Evidence map›Paper›PMID 2482731›Full record

ArticleThe Biochemical journal1989

Antigenic probes locate binding sites for the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, aldolase and phosphofructokinase on the actin monomer in microfilaments.

C Méjean, F Pons, Y Benyamin, C Roustan

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.1field-weighted citation impact, top 21% 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

19 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
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  3. Molecular Composition of Vestibular Hair Bundles.Cold Spring Harbor perspectives in medicine · 2019
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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

4 authors at 3 institutions in 1 country.

C MéjeanUPR 8402 Centre de Recherches de Biochimie Macromoléculaire (CNRS), U249 INSERM, Université de Montpellier I, France.
F Pons
Y Benyamin
C Roustan
École Pratique des Hautes Études · FRCentre National de la Recherche Scientifique · FRUniversité de Montpellier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The topology of the interfaces between actin monomers in microfilaments and three glycolytic enzymes (glyceraldehyde-3-phosphate dehydrogenase, aldolase and phosphofructokinase) was investigated using several specific antibodies directed against precisely located sequences in actin. A major contact area for glyceraldehyde-3-phosphate dehydrogenase was characterized in a region near residue 103. This interaction altered, by long-range conformational changes, the reactivity of antigenic epitopes in the C-terminal part of actin. The interface between actin and aldolase appeared to involve a sequence around residue 299 in the C-terminal region of actin. The interaction of phosphofructokinase, in contrast, modified the reactivity of all antibodies tested. Finally, the phosphagen kinases arginine kinase and creatine kinase showed no interaction with the microfilament.

Indexed as

Actin CytoskeletonActinsAnimalsAntibodiesAntigen-Antibody ComplexBinding SitesChromatography, AffinityCytoskeletonEnzyme-Linked Immunosorbent AssayEpitopesFructose-Bisphosphate AldolaseGlyceraldehyde-3-Phosphate DehydrogenasesGlycolysisKineticsMusclesPhosphofructokinase-1ActinsAntibodiesAntigen-Antibody ComplexEpitopesFructose-Bisphosphate AldolaseGlyceraldehyde-3-Phosphate DehydrogenasesPhosphofructokinase-1

Identifiers

PMID2482731
PMCPMC1133639
OpenAlexW2404441818

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.