Evidence map›Paper›PMID 33536238›Full record

ArticleLife science alliance2021

Structural comparison of GLUT1 to GLUT3 reveal transport regulation mechanism in sugar porter family.

Tânia Filipa Custódio, Peter Aasted Paulsen, Kelly May Frain, Bjørn Panyella Pedersen

Open access · goldAbstract read
In one paragraph

Article in Life science alliance, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
4.1field-weighted citation impact, top 5% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

45 citing papers in PubMed, 68 citations in OpenAlex.

  1. Identification of Small-Molecule Inhibitors ofPharmaceuticals (Basel, Switzerland) · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Direct targeting of GLUT1 in cancer: A decade of inhibitor discovery and medicinal chemistry insights.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2026
    Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. 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 · 2025
    Article
  14. Review
  15. Article
  16. Structural basis of disease mutation and substrate recognition by the human SLC2A9 transporter.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Sertoli cells as a hub in testicular development and male reproductive.Frontiers in cell and developmental biology · 2025
    Review
  18. Review
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Tânia Filipa CustódioDepartment of Molecular Biology and Genetics, Aarhus University, Aarhus C, Denmark.
Peter Aasted PaulsenDepartment of Molecular Biology and Genetics, Aarhus University, Aarhus C, Denmark.
Kelly May FrainDepartment of Molecular Biology and Genetics, Aarhus University, Aarhus C, Denmark.
Bjørn Panyella PedersenDepartment of Molecular Biology and Genetics, Aarhus University, Aarhus C, Denmark bpp@mbg.au.dk.ORCID 0000-0001-7860-7230
Aarhus University · DK

Funding

European Research Council 637372
6 · The paper itself

Abstract

The human glucose transporters GLUT1 and GLUT3 have a central role in glucose uptake as canonical members of the Sugar Porter (SP) family. GLUT1 and GLUT3 share a fully conserved substrate-binding site with identical substrate coordination, but differ significantly in transport affinity in line with their physiological function. Here, we present a 2.4 Å crystal structure of GLUT1 in an inward open conformation and compare it with GLUT3 using both structural and functional data. Our work shows that interactions between a cytosolic "SP motif" and a conserved "A motif" stabilize the outward conformational state and increases substrate apparent affinity. Furthermore, we identify a previously undescribed Cl

Indexed as

Models, MolecularProtein ConformationAmino Acid MotifsAmino Acid SequenceAnimalsBinding SitesBiological TransportGlucoseGlucose Transporter Type 1Glucose Transporter Type 3HumansLigandsOocytesProtein BindingProtein Interaction Domains and MotifsProtein IsoformsGlucoseGlucose Transporter Type 1Glucose Transporter Type 3LigandsProtein IsoformsSLC2A1 protein, humanSLC2A3 protein, humanSugars

Identifiers

PMID33536238
PMCPMC7898563
OpenAlexW3127340670

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.