Evidence map›Paper›PMID 30992367›Full record

ArticleThe Journal of biological chemistry2019

Polyadenylate-binding protein-interacting proteins PAIP1 and PAIP2 affect translation termination.

Alexandr Ivanov, Ekaterina Shuvalova, Tatiana Egorova, Alexey Shuvalov, Elizaveta Sokolova, Nikita Bizyaev, Ivan Shatsky, Ilya Terenin, Elena Alkalaeva

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

20 citing papers in PubMed, 41 citations in OpenAlex.

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  18. Tissue-specific dynamic codon redefinition inProceedings of the National Academy of Sciences of the United States of America · 2021
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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

9 authors at 3 institutions in 2 countries.

Alexandr IvanovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow 119991, Russia; Faculty of Bioengineering and Bioinformatics, M. V. Lomonosov Moscow State University, Moscow 119234, Russia.
Ekaterina ShuvalovaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow 119991, Russia.
Tatiana EgorovaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow 119991, Russia.
Alexey ShuvalovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow 119991, Russia.
Elizaveta SokolovaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow 119991, Russia.
Nikita BizyaevEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow 119991, Russia.
Ivan ShatskyBelozersky Institute of Physico-Chemical Biology, M. V. Lomonosov Moscow State University, Moscow 119234, Russia.
Ilya TereninBelozersky Institute of Physico-Chemical Biology, M. V. Lomonosov Moscow State University, Moscow 119234, Russia; Sechenov First Moscow State Medical University, Institute of Molecular Medicine, Moscow 119146, Russia. Electronic address: terenin@genebee.msu.ru.
Elena AlkalaevaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow 119991, Russia. Electronic address: alkalaeva@eimb.ru.
Engelhardt Institute of Molecular Biology · RULomonosov Moscow State University · RUSechenov University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polyadenylate-binding protein (PABP) stimulates translation termination via interaction of its C-terminal domain with eukaryotic polypeptide chain release factor, eRF3. Additionally, two other proteins, poly(A)-binding protein-interacting proteins 1 and 2 (PAIP1 and PAIP2), bind the same domain of PABP and regulate its translation-related activity. To study the biochemistry of eRF3 and PAIP1/2 competition for PABP binding, we quantified the effects of PAIPs on translation termination in the presence or absence of PABP. Our results demonstrated that both PAIP1 and PAIP2 prevented translation termination at the premature termination codon, by controlling PABP activity. Moreover, PAIP1 and PAIP2 inhibited the activity of free PABP on translation termination

Indexed as

Peptide Chain Termination, TranslationalHumansPeptide Initiation FactorsPeptide Termination FactorsPoly ARepressor ProteinsRNA-Binding ProteinsRNA, MessengerPAIP1 protein, humanPAIP2 protein, humanpeptide-chain-release factor 3Peptide Initiation FactorsPeptide Termination FactorsPoly ARepressor ProteinsRNA-Binding ProteinsRNA, MessengereRF3aPABPPAIP1PAIP2protein complexribosomestop codon readthroughtranslationtranslation controltranslation release factor

Identifiers

PMID30992367
PMCPMC6544843
OpenAlexW2939805847

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.