Evidence map›Paper›PMID 35886974›Full record

ArticleInternational journal of molecular sciences2022

Molecular Modelling of NONO and SFPQ Dimerization Process and RNA Recognition Mechanism.

Tommaso Laurenzi, Luca Palazzolo, Elisa Taiana, Simona Saporiti, Omar Ben Mariem, Uliano Guerrini, Antonino Neri, Ivano Eberini

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

13 citing papers in PubMed, 16 citations in OpenAlex.

  1. Engineering a protein homodimer from a heterodimer: A chimeric DBHS protein.Protein science : a publication of the Protein Society · 2026
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  2. Review
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  5. Dissolving stress granules.Nature chemical biology · 2025
    Article
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  7. Review
  8. Article
  9. Article
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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

8 authors at 1 institution in 1 country.

Tommaso LaurenziDepartment of Oncology and Hemato-Oncology, University of Milan, 20122 Milan, Italy.ORCID 0000-0002-0446-0392
Luca PalazzoloDipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, 20133 Milan, Italy.ORCID 0000-0002-5370-9588
Elisa TaianaDepartment of Oncology and Hemato-Oncology, University of Milan, 20122 Milan, Italy.ORCID 0000-0003-4940-1318
Simona SaporitiDipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, 20133 Milan, Italy.ORCID 0000-0002-2096-1066
Omar Ben MariemDipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, 20133 Milan, Italy.
Uliano GuerriniDipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, 20133 Milan, Italy.
Antonino NeriDepartment of Oncology and Hemato-Oncology, University of Milan, 20122 Milan, Italy.
Ivano EberiniDipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, 20133 Milan, Italy.ORCID 0000-0001-5521-3829
University of Milan · IT

Funding

Italian Association for Cancer Research IG24365Ministry of Education, Universities and Research Progetto Eccellenza
6 · The paper itself

Abstract

NONO and SFPQ are involved in multiple nuclear processes (e.g., pre-mRNA splicing, DNA repair, and transcriptional regulation). These proteins, along with NEAT1, enable paraspeckle formation, thus promoting multiple myeloma cell survival. In this paper, we investigate NONO and SFPQ dimer stability, highlighting the hetero- and homodimer structural differences, and model their interactions with RNA, simulating their binding to a polyG probe mimicking NEAT1guanine-rich regions. We demonstrated in silico that NONO::SFPQ heterodimerization is a more favorable process than homodimer formation. We also show that NONO and SFPQ RRM2 subunits are primarily required for protein-protein interactions with the other DBHS protomer. Simulation of RNA binding to NONO and SFPQ, beside validating RRM1 RNP signature importance, highlighted the role of β2 and β4 strand residues for RNA specific recognition. Moreover, we demonstrated the role of the NOPS region and other protomer's RRM2 β2/β3 loop in strengthening the interaction with RNA. Our results, having deepened RNA and DBHS dimer interactions, could contribute to the design of small molecules to modulate the activity of these proteins. RNA-mimetics, able to selectively bind to NONO and/or SFPQ RNA-recognition site, could impair paraspeckle formation, thus representing a first step towards the discovery of drugs for multiple myeloma treatment.

Indexed as

DNA-Binding ProteinsMultiple MyelomaPTB-Associated Splicing FactorRNADimerizationHumansProtein SubunitsRNA-Binding ProteinsRNA Splicing FactorsDNA-Binding ProteinsNONO protein, humanProtein SubunitsPTB-Associated Splicing FactorRNARNA-Binding ProteinsRNA Splicing FactorsDBHSNONOSFPQstructural bioinformatics

Identifiers

PMID35886974
PMCPMC9324803
OpenAlexW4285013182

What OpenQuestion holds

Textmetadata
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.