammalian taurine transporters.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Transporters in vitamin uptake and cellular metabolism: impacts on health and disease.Life metabolism · 2025Review
- Nucleobase-ascorbate transporter OsNAT9 regulates seed vigor and drought tolerance by modulating ascorbic acid homeostasis in rice.The Plant journal : for cell and molecular biology · 2025Article
- Vitamin C in Cardiovascular Disease: From Molecular Mechanisms to Clinical Evidence and Therapeutic Applications.Antioxidants (Basel, Switzerland) · 2025Review
- Structural basis of cytokinin transport by the Arabidopsis AZG2.Nature communications · 2025Article
- Association between vitamin C, D, and K intake and inflammatory bowel disease risk: findings from 2009 to 2010 NHANES.BMC gastroenterology · 2025Article
- Back Propagation Artificial Neural Network Enhanced Accuracy of Multi-Mode Sensors.Biosensors · 2025Article
- Article
- Interdomain-linkers control conformational transitions in the SLC23 elevator transporter UraA.Nature communications · 2024Article
- Dimeric transport mechanism of human vitamin C transporter SVCT1.Nature communications · 2024Article
- The Involvement of Ascorbic Acid in Cancer Treatment.Molecules (Basel, Switzerland) · 2024Review
- Oligomerization of drug transporters: Forms, functions, and mechanisms.Acta pharmaceutica Sinica. B · 2024Review
- Structures and mechanisms of the Arabidopsis cytokinin transporter AZG1.Nature plants · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vitamin C (L-ascorbic acid) is an essential nutrient for human health, and its deficiency has long been known to cause scurvy. Sodium-dependent vitamin C transporters (SVCTs) are responsible for vitamin C uptake and tissue distribution in mammals. Here, we present cryogenic electron microscopy structures of mouse SVCT1 in both the apo and substrate-bound states. Mouse SVCT1 forms a homodimer with each protomer containing a core domain and a gate domain. The tightly packed extracellular interfaces between the core domain and gate domain stabilize the protein in an inward-open conformation for both the apo and substrate-bound structures. Vitamin C binds at the core domain of each subunit, and two potential sodium ions are identified near the binding site. The coordination of sodium ions by vitamin C explains their coupling transport. SVCTs probably deliver substrate through an elevator mechanism in combination with local structural arrangements. Altogether, our results reveal the molecular mechanism by which SVCTs recognize vitamin C and lay a foundation for further mechanistic studies on SVCT substrate transport.
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.