Evidence map›Paper›PMID 36768895›Full record

ArticleInternational journal of molecular sciences2023

NMR Analysis Suggests Synergy between the RRM2 and the Carboxy-Terminal Segment of Human La Protein in the Recognition and Interaction with HCV IRES.

Aikaterini I Argyriou, Georgios A Machaliotis, Garyfallia I Makrynitsa, Eleni G Kaliatsi, Constantinos Stathopoulos, Georgios A Spyroulias

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Aikaterini I ArgyriouDepartment of Pharmacy, University of Patras, GR-26504 Patras, Greece.
Georgios A MachaliotisDepartment of Pharmacy, University of Patras, GR-26504 Patras, Greece.
Garyfallia I MakrynitsaDepartment of Pharmacy, University of Patras, GR-26504 Patras, Greece.
Eleni G KaliatsiDepartment of Biochemistry, School of Medicine, University of Patras, GR-26504 Patras, Greece.ORCID 0000-0001-5397-3445
Constantinos StathopoulosDepartment of Biochemistry, School of Medicine, University of Patras, GR-26504 Patras, Greece.ORCID 0000-0002-5699-4118
Georgios A SpyrouliasDepartment of Pharmacy, University of Patras, GR-26504 Patras, Greece.ORCID 0000-0003-1799-3312

Funding

Competitiveness, Entrepreneurship and Innovation' (NSRF 2014-2020) and co-financed by Greece and the European Union (European Regional Development Fund). 5002550EU FP7 REGPOT CT-2011 285950Greece and the European Union (European Social Fund- ESF) 5033021
6 · The paper itself

Abstract

The La protein (lupus antigen) is a ubiquitous RNA-binding protein found in all human cells. It is mainly localized in the nucleus, associates with all RNA polymerase III (Pol III) transcripts, as the first factor they interact with, and modulates subsequent processing events. Export of La to the cytoplasm has been reported to stimulate the decoding of specific cellular and viral mRNAs through IRES-dependent (Internal ribosome entry site) binding and translation. Using NMR (Nuclear Magnetic Resonance) spectroscopy, we provide atomic-level-resolution structural insights on the dynamical properties of human La (hLa) protein in solution. Moreover, using a combination of NMR spectroscopy and isothermal titration calorimetry (ITC), we provide evidence about the role and ligand specificity of the C-terminal domain of the La protein (RRM2 and C-terminal region) that could mediate the recognition of HCV-IRES.

Indexed as

Hepatitis CProtein BiosynthesisHepacivirusHumansInternal Ribosome Entry SitesMagnetic Resonance SpectroscopyPhosphoproteinsRibonucleoproteinsRibosomesRNA, ViralInternal Ribosome Entry SitesLa protein, humanPhosphoproteinsRibonucleoproteinsRNA, Viralhepatitis C virusIRESLalupus antigenNMRRNA-binding proteinsRNA virus

Identifiers

PMID36768895
PMCPMC9916714

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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.