Evidence map›Paper›PMID 29717210›Full record

ArticleScientific reports2018

Exploring intrinsically disordered proteins in Chlamydomonas reinhardtii.

Yizhi Zhang, Hélène Launay, Antoine Schramm, Régine Lebrun, Brigitte Gontero

Erratum issuedAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Yizhi ZhangAix Marseille Univ, CNRS, BIP, UMR 7281, IMM, 31 Chemin J. Aiguier, 13402, Marseille, Cedex 20, France.
Hélène LaunayAix Marseille Univ, CNRS, BIP, UMR 7281, IMM, 31 Chemin J. Aiguier, 13402, Marseille, Cedex 20, France.
Antoine SchrammAix Marseille Univ, CNRS, AFMB, UMR 7257, Marseille, France.
Régine LebrunPlate-forme Protéomique, Marseille Protéomique (MaP), IBiSA labeled, IMM, FR 3479, CNRS, B.P. 71, 13402, Marseille, Cedex 20, France.
Brigitte GonteroAix Marseille Univ, CNRS, BIP, UMR 7281, IMM, 31 Chemin J. Aiguier, 13402, Marseille, Cedex 20, France. bmeunier@imm.cnrs.fr.ORCID 0000-0003-1731-712X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The content of intrinsically disordered protein (IDP) is related to organism complexity, evolution, and regulation. In the Plantae, despite their high complexity, experimental investigation of IDP content is lacking. We identified by mass spectrometry 682 heat-resistant proteins from the green alga, Chlamydomonas reinhardtii. Using a phosphoproteome database, we found that 331 of these proteins are targets of phosphorylation. We analyzed the flexibility propensity of the heat-resistant proteins and their specific features as well as those of predicted IDPs from the same organism. Their mean percentage of disorder was about 20%. Most of the IDPs (~70%) were addressed to other compartments than mitochondrion and chloroplast. Their amino acid composition was biased compared to other classic IDPs. Their molecular functions were diverse; the predominant ones were nucleic acid binding and unfolded protein binding and the less abundant one was catalytic activity. The most represented proteins were ribosomal proteins, proteins associated to flagella, chaperones and histones. We also found CP12, the only experimental IDP from C. reinhardtii that is referenced in disordered protein database. This is the first experimental investigation of IDPs in C. reinhardtii that also combines in silico analysis.

Indexed as

Algal ProteinsChlamydomonas reinhardtiiFlagellaGene ExpressionGene OntologyHistonesHot TemperatureIntrinsically Disordered ProteinsMolecular ChaperonesMolecular Sequence AnnotationPhosphoproteinsPhosphorylationProtein StabilityRibosomal ProteinsAlgal ProteinsHistonesIntrinsically Disordered ProteinsMolecular ChaperonesPhosphoproteinsRibosomal Proteins

Identifiers

PMID29717210
PMCPMC5931566

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.