Evidence map›Paper›PMID 7579689›Full record

ArticleMolecular biology of the cell1995

The light chain p28 associates with a subset of inner dynein arm heavy chains in Chlamydomonas axonemes.

M LeDizet, G Piperno

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

64 citing papers in PubMed, 144 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Force-Generating Mechanism of Axonemal Dynein in Solo and Ensemble.International journal of molecular sciences · 2020
    Review
  11. Article
  12. Cells · 2018
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Ciliary Motility: Regulation of Axonemal Dynein Motors.Cold Spring Harbor perspectives in biology · 2017
    Review
  19. Posttranslational Modifications of Tubulin and Cilia.Cold Spring Harbor perspectives in biology · 2017
    Review
  20. Review

4 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

2 authors at 1 institution in 1 country.

M LeDizetDepartment of Cell Biology and Anatomy, Mount Sinai School of Medicine, New York, New York 10029, USA.
G Piperno
Icahn School of Medicine at Mount Sinai · US

Funding

ZIPRASIDONE (GEODON) AUGMENTATION IN SEROTONIN REUPTAKE INHIBITOR-RESISTANT OBM01RR000071 · NCRR · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI NEWCORN, JEFFREY H · 1985 to 2009
$41.5M
MOLECULAR INTERACTIONS IN MOVING AXONEMESR01GM044467 · NIGMS · ROCKEFELLER UNIVERSITY · PI PIPERNO, GIANNI · 1990 to 2004
$1.4M
NCRR NIH HHS 5 MO1 RR00071NIGMS NIH HHS GM-44467
6 · The paper itself

Abstract

We show here that I2 and I3 inner dynein arm heavy chains of Chlamydomonas axonemes are resolved into two classes: one class associated with the protein p28 and the other associated with the protein caltractin/centrin. We have determined the nucleotide sequence of the gene encoding p28, a light chain that, together with actin and caltractin/centrin, is associated with inner dynein arms I2 and I3 of Chlamydomonas axonemes. p28 is a novel protein with affinity for a subset of the inner dynein arm heavy chains, but with no apparent significant homologies to tubulin- or actin-binding proteins. An antiserum specific for p28 showed that p28 is present along the entire axoneme. The same antiserum coimmunoprecipitated p28, actin, and dynein heavy chains 2' and 2. In contrast, an anti-caltractin/centrin antiserum coimmunoprecipitated caltractin/centrin, actin, and the heavy chains 2, 3, and 3'. It is likely that the dynein heavy chain 2 associated with p28, referred to as 2A, is a different polypeptide from dynein heavy chain 2 bound to caltractin/centrin, referred to as 2B. The complex formed by heavy chain 2B, actin, and caltractin/centrin is preferentially extracted by exposure to Nonidet P-40 and is missing in mutants lacking components 1 and 2 of the dynein regulatory complex.

Indexed as

Chromosomal Proteins, Non-HistoneGenes, ProtozoanAmino Acid SequenceAnimalsBacterial ProteinsBase SequenceBlotting, SouthernBlotting, WesternCalcium-Binding ProteinsCell MovementChlamydomonasCloning, MolecularCodonDNA, ProtozoanDyneinsElectrophoresis, Polyacrylamide GelBacterial ProteinsCalcium-Binding ProteinscaltractinChromosomal Proteins, Non-HistoneCodonDNA, ProtozoanDyneinslight chain protein p28, Chlamydomonas

Identifiers

PMID7579689
PMCPMC301230
OpenAlexW2098782815

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.