Evidence map›Paper›PMID 30418564›Full record

ArticleGigaScience2018

NAT/NCS2-hound: a webserver for the detection and evolutionary classification of prokaryotic and eukaryotic nucleobase-cation symporters of the NAT/NCS2 family.

A Chaliotis, P Vlastaridis, C Ntountoumi, M Botou, V Yalelis, P Lazou, E Tatsaki, D Mossialos, S Frillingos, G D Amoutzias

Open access · goldAbstract read
In one paragraph

Article in GigaScience, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

3 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. AInternational journal of molecular sciences · 2022
    Article
  3. 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

10 authors at 2 institutions in 1 country.

A ChaliotisBioinformatics Laboratory, Department of Biochemistry and Biotechnology, University of Thessaly, Larisa, 41500, Greece.
P VlastaridisBioinformatics Laboratory, Department of Biochemistry and Biotechnology, University of Thessaly, Larisa, 41500, Greece.
C NtountoumiBioinformatics Laboratory, Department of Biochemistry and Biotechnology, University of Thessaly, Larisa, 41500, Greece.
M BotouLaboratory of Biological Chemistry, Department of Medicine, University of Ioannina, Ioannina, 45110, Greece.
V YalelisLaboratory of Biological Chemistry, Department of Medicine, University of Ioannina, Ioannina, 45110, Greece.
P LazouLaboratory of Biological Chemistry, Department of Medicine, University of Ioannina, Ioannina, 45110, Greece.
E TatsakiLaboratory of Biological Chemistry, Department of Medicine, University of Ioannina, Ioannina, 45110, Greece.
D MossialosMolecular Bacteriology Laboratory, Department of Biochemistry and Biotechnology, University of Thessaly, Larisa, 41500, Greece.
S FrillingosLaboratory of Biological Chemistry, Department of Medicine, University of Ioannina, Ioannina, 45110, Greece.
G D AmoutziasBioinformatics Laboratory, Department of Biochemistry and Biotechnology, University of Thessaly, Larisa, 41500, Greece.
University of Ioannina · GRUniversity of Thessaly · GR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nucleobase transporters are important for supplying the cell with purines and/or pyrimidines, for controlling the intracellular pool of nucleotides, and for obtaining exogenous nitrogen/carbon sources for metabolism. Nucleobase transporters are also evaluated as potential targets for antimicrobial therapies, since several pathogenic microorganisms rely on purine/pyrimidine salvage from their hosts. The majority of known nucleobase transporters belong to the evolutionarily conserved and ubiquitous nucleobase-ascorbate transporter/nucleobase-cation symporter-2 (NAT/NCS2) protein family. Based on a large-scale phylogenetic analysis that we performed on thousands of prokaryotic proteomes, we developed a webserver that can detect and distinguish this family of transporters from other homologous families that recognize different substrates. We can further categorize these transporters to certain evolutionary groups with distinct substrate preferences. The webserver scans whole proteomes and graphically displays which proteins are identified as NAT/NCS2, to which evolutionary groups and subgroups they belong to, and which conserved motifs they have. For key subgroups and motifs, the server displays annotated information from published crystal-structures and mutational studies pointing to key functional amino acids that may help experts assess the transport capability of the target sequences. The server is 100% accurate in detecting NAT/NCS2 family members. We also used the server to analyze 9,109 prokaryotic proteomes and identified Clostridia, Bacilli, β- and γ-Proteobacteria, Actinobacteria, and Fusobacteria as the taxa with the largest number of NAT/NCS2 transporters per proteome. An analysis of 120 representative eukaryotic proteomes also demonstrates the server's capability of correctly analyzing this major lineage, with plants emerging as the group with the highest number of NAT/NCS2 members per proteome.

Indexed as

User-Computer InterfaceArchaeaArchaeal ProteinsBacteriaBacterial ProteinsBiological EvolutionCluster AnalysisDatabases, FactualMarkov ChainsPlant ProteinsPlantsProteomeSymportersArchaeal ProteinsBacterial ProteinsPlant ProteinsProteomeSymporters

Identifiers

PMID30418564
PMCPMC6308229
OpenAlexW2949467861

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.