Evidence map›Paper›PMID 37762447›Full record

ArticleInternational journal of molecular sciences2023

Properties of Plant Virus Protein Encoded by the 5'-Proximal Gene of Tetra-Cistron Movement Block.

Denis A Chergintsev, Anna D Solovieva, Anastasia K Atabekova, Alexander A Lezzhov, Sergei A Golyshev, Sergey Y Morozov, Andrey G Solovyev

Open access · goldAbstract 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. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. Plants (Basel, Switzerland) · 2025
    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

7 authors at 1 institution in 1 country.

Denis A ChergintsevA. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119992 Moscow, Russia.ORCID 0000-0003-0234-0888
Anna D SolovievaDepartment of Virology, Biological Faculty, Moscow State University, 119234 Moscow, Russia.
Anastasia K AtabekovaA. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119992 Moscow, Russia.ORCID 0000-0003-1051-0517
Alexander A LezzhovA. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119992 Moscow, Russia.ORCID 0000-0003-4678-8334
Sergei A GolyshevA. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119992 Moscow, Russia.ORCID 0000-0002-4877-1061
Sergey Y MorozovA. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119992 Moscow, Russia.ORCID 0000-0001-5123-8025
Andrey G SolovyevA. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119992 Moscow, Russia.ORCID 0000-0001-6284-9155
Lomonosov Moscow State University · RU

Funding

Russian Science Foundation 22-14-00063
6 · The paper itself

Abstract

To move from cell to cell through plasmodesmata, many plant viruses require the concerted action of two or more movement proteins (MPs) encoded by transport gene modules of virus genomes. A tetra-cistron movement block (TCMB) is a newly discovered transport module comprising four genes. TCMB encodes three proteins, which are similar to MPs of the transport module known as the "triple gene block", and a protein unrelated to known viral MPs and containing a double-stranded RNA (dsRNA)-binding domain similar to that found in a family of cell proteins, including AtDRB4 and AtHYL1. Here, the latter TCMB protein, named vDRB for virus dsRNA-binding protein, is shown to bind both dsRNA and single-stranded RNA in vitro. In a turnip crinkle virus-based assay, vDRB exhibits the properties of a viral suppressor of RNA silencing (VSR). In the context of potato virus X infection, vDRB significantly decreases the number and size of "dark green islands", regions of local antiviral silencing, supporting the VSR function of vDRB. Nevertheless, vDRB does not exhibit the VSR properties in non-viral transient expression assays. Taken together, the data presented here indicate that vDRB is an RNA-binding protein exhibiting VSR functions in the context of viral infection.

Indexed as

Plant Viral Movement ProteinsPlant VirusesPotexvirusViral ProteinsNicotianaPlant DiseasesRNA, Double-StrandedRNA InterferenceRNA, ViralPlant Viral Movement ProteinsRNA, Double-StrandedRNA, ViralViral Proteinsdouble-stranded RNA bindingplant virusRNA-binding proteinRNA silencingviral suppressor of RNA silencingvirus cell-to-cell movementvirus movement protein

Identifiers

PMID37762447
PMCPMC10532019
OpenAlexW4386815136

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.