Evidence map›Paper›PMID 22407322›Full record

ArticleNature2012

Crystal structure of a concentrative nucleoside transporter from Vibrio cholerae at 2.4 Å.

Zachary Lee Johnson, Cheom-Gil Cheong, Seok-Yong Lee

Abstract read
In one paragraph

Article in Nature, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
6.2field-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

58 citing papers in PubMed, 122 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Elucidation of the Gemcitabine Transporters ofInternational journal of molecular sciences · 2024
    Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Ftsh Sensitizes Methicillin-ResistantAntibiotics (Basel, Switzerland) · 2021
    Article
  15. Review
  16. The Structure and Mechanism of Drug Transporters.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  17. Article
  18. Article
  19. Elevator-type mechanisms of membrane transport.Biochemical Society transactions · 2020
    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

3 authors at 2 institutions in 1 country.

Zachary Lee JohnsonDepartment of Biochemistry and Ion Channel Research Unit, Duke University Medical Center, 2 Genome Court, Durham, North Carolina 27710, USA.
Cheom-Gil Cheong
Seok-Yong Lee
Duke Medical Center · USDuke University · US

Funding

Pharmacology and biophysics of the voltage-gated sodium channel Nav1.7: a therapeDP2OD008380 · OD · DUKE UNIVERSITY · PI LEE, SEOK-YONG · 2011 to 2011
$2.4M
Structure and Function of Concentrative Nucleoside TransportersR01GM100984 · NIGMS · DUKE UNIVERSITY · PI LEE, SEOK-YONG · 2013 to 2016
$1.2M
NIGMS NIH HHS R01 GM100984NIH HHS 1 DP2 OD008380-01NIH HHS DP2 OD008380
6 · The paper itself

Abstract

Nucleosides are required for DNA and RNA synthesis, and the nucleoside adenosine has a function in a variety of signalling processes. Transport of nucleosides across cell membranes provides the major source of nucleosides in many cell types and is also responsible for the termination of adenosine signalling. As a result of their hydrophilic nature, nucleosides require a specialized class of integral membrane proteins, known as nucleoside transporters (NTs), for specific transport across cell membranes. In addition to nucleosides, NTs are important determinants for the transport of nucleoside-derived drugs across cell membranes. A wide range of nucleoside-derived drugs, including anticancer drugs (such as Ara-C and gemcitabine) and antiviral drugs (such as zidovudine and ribavirin), have been shown to depend, at least in part, on NTs for transport across cell membranes. Concentrative nucleoside transporters, members of the solute carrier transporter superfamily SLC28, use an ion gradient in the active transport of both nucleosides and nucleoside-derived drugs against their chemical gradients. The structural basis for selective ion-coupled nucleoside transport by concentrative nucleoside transporters is unknown. Here we present the crystal structure of a concentrative nucleoside transporter from Vibrio cholerae in complex with uridine at 2.4 Å. Our functional data show that, like its human orthologues, the transporter uses a sodium-ion gradient for nucleoside transport. The structure reveals the overall architecture of this class of transporter, unravels the molecular determinants for nucleoside and sodium binding, and provides a framework for understanding the mechanism of nucleoside and nucleoside drug transport across cell membranes.

Indexed as

Binding SitesBiological TransportCrystallography, X-RayHumansModels, MolecularNucleosidesNucleoside Transport ProteinsProtein ConformationProtein FoldingSodiumUridineVibrio choleraeNucleosidesNucleoside Transport ProteinsSodiumUridine

Identifiers

PMID22407322
PMCPMC3310960
OpenAlexW1990613087

What OpenQuestion holds

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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.