Evidence map›Paper›PMID 19429781›Full record

ArticleEukaryotic cell2009

Analysis of flagellar phosphoproteins from Chlamydomonas reinhardtii.

Jens Boesger, Volker Wagner, Wolfram Weisheit, Maria Mittag

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

31 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Review
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  4. mSphere · 2024
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  6. The methylome of motile cilia.Molecular biology of the cell · 2024
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  7. Article
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  9. Article
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  11. Article
  12. Alcohol-induced ciliary dysfunction targets the outer dynein arm.American journal of physiology. Lung cellular and molecular physiology · 2015
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Cryoelectron tomography reveals doublet-specific structures and unique interactions in the I1 dynein.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
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

4 authors at 1 institution in 1 country.

Jens BoesgerInstitut für Allgemeine Botanik und Pflanzenphysiologie, Friedrich-Schiller-Universität Jena, Am Planetarium 1, 07743 Jena, Germany.
Volker Wagner
Wolfram Weisheit
Maria Mittag
Friedrich Schiller University Jena · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cilia and flagella are cell organelles that are highly conserved throughout evolution. For many years, the green biflagellate alga Chlamydomonas reinhardtii has served as a model for examination of the structure and function of its flagella, which are similar to certain mammalian cilia. Proteome analysis revealed the presence of several kinases and protein phosphatases in these organelles. Reversible protein phosphorylation can control ciliary beating, motility, signaling, length, and assembly. Despite the importance of this posttranslational modification, the identities of many ciliary phosphoproteins and knowledge about their in vivo phosphorylation sites are still missing. Here we used immobilized metal affinity chromatography to enrich phosphopeptides from purified flagella and analyzed them by mass spectrometry. One hundred forty-one phosphorylated peptides were identified, belonging to 32 flagellar proteins. Thereby, 126 in vivo phosphorylation sites were determined. The flagellar phosphoproteome includes different structural and motor proteins, kinases, proteins with protein interaction domains, and many proteins whose functions are still unknown. In several cases, a dynamic phosphorylation pattern and clustering of phosphorylation sites were found, indicating a complex physiological status and specific control by reversible protein phosphorylation in the flagellum.

Indexed as

AnimalsCatalytic DomainCell MovementChlamydomonas reinhardtiiChromatography, AffinityConserved SequenceEvolution, MolecularFlagellaMass SpectrometryPeptidesPhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationPhosphotransferasesProtein Structure, TertiaryProteomePeptidesPhosphoprotein PhosphatasesPhosphoproteinsPhosphotransferasesProteome

Identifiers

PMID19429781
PMCPMC2708455
OpenAlexW2159900734

What OpenQuestion holds

Textmetadata
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.