Evidence map›Paper›PMID 30694421›Full record

ArticleVirus genes2019

Recombinant HCV NS3 and NS5B enzymes exhibit multiple posttranslational modifications for potential regulation.

Sergio Hernández, Ariel Díaz, Alejandra Loyola, Rodrigo A Villanueva

Abstract read
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In one paragraph

Article in Virus genes, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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

1 citing paper in PubMed.

  1. Article
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

4 authors.

Sergio HernándezFundación Ciencia &, Vida, Avda. Zañartu 1482, 7780272, Ñuñoa, Santiago, Chile.
Ariel DíazFundación Ciencia &, Vida, Avda. Zañartu 1482, 7780272, Ñuñoa, Santiago, Chile.
Alejandra LoyolaFundación Ciencia &, Vida, Avda. Zañartu 1482, 7780272, Ñuñoa, Santiago, Chile.
Rodrigo A VillanuevaFundación Ciencia &, Vida, Avda. Zañartu 1482, 7780272, Ñuñoa, Santiago, Chile. rvillanueva@cienciavida.org.

Funding

Conicyt CONICYT, Basal Project AFB 170004Conicyt PCHA/Doctorado Nacional/2014-21140956Fondecyt FONDECYT 1100200Fondecyt FONDECYT 1160480
6 · The paper itself

Abstract

Posttranslational modification (PTM) of proteins is critical to modulate protein function and to improve the functional diversity of polypeptides. In this report, we have analyzed the PTM of both hepatitis C virus NS3 and NS5B enzyme proteins, upon their individual expression in insect cells under the baculovirus expression system. Using mass spectrometry, we present evidence that these recombinant proteins exhibit diverse covalent modifications on certain amino acid side chains, such as phosphorylation, ubiquitination, and acetylation. Although the functional implications of these PTM must be further addressed, these data may prove useful toward the understanding of the complex regulation of these key viral enzymes and to uncover novel potential targets for antiviral design.

Indexed as

DEAD-box RNA HelicasesGene Expression Regulation, ViralHepacivirusHepatitis CHumansNucleoside-TriphosphataseProtein Processing, Post-TranslationalRNA-Dependent RNA PolymeraseSerine EndopeptidasesViral Nonstructural ProteinsViral ProteasesDEAD-box RNA HelicasesNS3 protein, hepatitis C virusNS-5 protein, hepatitis C virusNucleoside-TriphosphataseRNA-Dependent RNA PolymeraseSerine EndopeptidasesViral Nonstructural ProteinsViral ProteasesHCVHepatitis C virusNS3NS5BPosttranslational modificationProtein regulation

Identifiers

What OpenQuestion holds

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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.