Evidence map›Paper›PMID 17344283›Full record

ArticleJournal of virology2007

Role of the foamy virus Pol cleavage site in viral replication.

Jacqueline Roy, Maxine L Linial

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.7field-weighted citation impact, top 37% 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

16 citing papers in PubMed, 24 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

Jacqueline RoyDivision of Basic Sciences, Fred Hutchinson Cancer Research Center, 1100 Fairview Ave. N., Seattle, WA 98109-1024, USA.
Maxine L Linial
Fred Hutch Cancer Center · US

Funding

VIRAL CODED FUNCTIONS IN ROUS SARCOMA VIRUSR01CA018282 · NCI · FRED HUTCHINSON CANCER RESEARCH CENTER · PI LINIAL, MAXINE L · 1985 to 2011
$5.0M
NCI NIH HHS CA-18282NCI NIH HHS R01 CA018282
6 · The paper itself

Abstract

Foamy virus Pol precursor protein processing by the viral protease occurs at only one site, releasing a protease-reverse transcriptase and an integrase protein. To examine whether the cleavage of the Pol precursor protein is necessary for enzymatic activities and efficient viral replication, several mutations were generated around the cleavage site. All cleavage site mutants synthesize wild-type levels of Pol precursor protein. Mutants containing more than two amino acid substitutions around the cleavage site exhibit no detectable Pol processing. The Pol cleavage site is not required for the production of infectious particles in a single round of infection, but is important for subsequent rounds of viral infection. Mutations around the cleavage site affected the enzymatic activities of the protease and reverse transcriptase and prevented replication after two rounds of infection. Interestingly, Pol encapsidation is significantly reduced in some of the mutants.

Indexed as

Virus ReplicationAmino Acid SubstitutionGene Products, polMutagenesisMutationPeptide HydrolasesProtein PrecursorsProtein Processing, Post-TranslationalReplication OriginRNA-Directed DNA PolymeraseSpumavirusGene Products, polPeptide HydrolasesProtein PrecursorsRNA-Directed DNA Polymerase

Identifiers

PMID17344283
PMCPMC1900213
OpenAlexW2047480046

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.