Evidence map›Paper›PMID 3446177›Full record

ArticleThe Biochemical journal1987

Anti-actin antibodies. An immunological approach to the myosin-actin and the tropomyosin-actin interfaces.

C Mejean, M Boyer, J P Labbé, L Marlier, Y Benyamin, C Roustan

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.2field-weighted citation impact, top 10% 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

13 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Charge-reversion mutagenesis of Dictyostelium actin to map the surface recognized by myosin during ATP-driven sliding motion.Proceedings of the National Academy of Sciences of the United States of America · 1993
    Article
  4. Article
  5. The interaction of caldesmon with the COOH terminus of actin.The Journal of biological chemistry · 1991
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Functional sequences of the myosin head.Journal of muscle research and cell motility · 1989
    Review
  12. Article
  13. 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

6 authors at 1 institution in 1 country.

C MejeanCentre de Recherches de Biochimie Macromoléculaire (CNRS), U 249 (INSERM), Université de Montpellier I, France.
M Boyer
J P Labbé
L Marlier
Y Benyamin
C Roustan
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The topography of the rigor complex between subfragment-1 (S-1) of myosin and actin was investigated by using several specific antibodies directed to well-located sequences in actin. A major contact area for S-1 was characterized in the hydrophilic 18-28 constant sequence, and the variable 1-7 sequence was only found to be in close proximity to the interface. The C-terminal extremity of actin situated around Cys-374 appeared to be included in a region close to the S-1 heavy chain and the N-terminal part of actin. The interaction between tropomyosin and actin was also studied. Neither of the terminal parts of actin were involved in this interaction. Thus, the regions involved in the interactions of S-1 and tropomyosin with actin do not overlap.

Indexed as

AntibodiesActinsAmino Acid SequenceAnimalsBinding SitesEnzyme-Linked Immunosorbent AssayMacromolecular SubstancesMyosinsPeptide FragmentsRabbitsTropomyosinActinsAntibodiesMacromolecular SubstancesMyosinsPeptide FragmentsTropomyosin

Identifiers

PMID3446177
PMCPMC1148034
OpenAlexW11834068

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.