Evidence map›Paper›PMID 16373495›Full record

ArticleRNA (New York, N.Y.)2006

Virus-like particles of the Ty3 retrotransposon assemble in association with P-body components.

Nadejda Beliakova-Bethell, Carla Beckham, Thomas H Giddings, Mark Winey, Roy Parker, Suzanne Sandmeyer

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

70 citing papers in PubMed, 99 citations in OpenAlex.

  1. Review
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  4. Elimination of virus-like particles reduces protein aggregation and extends replicative lifespan inProceedings of the National Academy of Sciences of the United States of America · 2024
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10 more citing papers are in PubMed but not listed here.

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 at 3 institutions in 1 country.

Nadejda Beliakova-BethellDepartment of Biological Chemistry, School of Medicine, University of California, Irvine, CA 92697-1700, USA.
Carla Beckham
Thomas H Giddings
Mark Winey
Roy Parker
Suzanne Sandmeyer
Howard Hughes Medical Institute · USUniversity of California, Irvine · USUniversity of Colorado Boulder · US

Funding

mRNA Decapping in YeastR37GM045443 · NIGMS · UNIVERSITY OF COLORADO · PI PARKER, ROY · 2004 to 2013
$3.1M
NIGMS NIH HHS R37 GM045443
6 · The paper itself

Abstract

Retroviruses and retrotransposons assemble intracellular immature core particles around a RNA genome, and nascent particles collect in association with membranes or as intracellular clusters. How and where genomic RNA are identified for retrovirus and retrotransposon assembly, and how translation and assembly processes are coordinated is poorly understood. To understand this process, the subcellular localization of Ty3 RNA and capsid proteins and virus-like particles was investigated. We demonstrate that mRNAs, proteins, and virus-like particles of the yeast Ty3 retrotransposon accumulate in association with cytoplasmic P-bodies, which are sites of mRNA translation repression, storage, and degradation. Deletions of genes encoding P-body proteins decreased Ty3 transposition and caused changes in the pattern of Ty3 foci, underscoring the biological significance of the association of Ty3 virus-like protein components and P-bodies. These results suggest the hypothesis that P-bodies may serve to segregate translation and assembly functions of the Ty3 genomic RNA to promote assembly of virus-like particles. Because Ty3 has features of a simple retrovirus and P-body functions are conserved between yeast and metazoan organisms, these findings may provide insights into host factors that facilitate retrovirus assembly.

Indexed as

VirionVirus AssemblyInclusion BodiesRetroelementsRetroviridaeRNA-Directed DNA PolymeraseSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence HomologyRetroelementsreverse transcriptase Ty3, S cerevisiaeRNA-Directed DNA PolymeraseSaccharomyces cerevisiae Proteins

Identifiers

PMID16373495
PMCPMC1370889
OpenAlexW2128244810

What OpenQuestion holds

Textmetadata
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.