Evidence map›Paper›PMID 9228291›Full record

ReviewMolecular biology reports1997

Proteasome (prosome) associated endonuclease activity.

F Petit, A S Jarrousse, G Boissonnet, M H Dadet, J Buri, Y Briand, H P Schmid

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular biology reports, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

6 citing papers in PubMed, 27 citations in OpenAlex.

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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

7 authors at 2 institutions in 2 countries.

F PetitUniversité Blaise Pascal, Clermont-Ferrand II, Aubière, France.
A S Jarrousse
G Boissonnet
M H Dadet
J Buri
Y Briand
H P Schmid
Université Clermont Auvergne · FRInstitut National de la Recherche Agronomique · MA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The 20S proteasome (prosome) is a highly organized multiprotein complex with approximate molecular weight of about 700 kDa. Whilst the role of the proteasome in the processing and turnover of cellular proteins is becoming clearer, its relationship with RNA remains still obscure. Here we focus on the nature and function of proteasome associated endonuclease activity. Thus the involvement of a proteasome alpha-type subunit in RNA-degradation, the catalytic requirements, the interaction of proteasomes with their RNA-substrate and the identification of a well defined cleavage site in the 3'UTR of short-lived cellular mRNAs will be described in detail. All data indicate that proteasomes associated endonuclease activity could be involved in post-transcriptional gene control at the level of translation.

Indexed as

AnimalsBase SequenceCysteine EndopeptidasesEndoribonucleasesHumansMolecular Sequence DataMultienzyme ComplexesProteasome Endopeptidase ComplexRNA, MessengerRNA, ViralCysteine EndopeptidasesEndoribonucleasesMultienzyme ComplexesProteasome Endopeptidase ComplexRNA, MessengerRNA, Viral

Identifiers

PMID9228291
OpenAlexW196456871

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.