Evidence map›Paper›PMID 28385889›Full record

ArticleThe Journal of biological chemistry2017

Substituted cysteine accessibility method (SCAM) analysis of the transport domain of human concentrative nucleoside transporter 3 (hCNT3) and other family members reveals features of structural and functional importance.

Ras Mulinta, Sylvia Y M Yao, Amy M L Ng, Carol E Cass, James D Young

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

7 citing papers in PubMed, 13 citations in OpenAlex.

  1. Solvent accessibility changes in a NaThe Journal of biological chemistry · 2020
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Who Is Who in Adenosine Transport.Frontiers in pharmacology · 2018
    Review
  7. 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

5 authors at 1 institution in 1 country.

Ras MulintaFrom the Membrane Protein Disease Research Group, Departments of Physiology and.
Sylvia Y M YaoFrom the Membrane Protein Disease Research Group, Departments of Physiology and.
Amy M L NgFrom the Membrane Protein Disease Research Group, Departments of Physiology and.
Carol E CassOncology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada and.
James D YoungFrom the Membrane Protein Disease Research Group, Departments of Physiology and james.young@ualberta.ca.
University of Alberta · CA

Funding

Wellcome Trust
6 · The paper itself

Abstract

The human SLC28 family of concentrative nucleoside transporter (CNT) proteins has three members: hCNT1, hCNT2, and hCNT3. Na

Indexed as

Amino Acid SubstitutionAnimalsEscherichia coliEscherichia coli ProteinsHumansMembrane Transport ProteinsMutation, MissenseProtein DomainsProtein Structure, SecondaryStructural Homology, ProteinStructure-Activity RelationshipXenopus laeviscif nucleoside transporterEscherichia coli ProteinsMembrane Transport ProteinsNupC protein, E colihuman concentrative nucleoside transporter 3 (hCNT3)membrane proteinmembrane transportnucleoside/nucleotide transportnucleoside transportnucleoside transporterrecombinant protein expressionsubstituted cysteine accessibility (SCAM) analysistransporter

Identifiers

PMID28385889
PMCPMC5465479
OpenAlexW2604938190

What OpenQuestion 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 OpenQuestion graph.