Evidence map›Paper›PMID 8694763›Full record

ArticleThe Biochemical journal1996

The variable subunit associated with protein phosphatase 2A0 defines a novel multimember family of regulatory subunits.

S Zolnierowicz, C Van Hoof, N Andjelković, P Cron, I Stevens, W Merlevede, J Goris, B A Hemmings

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.8field-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

23 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
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  4. Protein kinase A activates protein phosphatase 2A by phosphorylation of the B56delta subunit.Proceedings of the National Academy of Sciences of the United States of America · 2007
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  11. Amplification of dopaminergic signaling by a positive feedback loop.Proceedings of the National Academy of Sciences of the United States of America · 2000
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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

8 authors at 2 institutions in 2 countries.

S ZolnierowiczFriedrich Miescher-Institut, Basel, Switzerland.
C Van Hoof
N Andjelković
P Cron
I Stevens
W Merlevede
J Goris
B A Hemmings
KU Leuven · BEFriedrich Miescher Institute · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two protein phosphatase 2A (PP2A) holoenzymes were isolated from rabbit skeletal muscle containing, in addition to the catalytic and PR65 regulatory subunits, proteins of apparent molecular masses of 61 and 56 kDa respectively. Both holoenzymes displayed low basal phosphorylase phosphatase activity, which could be stimulated by protamine to an extent similar to that of previously characterized PP2A holoenzymes. Protein micro-sequencing of tryptic peptides derived from the 61 kDa protein, termed PR61, yielded 117 residues of amino acid sequence. Molecular cloning by enrichment of specific mRNAs, followed by reverse transcription-PCR and cDNA library screening, revealed that this protein exists in multiple isoforms encoded by at least three genes, one of which gives rise to several splicing variants. Comparisons of these sequences with the available databases identified one more human gene and predicted another based on a rabbit cDNA-derived sequence, thus bringing the number of genes encoding PR61 family members to five. Peptide sequences derived from PR61 corresponded to the deduced amino acid sequences of either alpha or beta isoforms, indicating that the purified PP2A preparation was a mixture of at least two trimers. In contrast, the 56 kDa subunit (termed PR56) seems to correspond to the epsilon isoform of PR61. Several regulatory subunits of PP2A belonging to the PR61 family contain consensus sequences for nuclear localization and might therefore target PP2A to nuclear substrates.

Indexed as

Alternative SplicingAmino Acid SequenceAnimalsBase SequenceCloning, MolecularEnzyme ActivationGene Expression Regulation, EnzymologicIsoenzymesMolecular Sequence DataMolecular WeightMultigene FamilyMuscle, SkeletalPeptide FragmentsPhosphoprotein PhosphatasesPolymerase Chain ReactionProtein ConformationIsoenzymesPeptide FragmentsPhosphoprotein PhosphatasesProtein Phosphatase 2

Identifiers

PMID8694763
PMCPMC1217462
OpenAlexW2302077191

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.