Evidence map›Paper›PMID 23357313›Full record

ArticleAdvances in biological regulation2013

Comparative analysis of interactions of RASSF1-10.

Jia Jia Chan, Delphine Flatters, Fernando Rodrigues-Lima, Jun Yan, Konstantinos Thalassinos, Matilda Katan

Open access · greenAbstract read
In one paragraph

Article in Advances in biological regulation, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

19 citing papers in PubMed, 36 citations in OpenAlex.

  1. The Dual Role ofBiology · 2025
    Review
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  6. Tumor suppressor C-RASSF proteins.Cellular and molecular life sciences : CMLS · 2018
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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 4 institutions in 2 countries.

Jia Jia ChanInstitute of Structural and Molecular Biology, Division of Biosciences, University College London, Gower Street, London WC1E 6BT, UK.
Delphine Flatters
Fernando Rodrigues-Lima
Jun Yan
Konstantinos Thalassinos
Matilda Katan
Institute of Structural and Molecular Biology · GBSorbonne Paris Cité · FRUniversité Paris Cité · FRUniversity College London · GB

Funding

Cancer Research UK A16567Wellcome Trust
6 · The paper itself

Abstract

Members of the RASSF family (RASSF1-10) have been identified as candidate tumour suppressors that are frequently downregulated by promoter hypermethylation in cancers. These proteins carry a common Ras-association (RA) and SARAH domain (RASSF1-6) that can potentially bind Ras oncoproteins and mediate protein-protein interactions with other SARAH domain proteins. However, there is a notable lack of comparative characterisation of the RASSF family, as well as molecular and structural information that facilitate their tumour suppressive functions. As part of our comparative analysis, we modelled the RA and SARAH domains of the RASSF members based on existing structures and predicted their potential interactions. These in silico predictions were compared to in vitro interaction studies with Ras and MST kinase (a SARAH domain-containing protein). Our data shows a diversity of interaction within the RASSF family RA domain, whereas the SARAH domain-mediated interactions for RASSF1-6 are consistent with the predictions. This suggests that different members, despite shared general architecture, could have distinct functional properties. Additionally, we identify a new interacting partner for MST kinase in the form of RASSF7. Current data supports an interaction model where RASSF serves as an adaptor for the assembly of multiple protein complexes and further functional interactions, involving MST kinases and other SARAH domain proteins, which could be regulated by Ras.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceApoptosis Regulatory ProteinsHippo KinasesIntracellular Signaling Peptides and ProteinsModels, MolecularMonomeric GTP-Binding ProteinsProtein MultimerizationProtein Serine-Threonine KinasesProtein Structure, Tertiaryras ProteinsSequence AlignmentTranscription FactorsTumor Suppressor ProteinsAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsHippo KinasesIntracellular Signaling Peptides and ProteinsMonomeric GTP-Binding ProteinsProtein Serine-Threonine Kinasesras ProteinsRASSF1 protein, humanRASSF5 protein, humanRASSF7 protein, humanRASSF8 protein, humanSTK4 protein, humanTranscription FactorsTumor Suppressor Proteins

Identifiers

PMID23357313
PMCPMC4221134
OpenAlexW2031449303

What OpenQuestion holds

Textmetadata
LicenceTDM
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.