Evidence map›Paper›PMID 11907279›Full record

ArticleMolecular biology of the cell2002

The outer dynein arm-docking complex: composition and characterization of a subunit (oda1) necessary for outer arm assembly.

Saeko Takada, Curtis G Wilkerson, Ken-ichi Wakabayashi, Ritsu Kamiya, George B Witman

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

66 citing papers in PubMed, 128 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. International journal of molecular sciences · 2023
    Review
  8. Article
  9. Article
  10. Article
  11. Expression of a Truncated Form ofInternational journal of molecular sciences · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Force-Generating Mechanism of Axonemal Dynein in Solo and Ensemble.International journal of molecular sciences · 2020
    Review
  16. Asymmetries in the cilia ofPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020
    Review
  17. Article
  18. Review
  19. Article
  20. Review

6 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

5 authors at 3 institutions in 2 countries.

Saeko TakadaDepartment of Cell Biology, University of Massachusetts Medical School, Worcester, Massachusetts 01655, USA.
Curtis G Wilkerson
Ken-ichi Wakabayashi
Ritsu Kamiya
George B Witman
National Institute for Basic Biology · JPUniversity of Massachusetts Chan Medical School · USTokyo University of Science · JP

Funding

Flagellar Motility and AssemlbyR37GM030626 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI WITMAN, GEORGE B · 2007 to 2016
$6.3M
MOLECULAR MECHANISM OF FLAGELLAR MOTILITYR01GM030626 · NIGMS · WORCESTER FOUNDATION FOR BIOMEDICAL RES · PI WITMAN, GEORGE B · 1985 to 2006
$3.0M
NIGMS NIH HHS GM-30626NIGMS NIH HHS R01 GM030626NIGMS NIH HHS R37 GM030626
6 · The paper itself

Abstract

To learn more about how dyneins are targeted to specific sites in the flagellum, we have investigated a factor necessary for binding of outer arm dynein to the axonemal microtubules of Chlamydomonas. This factor, termed the outer dynein arm-docking complex (ODA-DC), previously was shown to be missing from axonemes of the outer dynein armless mutants oda1 and oda3. We have now partially purified the ODA-DC, determined that it contains equimolar amounts of M(r) approximately 105,000 and approximately 70,000 proteins plus a third protein of M(r) approximately 25,000, and found that it is associated with the isolated outer arm in a 1:1 molar ratio. We have cloned a full-length cDNA encoding the M(r) approximately 70,000 protein; the sequence predicts a 62.5-kDa protein with potential homologs in higher ciliated organisms, including humans. Sequencing of corresponding cDNA from strain oda1 revealed it has a mutation resulting in a stop codon just downstream of the initiator ATG; thus, it is unable to make the full-length M(r) approximately 70,000 protein. These results demonstrate that the ODA1 gene encodes the M(r) approximately 70,000 protein, and that the protein is essential for assembly of the ODA-DC and the outer dynein arm onto the doublet microtubule.

Indexed as

Algal ProteinsAmino Acid SequenceAnimalsBase SequenceChlamydomonasDyneinsFlagellaHumansMacromolecular SubstancesModels, MolecularMolecular Sequence DataMolecular WeightPeptidesProtein Structure, SecondaryProtein SubunitsProtozoan ProteinsAlgal ProteinsDyneinsMacromolecular SubstancesPeptidesProtein SubunitsProtozoan Proteins

Identifiers

PMID11907279
PMCPMC99616
OpenAlexW2136485352

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.