Evidence map›Paper›PMID 2464998›Full record

ArticleThe Biochemical journal1988

Structural and functional variations in skeletal-muscle and scallop muscle actins.

H K Hue, J P Labbé, M C Harricane, J C Cavadore, Y Benyamin, C Roustan

Open access · bronzeAbstract readComparative Study
PubMed Full text at PMC Publisher
In one paragraph

Article in The Biochemical journal, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 43% 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

3 citing papers in PubMed, 13 citations in OpenAlex.

  1. Molecular genetics of actin function.The Biochemical journal · 1993
    Review
  2. Article
  3. 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.

H K HueCentre de Recherches de Biochimie Macromoléculaire (C.N.R.S.), Unité 249 (I.N.S.E.R.M.), Université de Montpellier I, France.
J P Labbé
M C Harricane
J C Cavadore
Y Benyamin
C Roustan
Université de Montpellier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Structural and functional properties in two striated-muscle actins, one from a vertebrate, the other from an invertebrate (scallop), were compared in relation to a smooth-muscle actin isoform (aortic actin). In spite of differences in the variable N-terminal region, the two striated-muscle isoactins showed, in contrast with aortic actin, a large structural homology revealed by proteinase-susceptibility and interaction with the myosin head. Thus the myosin head may bind to the two striated-muscle actins in constant parts of the 18-113 sequence. In contrast, antigenic reactivity of conformational epitopes of these actins strongly differentiated scallop actin from the two others. The behaviour of the scallop actin appears to be related to several amino acid substitutions located near or at functional domains such as monomer-monomer binding site, DNAase-I-dependent actin-actin binding site and actin-severing domain, which modified the polypeptide chain exposure.

Indexed as

ActinsAmino Acid SequenceAnimalsCa(2+) Mg(2+)-ATPaseEnzyme ActivationEpitopesMolluscaMusclesMyofibrilsMyosinsPeptide HydrolasesRabbitsActinsCa(2+) Mg(2+)-ATPaseEpitopesMyosinsPeptide Hydrolases

Identifiers

PMID2464998
PMCPMC1135494
OpenAlexW2400177034

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.