Evidence map›Paper›PMID 24497645›Full record

ArticleThe Journal of biological chemistry2014

Identification of the intracellular gate for a member of the equilibrative nucleoside transporter (ENT) family.

Raquel Valdés, Johannes Elferich, Ujwal Shinde, Scott M Landfear

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
4.1field-weighted citation impact, top 7% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Purinergic Regulation of Neutrophil Function.Frontiers in immunology · 2018
    Review
  9. Article
  10. Article
  11. Article
  12. Equilibrative nucleoside transporters-A review.Nucleosides, nucleotides & nucleic acids · 2017
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
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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.

Raquel ValdésFrom the Departments of Molecular Microbiology and Immunology and.
Johannes Elferich
Ujwal Shinde
Scott M Landfear
Oregon Health & Science University · US

Funding

Purine Nucleoside/Nucleobase Transporters in LeishmaniaR01AI044138 · NIAID · OREGON HEALTH & SCIENCE UNIVERSITY · PI LANDFEAR, SCOTT M · 1999 to 2014
$4.6M
GENETICS OF PURINE METABOLISM IN LEISHMANIA DONOVANIR01AI023682 · NIAID · UNIVERSITY OF KENTUCKY · PI ULLMAN, BUDDY · 1985 to 2013
$2.0M
NIAID NIH HHS AI44138NIAID NIH HHS R01 AI023682NIAID NIH HHS R01 AI044138
6 · The paper itself

Abstract

Equilibrative nucleoside transporters of the SLC29 family play important roles in many physiological and pharmacological processes, including import of drugs for treatment of cancer, AIDS, cardiovascular, and parasitic diseases. However, no crystal structure is available for any member of this family. In previous studies we generated a computational model of the Leishmania donovani nucleoside transporter 1.1 (LdNT1.1) that captured this permease in the outward-closed conformation, and we identified the extracellular gate. In the present study we have modeled the inward-closed conformation of LdNT1.1 using the crystal structure of the Escherichia coli fucose transporter FucP and have identified four transmembrane helices whose ends close to form a predicted intracellular gate. We have tested this prediction by site-directed mutagenesis of relevant helix residues and by cross-linking of introduced cysteine pairs. The results are consistent with the predictions of the computational model and suggest that a similarly constituted gate operates in other members of the equilibrative nucleoside transporter family.

Indexed as

Conserved SequenceHydrophobic and Hydrophilic InteractionsIntracellular SpaceLeishmania donovaniModels, MolecularMutagenesis, Site-DirectedMutationNucleoside Transport ProteinsProtein ConformationProtozoan ProteinsSequence AlignmentSequence HomologySulfhydryl CompoundsNucleoside Transport ProteinsProtozoan ProteinsSulfhydryl CompoundsComputer ModelingGatingNucleoside Nucleotide TransportPurineTransporters

Identifiers

PMID24497645
PMCPMC3979384
OpenAlexW2032688578

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.