Evidence map›Paper›PMID 24550316›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Functional architecture of MFS D-glucose transporters.

M Gregor Madej, Linfeng Sun, Nieng Yan, H Ronald Kaback

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

71 citing papers in PubMed, 117 citations in OpenAlex.

  1. Article
  2. Multi-layered metabolic remodeling ofMetabolic engineering communications · 2026
    Article
  3. A two-step mechanism for sugar translocation.Nature structural & molecular biology · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Functional Outlook ofMicroorganisms · 2025
    Article
  9. Article
  10. Article
  11. Review
  12. Key sugar transporters drive development and pathogenicity inFrontiers in cellular and infection microbiology · 2025
    Article
  13. Review
  14. Article
  15. Expression patterns ofApplied and environmental microbiology · 2024
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

11 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

4 authors at 3 institutions in 4 countries.

M Gregor MadejDepartment of Physiology, Department of Microbiology, Immunology, and Molecular Genetics, and Molecular Biology Institute, University of California, Los Angeles, CA 90095-1662.
Linfeng Sun
Nieng Yan
H Ronald Kaback
Tsinghua University · CNCzech Academy of Sciences, Institute of Physiology · CZLaboratory of Molecular Genetics · PL

Funding

Yeast ExpressionP50GM073210 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 2004 to 2013
$21.5M
NEW APPROACHES TO MEMBRANE PROTEIN STRUCTURESR01DK051131 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 1996 to 2014
$5.2M
Structural Basis for Mechanism of Secondary TransportersR01DK069463 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 2005 to 2013
$3.7M
Structural Basis for Mechanism of Secondary TransportersR56DK069463 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 2009 to 2009
$500k
Dynamics of the Lactose Permease of Escherichia ColiR56DK051131 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 2015 to 2015
$154k
NIDDK NIH HHS DK069463NIDDK NIH HHS DK51131NIDDK NIH HHS R01 DK051131NIDDK NIH HHS R01 DK069463NIDDK NIH HHS R56 DK051131NIDDK NIH HHS R56 DK069463NIGMS NIH HHS GM073210NIGMS NIH HHS P50 GM073210
6 · The paper itself

Abstract

The Major Facilitator Superfamily (MFS) is a diverse group of secondary transporters with over 10,000 members, found in all kingdoms of life, including Homo sapiens. One objective of determining crystallographic models of the bacterial representatives is identification and physical localization of residues important for catalysis in transporters with medical relevance. The recently solved crystallographic models of the D-xylose permease XylE from Escherichia coli and GlcP from Staphylococcus epidermidus, homologs of the human D-glucose transporters, the GLUTs (SLC2), provide information about the structure of these transporters. The goal of this work is to examine general concepts derived from the bacterial XylE, GlcP, and other MFS transporters for their relevance to the GLUTs by comparing conservation of functionally critical residues. An energy landscape for symport and uniport is presented. Furthermore, the substrate selectivity of XylE is compared with GLUT1 and GLUT5, as well as a XylE mutant that transports D-glucose.

Indexed as

Models, MolecularProtein ConformationBase SequenceBinding SitesBiological TransportCalorimetryDNA, ComplementaryEscherichia coli O157Escherichia coli ProteinsGlucose Transport Proteins, FacilitativeHumansLiposomesMolecular Sequence DataSequence AlignmentSequence Analysis, DNASequence HomologyDNA, ComplementaryEscherichia coli ProteinsGlucose Transport Proteins, FacilitativeLiposomesSymportersxylE protein, E coliglucose transportligand dockingmembrane proteinssequence analysissolute carrier transporter

Identifiers

PMID24550316
PMCPMC3932877
OpenAlexW2096985447

What OpenQuestion holds

Textmetadata
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.