Evidence map›Paper›PMID 23392125›Full record

ArticleCell death and differentiation2013

ASPP1 and ASPP2 bind active RAS, potentiate RAS signalling and enhance p53 activity in cancer cells.

Y Wang, N Godin-Heymann, X Dan Wang, D Bergamaschi, S Llanos, X Lu

Open access · hybridAbstract read
In one paragraph

Article in Cell death and differentiation, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.6field-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

41 citing papers in PubMed, 63 citations in OpenAlex.

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  16. CagA-ASPP2 complex mediates loss of cell polarity and favorsProceedings of the National Academy of Sciences of the United States of America · 2020
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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

6 authors at 2 institutions in 2 countries.

Y WangNuffield Department of Clinical Medicine, Ludwig Institute for Cancer Research Ltd, University of Oxford, Oxford, UK.
N Godin-Heymann
X Dan Wang
D Bergamaschi
S Llanos
X Lu
Ludwig Cancer Research · GBThe Honourable Society of Lincoln's Inn · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RAS mutations occur frequently in human cancer and activated RAS signalling contributes to tumour development and progression. Apart from its oncogenic effects on cell growth, active RAS has tumour-suppressive functions via its ability to induce cellular senescence and apoptosis. RAS is known to induce p53-dependent cell cycle arrest, yet its effect on p53-dependent apoptosis remains unclear. We report here that apoptosis-stimulating protein of p53 (ASPP) 1 and 2, two activators of p53, preferentially bind active RAS via their N-terminal RAS-association domains (RAD). Additionally, ASPP2 colocalises with and contributes to RAS cellular membrane localisation and potentiates RAS signalling. In cancer cells, ASPP1 and ASPP2 cooperate with oncogenic RAS to enhance the transcription and apoptotic function of p53. Thus, loss of ASPP1 and ASPP2 in human cancer cells may contribute to the full transforming property of RAS oncogene.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsApoptosis Regulatory ProteinsCell LineHumansMCF-7 CellsMiceProtein Bindingras ProteinsRecombinant ProteinsRNA InterferenceRNA, Small InterferingSignal TransductionTumor Suppressor Protein p53Adaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsPPP1R13B protein, humanras ProteinsRecombinant ProteinsRNA, Small InterferingTP53BP2 protein, humanTumor Suppressor Protein p53

Identifiers

PMID23392125
PMCPMC3595493
OpenAlexW2008976455

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.