Evidence map›Paper›PMID 32591905›Full record

ReviewPflugers Archiv : European journal of physiology2020

Structure, function and regulation of mammalian glucose transporters of the SLC2 family.

Geoffrey D Holman

Open access · hybridAbstract readReview
In one paragraph

Review in Pflugers Archiv : European journal of physiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 129 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
129citing papers in PubMed, 2 pooled it
8.7field-weighted citation impact, top 1% 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

129 citing papers in PubMed, 2 syntheses or guidelines pooled it, 215 citations in OpenAlex.

  1. Pooled it
  2. Natural products targeting glycolysis in cancer.Frontiers in pharmacology · 2022
    Pooled it
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. A two-step mechanism for sugar translocation.Nature structural & molecular biology · 2026
    Article
  15. Article
  16. Article
  17. Article
  18. Mechanistic Role of Disulfidptosis in Type 2 Diabetes Mellitus.Molecular nutrition & food research · 2026
    Review
  19. Article
  20. Review

69 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

Geoffrey D HolmanDepartment of Biology and Biochemistry, University of Bath, Bath, BA2 7AY, UK. g.d.holman@bath.ac.uk.ORCID http://orcid.org/0000-0001-7045-1358
University of Bath · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The SLC2 genes code for a family of GLUT proteins that are part of the major facilitator superfamily (MFS) of membrane transporters. Crystal structures have recently revealed how the unique protein fold of these proteins enables the catalysis of transport. The proteins have 12 transmembrane spans built from a replicated trimer substructure. This enables 4 trimer substructures to move relative to each other, and thereby alternately opening and closing a cleft to either the internal or the external side of the membrane. The physiological substrate for the GLUTs is usually a hexose but substrates for GLUTs can include urate, dehydro-ascorbate and myo-inositol. The GLUT proteins have varied physiological functions that are related to their principal substrates, the cell type in which the GLUTs are expressed and the extent to which the proteins are associated with subcellular compartments. Some of the GLUT proteins translocate between subcellular compartments and this facilitates the control of their function over long- and short-time scales. The control of GLUT function is necessary for a regulated supply of metabolites (mainly glucose) to tissues. Pathophysiological abnormalities in GLUT proteins are responsible for, or associated with, clinical problems including type 2 diabetes and cancer and a range of tissue disorders, related to tissue-specific GLUT protein profiles. The availability of GLUT crystal structures has facilitated the search for inhibitors and substrates and that are specific for each GLUT and that can be used therapeutically. Recent studies are starting to unravel the drug targetable properties of each of the GLUT proteins.

Indexed as

AnimalsCatalytic DomainEnzyme StabilityGlucoseGlucose Transport Proteins, FacilitativeHumansProtein TransportGlucoseGlucose Transport Proteins, FacilitativeATP depletionGlucose transportGLUT1GLUT2GLUT3GLUT4GLUT5GLUT proteinsHypoxiaInsulinMembrane transportRegulated transport

Identifiers

PMID32591905
PMCPMC7462842
OpenAlexW3037722694

What Socratic 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 Socratic graph.