Evidence map›Paper›PMID 22312432›Full record

ArticlePloS one2012

Polyglutamine repeats are associated to specific sequence biases that are conserved among eukaryotes.

Matteo Ramazzotti, Elodie Monsellier, Choumouss Kamoun, Donatella Degl'Innocenti, Ronald Melki

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.5field-weighted citation impact, top 42% 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

17 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
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  7. Dilute phase oligomerization can oppose phase separation and modulate material properties of a ribonucleoprotein condensate.Proceedings of the National Academy of Sciences of the United States of America · 2022
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  12. The Information Content of Glutamine-Rich Sequences Define Protein Functional Characteristics.Proceedings of the IEEE. Institute of Electrical and Electronics Engineers · 2017
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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

5 authors at 3 institutions in 2 countries.

Matteo RamazzottiDipartimento di Scienze Biochimiche, Università degli Studi di Firenze, Florence, Italy. matteo.ramazzotti@unifi.it
Elodie Monsellier
Choumouss Kamoun
Donatella Degl'Innocenti
Ronald Melki
Laboratoire d'Enzymologie et Biochimie Structurales · FRUniversity of Florence · ITCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nine human neurodegenerative diseases, including Huntington's disease and several spinocerebellar ataxia, are associated to the aggregation of proteins comprising an extended tract of consecutive glutamine residues (polyQs) once it exceeds a certain length threshold. This event is believed to be the consequence of the expansion of polyCAG codons during the replication process. This is in apparent contradiction with the fact that many polyQs-containing proteins remain soluble and are encoded by invariant genes in a number of eukaryotes. The latter suggests that polyQs expansion and/or aggregation might be counter-selected through a genetic and/or protein context. To identify this context, we designed a software that scrutinize entire proteomes in search for imperfect polyQs. The nature of residues flanking the polyQs and that of residues other than Gln within polyQs (insertions) were assessed. We discovered strong amino acid residue biases robustly associated to polyQs in the 15 eukaryotic proteomes we examined, with an over-representation of Pro, Leu and His and an under-representation of Asp, Cys and Gly amino acid residues. These biases are conserved amongst unrelated proteins and are independent of specific functional classes. Our findings suggest that specific residues have been co-selected with polyQs during evolution. We discuss the possible selective pressures responsible of the observed biases.

Indexed as

Conserved SequenceEukaryotaPeptidesProteomicsRepetitive Sequences, Amino AcidAmino Acid SequenceAnimalsCodonDiseaseEvolution, MolecularGenome, ArchaealGenome, BacterialHumansSelection, GeneticCodonPeptidespolyglutamine

Identifiers

PMID22312432
PMCPMC3270027
OpenAlexW2048057867

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.