Evidence map›Paper›PMID 31504783›Full record

ArticleNucleic acids research2019

Low complexity regions in the proteins of prokaryotes perform important functional roles and are highly conserved.

Chrysa Ntountoumi, Panayotis Vlastaridis, Dimitris Mossialos, Constantinos Stathopoulos, Ioannis Iliopoulos, Vasilios Promponas, Stephen G Oliver, Grigoris D Amoutzias

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.0field-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

41 citing papers in PubMed, 64 citations in OpenAlex.

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  15. Compensatory relationship between low-complexity regions and gene paralogy in the evolution of prokaryotes.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

8 authors at 5 institutions in 3 countries.

Chrysa NtountoumiBioinformatics Laboratory, Department of Biochemistry and Biotechnology, University of Thessaly, 41500, Greece.
Panayotis VlastaridisBioinformatics Laboratory, Department of Biochemistry and Biotechnology, University of Thessaly, 41500, Greece.
Dimitris MossialosMicrobial Biotechnology-Molecular Bacteriology-Virology Laboratory, Department of Biochemistry and Biotechnology, University of Thessaly, 41500, Greece.
Constantinos StathopoulosDepartment of Biochemistry, School of Medicine, University of Patras, 26504, Greece.
Ioannis IliopoulosDepartment of Medicine, University of Crete, Heraklion 71003, Greece.
Vasilios PromponasBioinformatics Research Laboratory, Department of Biological Sciences, New Campus, University of Cyprus, PO Box 20537, CY-1678 Nicosia, Cyprus.
Stephen G OliverCambridge Systems Biology Centre & Department of Biochemistry, University of Cambridge, CB2 1GA, UK.
Grigoris D AmoutziasBioinformatics Laboratory, Department of Biochemistry and Biotechnology, University of Thessaly, 41500, Greece.
University of Thessaly · GRUniversity of Cambridge · GBUniversity of Crete · GRUniversity of Cyprus · CYUniversity of Patras · GR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We provide the first high-throughput analysis of the properties and functional role of Low Complexity Regions (LCRs) in more than 1500 prokaryotic and phage proteomes. We observe that, contrary to a widespread belief based on older and sparse data, LCRs actually have a significant, persistent and highly conserved presence and role in many and diverse prokaryotes. Their specific amino acid content is linked to proteins with certain molecular functions, such as the binding of RNA, DNA, metal-ions and polysaccharides. In addition, LCRs have been repeatedly identified in very ancient, and usually highly expressed proteins of the translation machinery. At last, based on the amino acid content enriched in certain categories, we have developed a neural network web server to identify LCRs and accurately predict whether they can bind nucleic acids, metal-ions or are involved in chaperone functions. An evaluation of the tool showed that it is highly accurate for eukaryotic proteins as well.

Indexed as

Evolution, MolecularAmino AcidsDNAEukaryotic CellsHigh-Throughput Screening AssaysProkaryotic CellsProtein DomainsProteinsProteomeRNASequence AlignmentAmino AcidsDNAProteinsProteomeRNA

Identifiers

PMID31504783
PMCPMC6821194
OpenAlexW2971718802

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.