Evidence map›Paper›PMID 25043943›Full record

ArticleProteins2014

Expansion of the APC superfamily of secondary carriers.

Ake Vastermark, Simon Wollwage, Michael E Houle, Rita Rio, Milton H Saier

Open access · greenAbstract read
In one paragraph

Article in Proteins, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

52 citing papers in PubMed, 96 citations in OpenAlex.

  1. Review
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  12. Review
  13. Nramp: Deprive and conquer?Frontiers in cell and developmental biology · 2022
    Article
  14. Wheat potassium transporter TaHAK13 mediates KFrontiers in plant science · 2022
    Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Microbial methionine transporters and biotechnological applications.Applied microbiology and biotechnology · 2021
    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

5 authors at 3 institutions in 2 countries.

Ake VastermarkDepartment of Molecular Biology, University of California at San Diego, La Jolla, California, 92093-0116.
Simon Wollwage
Michael E Houle
Rita Rio
Milton H Saier
National Institute of Informatics · JPUniversity of California, San Diego · USWest Virginia University · US

Funding

The Transporter Classification Database (TCDB)R01GM077402 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SAIER, MILTON H. · 2006 to 2021
$4.7M
NIGMS NIH HHS GM077402A1NIGMS NIH HHS R01 GM077402
6 · The paper itself

Abstract

The amino acid-polyamine-organoCation (APC) superfamily is the second largest superfamily of secondary carriers currently known. In this study, we establish homology between previously recognized APC superfamily members and proteins of seven new families. These families include the PAAP (Putative Amino Acid Permease), LIVCS (Branched Chain Amino Acid:Cation Symporter), NRAMP (Natural Resistance-Associated Macrophage Protein), CstA (Carbon starvation A protein), KUP (K⁺ Uptake Permease), BenE (Benzoate:H⁺ Virginia Symporter), and AE (Anion Exchanger). The topology of the well-characterized human Anion Exchanger 1 (AE1) conforms to a UraA-like topology of 14 TMSs (12 α-helical TMSs and 2 mixed coil/helical TMSs). All functionally characterized members of the APC superfamily use cation symport for substrate accumulation except for some members of the AE family which frequently use anion:anion exchange. We show how the different topologies fit into the framework of the common LeuT-like fold, defined earlier (Proteins. 2014 Feb;82(2):336-46), and determine that some of the new members contain previously undocumented topological variations. All new entries contain the two 5 or 7 TMS APC superfamily repeat units, sometimes with extra TMSs at the ends, the variations being greatest within the CstA family. New, functionally characterized members transport amino acids, peptides, and inorganic anions or cations. Except for anions, these are typical substrates of established APC superfamily members. Active site TMSs are rich in glycyl residues in variable but conserved constellations. This work expands the APC superfamily and our understanding of its topological variations.

Indexed as

Models, MolecularAmino Acid MotifsAmino Acid Transport SystemsAnimalsAntiportersBiological TransportCation Transport ProteinsCluster AnalysisComputational BiologyDatabases, ProteinEscherichia coli ProteinsHumansInternetNatural Resistance-associated Macrophage Protein 1Organic Cation Transport ProteinsPhylogenyAmino Acid Transport SystemsAntiportersCation Transport ProteinscstA protein, E coliEscherichia coli ProteinsNatural Resistance-associated Macrophage Protein 1Organic Cation Transport ProteinsProtein IsoformsTrans-Activatorsamino acid-polyamine-organoCation (APC) superfamilyanion exchanger 1carbon starvation A proteinsuperfamily treetransporter classification database

Identifiers

PMID25043943
PMCPMC4177346
OpenAlexW1596955265

What OpenQuestion holds

Textmetadata
LicenceTDM
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.