Evidence map›Paper›PMID 30698641›Full record

ReviewBriefings in bioinformatics2020

Disentangling the complexity of low complexity proteins.

Pablo Mier, Lisanna Paladin, Stella Tamana, Sophia Petrosian, Borbála Hajdu-Soltész, Annika Urbanek, Aleksandra Gruca, Dariusz Plewczynski, Marcin Grynberg, Pau Bernadó and 8 more

Abstract readReview
In one paragraph

Review in Briefings in bioinformatics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
–field-weighted citation impact
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

64 citing papers in PubMed.

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  12. The C-terminal end of PLIN1 displays structural disorder.Biochemistry and biophysics reports · 2025
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4 more citing papers are in PubMed but not listed here.

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

18 authors.

Pablo MierInstitute of Organismic and Molecular Evolution, Johannes Gutenberg University of Mainz, Mainz, Germany.
Lisanna PaladinDepartment of Biomedical Science, University of Padova, Padova, Italy.
Stella TamanaBioinformatics Research Laboratory, Department of Biological Sciences, University of Cyprus, Nicosia, Cyprus.
Sophia PetrosianBiological Computation and Process Laboratory, Chemical Process & Energy Resources Institute, Centre for Research & Technology Hellas, Thessalonica, Greece.
Borbála Hajdu-SoltészMTA-ELTE Lendület Bioinformatics Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
Annika UrbanekCentre de Biochimie Structurale, INSERM, CNRS, Université de Montpellier, Montpellier, France.
Aleksandra GrucaInstitute of Informatics, Silesian University of Technology, Gliwice, Poland.
Dariusz PlewczynskiCenter of New Technologies, University of Warsaw, Warsaw, Poland.
Marcin GrynbergInstitute of Biochemistry and Biophysics, Warsaw, Poland.
Pau BernadóCentre de Biochimie Structurale, INSERM, CNRS, Université de Montpellier, Montpellier, France.
Zoltán GáspáriFaculty of Information Technology and Bionics, Pázmány Péter Catholic University, Budapest, Hungary.
Christos A OuzounisBiological Computation and Process Laboratory, Chemical Process & Energy Resources Institute, Centre for Research & Technology Hellas, Thessalonica, Greece.
Vasilis J PromponasBioinformatics Research Laboratory, Department of Biological Sciences, University of Cyprus, Nicosia, Cyprus.
Andrey V KajavaCentre de Recherche en Biologie Cellulaire de Montpellier, CNRS-UMR, Institut de Biologie Computationnelle, Universite de Montpellier, Montpellier, France.
John M HancockEarlham Institute, Norwich, UK.
Silvio C E TosattoDepartment of Biomedical Science, University of Padova, Padova, Italy.
Zsuzsanna DosztanyiMTA-ELTE Lendület Bioinformatics Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
Miguel A Andrade-NavarroInstitute of Organismic and Molecular Evolution, Johannes Gutenberg University of Mainz, Mainz, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There are multiple definitions for low complexity regions (LCRs) in protein sequences, with all of them broadly considering LCRs as regions with fewer amino acid types compared to an average composition. Following this view, LCRs can also be defined as regions showing composition bias. In this critical review, we focus on the definition of sequence complexity of LCRs and their connection with structure. We present statistics and methodological approaches that measure low complexity (LC) and related sequence properties. Composition bias is often associated with LC and disorder, but repeats, while compositionally biased, might also induce ordered structures. We illustrate this dichotomy, and more generally the overlaps between different properties related to LCRs, using examples. We argue that statistical measures alone cannot capture all structural aspects of LCRs and recommend the combined usage of a variety of predictive tools and measurements. While the methodologies available to study LCRs are already very advanced, we foresee that a more comprehensive annotation of sequences in the databases will enable the improvement of predictions and a better understanding of the evolution and the connection between structure and function of LCRs. This will require the use of standards for the generation and exchange of data describing all aspects of LCRs. SHORT ABSTRACT: There are multiple definitions for low complexity regions (LCRs) in protein sequences. In this critical review, we focus on the definition of sequence complexity of LCRs and their connection with structure. We present statistics and methodological approaches that measure low complexity (LC) and related sequence properties. Composition bias is often associated with LC and disorder, but repeats, while compositionally biased, might also induce ordered structures. We illustrate this dichotomy, plus overlaps between different properties related to LCRs, using examples.

Indexed as

AlgorithmsAmino Acid SequenceDatabases, ProteinEvolution, MolecularProtein ConformationProtein DomainsProteinsProteinscomposition biasdisorderlow complexity regionsstructure

Identifiers

PMID30698641
PMCPMC7299295

What OpenQuestion holds

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LicenceCC BY-NC
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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.