Evidence map›Paper›PMID 10949930›Full record

ArticleOncogene2000

Adenovirus E4orf4 protein interacts with both Balpha and B' subunits of protein phosphatase 2A, but E4orf4-induced apoptosis is mediated only by the interaction with Balpha.

R Shtrichman, R Sharf, T Kleinberger

Abstract read
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In one paragraph

Article in Oncogene, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

39 citing papers in PubMed, 68 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

3 authors at 1 institution in 1 country.

R ShtrichmanThe Gonda Center of Molecular Microbiology, The B. Rappaport Faculty of Medicine, Technion, Haifa, Israel.
R Sharf
T Kleinberger
Rappaport Family Institute for Research in the Medical Sciences · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Adenovirus E4orf4 protein is a multifunctional viral regulator, which is involved in down regulation of virally-modulated signal transduction, in control of alternative splicing of viral mRNAs, and in induction of apoptosis in transformed cells. It has been previously shown that E4orf4 interacts with protein phosphatase 2A through the phosphatase Balpha subunit. It was further shown that PP2A is required for performing the various E4orf4 functions. We report here that E4orf4 interacts with multiple isoforms of the PP2A-B' subunit, as well as with Balpha. We map the interaction sites of the B subunits on E4orf4 and show that they overlap but are not identical. We identify a dominant negative E4orf4 mutant, which disrupts the PP2A holoenzyme. We show that induction of apoptosis by E4orf4, which we previously reported to require the interaction with Balpha, is not affected by the interaction with B'. Our results suggest that the interaction of E4orf4 with various PP2A subpopulations may mediate the different E4orf4 functions.

Indexed as

ApoptosisFungal ProteinsAdenovirus E4 ProteinsAdenoviruses, HumanBinding SitesCatalytic DomainCell Line, TransformedHumansMutagenesisPhosphoprotein PhosphatasesPlant ProteinsProtein Phosphatase 2Protein Structure, TertiaryTumor Cells, CulturedViral ProteinsAdenovirus E4 ProteinsE4orf4 protein, adenovirusFungal ProteinsPhosphoprotein PhosphatasesPlant ProteinsPPP2R1B protein, humanProtein Phosphatase 2RGB-1protein, Neurospora crassaViral Proteins

Identifiers

PMID10949930
OpenAlexW2318903071

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.