Evidence map›Paper›PMID 24003031›Full record

ArticleNucleic acids research2013

Principles of self-organization in biological pathways: a hypothesis on the autogenous association of alpha-synuclein.

Andreas Zanzoni, Domenica Marchese, Federico Agostini, Benedetta Bolognesi, Davide Cirillo, Maria Botta-Orfila, Carmen Maria Livi, Silvia Rodriguez-Mulero, Gian Gaetano Tartaglia

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

30 citing papers in PubMed, 51 citations in OpenAlex.

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  11. Auto-regulatory feedback by RNA-binding proteins.Journal of molecular cell biology · 2019
    Review
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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 2 institutions in 1 country.

Andreas ZanzoniGene Function and Evolution, Bioinformatics and Genomics, Centre for Genomic Regulation (CRG), 08003 Barcelona, Spain and Universitat Pompeu Fabra (UPF), 08003 Barcelona, Spain.
Domenica Marchese
Federico Agostini
Benedetta Bolognesi
Davide Cirillo
Maria Botta-Orfila
Carmen Maria Livi
Silvia Rodriguez-Mulero
Gian Gaetano Tartaglia
Pompeu Fabra University · ESCentre for Genomic Regulation · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Previous evidence indicates that a number of proteins are able to interact with cognate mRNAs. These autogenous associations represent important regulatory mechanisms that control gene expression at the translational level. Using the catRAPID approach to predict the propensity of proteins to bind to RNA, we investigated the occurrence of autogenous associations in the human proteome. Our algorithm correctly identified binding sites in well-known cases such as thymidylate synthase, tumor suppressor P53, synaptotagmin-1, serine/ariginine-rich splicing factor 2, heat shock 70 kDa, ribonucleic particle-specific U1A and ribosomal protein S13. In addition, we found that several other proteins are able to bind to their own mRNAs. A large-scale analysis of biological pathways revealed that aggregation-prone and structurally disordered proteins have the highest propensity to interact with cognate RNAs. These findings are substantiated by experimental evidence on amyloidogenic proteins such as TAR DNA-binding protein 43 and fragile X mental retardation protein. Among the amyloidogenic proteins, we predicted that Parkinson's disease-related α-synuclein is highly prone to interact with cognate transcripts, which suggests the existence of RNA-dependent factors in its function and dysfunction. Indeed, as aggregation is intrinsically concentration dependent, it is possible that autogenous interactions play a crucial role in controlling protein homeostasis.

Indexed as

Algorithmsalpha-SynucleinBinding SitesGene Expression RegulationHumansIntrinsically Disordered ProteinsNuclear ProteinsProtein BiosynthesisRibonucleoproteinsRNARNA-Binding ProteinsRNA, MessengerSerine-Arginine Splicing FactorsTumor Suppressor Protein p53alpha-SynucleinIntrinsically Disordered ProteinsNuclear ProteinsRibonucleoproteinsRNARNA-Binding ProteinsRNA, MessengerSerine-Arginine Splicing FactorsSRSF2 protein, humanTumor Suppressor Protein p53

Identifiers

PMID24003031
PMCPMC3905859
OpenAlexW2121580577

What OpenQuestion holds

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LicenceCC BY
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.