Evidence map›Paper›PMID 22689780›Full record

ArticleBioinformatics (Oxford, England)2012

Novel domain combinations in proteins encoded by chimeric transcripts.

Milana Frenkel-Morgenstern, Alfonso Valencia

Abstract read
In one paragraph

Article in Bioinformatics (Oxford, England), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

26 citing papers in PubMed.

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  8. Molecular Signatures of Fusion Proteins in Cancer.ACS pharmacology & translational science · 2019
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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

2 authors.

Milana Frenkel-MorgensternStructural Biology and BioComputing Program, Spanish National Cancer Research Centre (CNIO), 28029 Madrid, Spain.
Alfonso Valencia

Funding

NHGRI NIH HHS HG00455-04
6 · The paper itself

Abstract

motivationChimeric RNA transcripts are generated by different mechanisms including pre-mRNA trans-splicing, chromosomal translocations and/or gene fusions. It was shown recently that at least some of chimeric transcripts can be translated into functional chimeric proteins.

resultsTo gain a better understanding of the design principles underlying chimeric proteins, we have analyzed 7,424 chimeric RNAs from humans. We focused on the specific domains present in these proteins, comparing their permutations with those of known human proteins. Our method uses genomic alignments of the chimeras, identification of the gene-gene junction sites and prediction of the protein domains. We found that chimeras contain complete protein domains significantly more often than in random data sets. Specifically, we show that eight different types of domains are over-represented among all chimeras as well as in those chimeras confirmed by RNA-seq experiments. Moreover, we discovered that some chimeras potentially encode proteins with novel and unique domain combinations. Given the observed prevalence of entire protein domains in chimeras, we predict that certain putative chimeras that lack activation domains may actively compete with their parental proteins, thereby exerting dominant negative effects. More generally, the production of chimeric transcripts enables a combinatorial increase in the number of protein products available, which may disturb the function of parental genes and influence their protein-protein interaction network. AVAILABILITY: our scripts are available upon request.

Indexed as

Protein Interaction Domains and MotifsTrans-SplicingHumansMutant Chimeric ProteinsOncogene Proteins, FusionProtein Interaction MapsRNASequence Analysis, RNAMutant Chimeric ProteinsOncogene Proteins, FusionRNA

Identifiers

PMID22689780
PMCPMC3371848

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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.