Evidence map›Paper›PMID 26406980›Full record

ArticlePloS one2015

The Role of Flexible Loops in Folding, Trafficking and Activity of Equilibrative Nucleoside Transporters.

Jaya Aseervatham, Lucky Tran, Khaled Machaca, Olga Boudker

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 17 citations in OpenAlex.

  1. A review of the Augustine blood group system.International journal of hematology · 2024
    Review
  2. Article
  3. Insight into the nucleoside transport and inhibition of human ENT1.Current research in structural biology · 2022
    Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Equilibrative nucleoside transporters-A review.Nucleosides, nucleotides & nucleic acids · 2017
    Review
  13. 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 2 institutions in 2 countries.

Jaya AseervathamDepartment of Physiology and Biophysics, Weill Cornell Medical College in Qatar, Qatar foundation, Education City, Doha, Qatar.
Lucky TranDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, United States of America.
Khaled MachacaDepartment of Physiology and Biophysics, Weill Cornell Medical College in Qatar, Qatar foundation, Education City, Doha, Qatar.
Olga BoudkerDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, United States of America.
Cornell University · USWeill Cornell Medical College in Qatar · QA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Equilibrative nucleoside transporters (ENTs) are integral membrane proteins, which reside in plasma membranes of all eukaryotic cells and mediate thermodynamically downhill transport of nucleosides. This process is essential for nucleoside recycling, and also plays a key role in terminating adenosine-mediated cellular signaling. Furthermore, ENTs mediate the uptake of many drugs, including anticancer and antiviral nucleoside analogues. The structure and mechanism, by which ENTs catalyze trans-membrane transport of their substrates, remain unknown. To identify the core of the transporter needed for stability, activity, and for its correct trafficking to the plasma membrane, we have expressed human ENT deletion mutants in Xenopus laevis oocytes and determined their localization, transport properties and susceptibility to inhibition. We found that the carboxyl terminal trans-membrane segments are essential for correct protein folding and trafficking. In contrast, the soluble extracellular and intracellular loops appear to be dispensable, and must be involved in the fine-tuning of transport regulation.

Indexed as

Amino Acid SequenceProtein FoldingSequence DeletionAnimalsCell MembraneEquilibrative Nucleoside Transporter 1HumansProtein Structure, SecondaryProtein TransportXenopus laevisEquilibrative Nucleoside Transporter 1SLC29A1 protein, human

Identifiers

PMID26406980
PMCPMC4583308
OpenAlexW2267333032

What OpenQuestion holds

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LicenceCC BY
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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.