Evidence map›Paper›PMID 8970153›Full record

ArticleMolecular biology of the cell1996

Is outer arm dynein intermediate chain 1 multifunctional?

K Ogawa, H Takai, A Ogiwara, E Yokota, T Shimizu, K Inaba, H Mohri

Abstract read
In one paragraph

Article in Molecular biology of the cell, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

29 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Axonemal Dynein Arms.Cold Spring Harbor perspectives in biology · 2016
    Review
  7. Sperm dysfunction and ciliopathy.Reproductive medicine and biology · 2016
    Review
  8. Article
  9. Article
  10. Article
  11. Integrated control of axonemal dynein AAA(+) motors.Journal of structural biology · 2012
    Review
  12. Tubulin-dynein system in flagellar and ciliary movement.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2012
    Review
  13. A unified taxonomy for ciliary dyneins.Cytoskeleton (Hoboken, N.J.) · 2011
    Article
  14. Article
  15. Article
  16. Review
  17. A common variant in combination with a nonsense mutation in a member of the thioredoxin family causes primary ciliary dyskinesia.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  18. Article
  19. Article
  20. 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

7 authors at 1 institution in 1 country.

K OgawaNational Institute for Basic Biology, Okazaki, Japan.
H Takai
A Ogiwara
E Yokota
T Shimizu
K Inaba
H Mohri
National Institute for Basic Biology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The outer arm dynein of sea urchin sperm axoneme contains three intermediate chains (IC1, IC2, and IC3; M(r) 128,000, 98,000, and 74,000, respectively). IC2 and IC3 are members of the WD family; the WD motif is responsible for a protein-protein interaction. We describe here the molecular cloning of IC1. IC1 has a unique primary structure, the N-terminal part is homologous to the sequence of thioredoxin, the middle part consists of three repetitive sequences homologous to the sequence of nucleoside diphosphate kinase, and the C-terminal part contains a high proportion of negatively charged glutamic acid residues. Thus, IC1 is a novel dynein intermediate chain distinct from IC2 and IC3 and may be a multifunctional protein. The thioredoxin-related part of IC1 is more closely related to those of two redox-active Chlamydomonas light chains than thioredoxin. Antibodies were prepared against the N-terminal and middle domains of IC1 expressed as His-tagged proteins in bacteria. These antibodies cross-reacted with some dynein polypeptides (potential homologues of IC1) from distantly related species. We propose here that the three intermediate chains are the basic core units of sperm outer arm dynein because of their ubiquitous existence. The recombinant thioredoxin-related part of IC1 and outer arm dyneins from sea urchin and distantly related species were specifically bound to and eluted from a phenylarsine oxide affinity column with 2-mercaptoethanol, indicating that they contain vicinal dithiols competent to undergo reversible oxidation/reduction.

Indexed as

Amino Acid SequenceAnimalsBase SequenceDNA, ComplementaryDyneinsMaleMolecular Sequence DataNucleoside-Diphosphate KinaseOxidation-ReductionSea UrchinsSequence Homology, Amino AcidSulfhydryl CompoundsThioredoxinsDNA, ComplementaryDyneinsNucleoside-Diphosphate KinaseSulfhydryl CompoundsThioredoxins

Identifiers

PMID8970153
PMCPMC276038
OpenAlexW2043539013

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.