Evidence map›Paper›PMID 20385029›Full record

ArticleBMC systems biology2010

Low-complexity regions within protein sequences have position-dependent roles.

Alain Coletta, John W Pinney, David Y Weiss Solís, James Marsh, Steve R Pettifer, Teresa K Attwood

Abstract read
In one paragraph

Article in BMC systems biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.

0numbers the graph read from it
0cells of the map it votes in
102citing 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

102 citing papers in PubMed.

  1. Article
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  9. Biophysical characterization of high-confidence, small human proteins.bioRxiv : the preprint server for biology · 2024
    Article
  10. Diverse cytomegalovirus US11 antagonism and MHC-A evasion strategies reveal a tit-for-tat coevolutionary arms race in hominids.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Article
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  15. Identification and Functional Analysis ofInternational journal of molecular sciences · 2023
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review

42 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

6 authors.

Alain ColettaFaculty of Life Sciences, University of Manchester, Manchester M13 9PL, UK. alain.coletta@vub.ac.be
John W Pinney
David Y Weiss Solís
James Marsh
Steve R Pettifer
Teresa K Attwood

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundRegions of protein sequences with biased amino acid composition (so-called Low-Complexity Regions (LCRs)) are abundant in the protein universe. A number of studies have revealed that i) these regions show significant divergence across protein families; ii) the genetic mechanisms from which they arise lends them remarkable degrees of compositional plasticity. They have therefore proved difficult to compare using conventional sequence analysis techniques, and functions remain to be elucidated for most of them. Here we undertake a systematic investigation of LCRs in order to explore their possible functional significance, placed in the particular context of Protein-Protein Interaction (PPI) networks and Gene Ontology (GO)-term analysis.

resultsIn keeping with previous results, we found that LCR-containing proteins tend to have more binding partners across different PPI networks than proteins that have no LCRs. More specifically, our study suggests i) that LCRs are preferentially positioned towards the protein sequence extremities and, in contrast with centrally-located LCRs, such terminal LCRs show a correlation between their lengths and degrees of connectivity, and ii) that centrally-located LCRs are enriched with transcription-related GO terms, while terminal LCRs are enriched with translation and stress response-related terms.

conclusionsOur results suggest not only that LCRs may be involved in flexible binding associated with specific functions, but also that their positions within a sequence may be important in determining both their binding properties and their biological roles.

Indexed as

Protein Interaction MappingAlgorithmsAmino AcidsComputational BiologyFungal ProteinsGene Expression Regulation, FungalModels, BiologicalModels, GeneticModels, StatisticalProteinsSaccharomyces cerevisiaeSequence AlignmentSequence Analysis, ProteinAmino AcidsFungal ProteinsProteins

Identifiers

PMID20385029
PMCPMC2873317

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Registered trials

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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.