Evidence map›Paper›PMID 19176617›Full record

ArticleJournal of virology2009

Functional replacement of a domain in the rubella virus p150 replicase protein by the virus capsid protein.

Wen-Pin Tzeng, Teryl K Frey

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.5field-weighted citation impact, top 16% 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

12 citing papers in PubMed, 18 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.

Wen-Pin TzengBiology Department, Georgia State University, P.O. Box 4010, Atlanta, GA 30302-4010, USA.
Teryl K Frey
Georgia State University · US

Funding

MOLECULAR BIOLOGY OF RUBELLA VIRUSR01AI021389 · NIAID · GEORGIA STATE UNIVERSITY · PI FREY, TERYL K · 1987 to 2006
$1.7M
Nonstructural roles of capsid proteins in virus replicationR21AI073799 · NIAID · GEORGIA STATE UNIVERSITY · PI FREY, TERYL K · 2008 to 2009
$361k
MOLECULAR BIOLOGY OF RUBELLA VIRUSR23AI021389 · NIAID · GEORGIA STATE UNIVERSITY · PI FREY, TERYL K · 1985 to 1986
–
NIAID NIH HHS AI21389NIAID NIH HHS AI73799NIAID NIH HHS R01 AI021389NIAID NIH HHS R21 AI073799
6 · The paper itself

Abstract

The rubella virus (RUBV) capsid (C) protein rescues mutants with a lethal deletion between two in-frame NotI sites in the P150 replicase gene, a deletion encompassing nucleotides 1685 to 2192 of the RUBV genome and amino acids (aa) 548 to 717 of P150 (which has a total length of 1,301 aa). The complete domain rescuable by the C protein was mapped to aa 497 to 803 of P150. Introduction of aa 1 to 277 of the C protein (lacking the C-terminal E2 signal sequence) between the NotI sites in the P150 gene in a replicon construct yielded a viable construct that synthesized viral RNA with wild-type kinetics, indicating that C and this region of P150 share a common function. Further genetic analysis revealed that an arginine-rich motif between aa 60 and 68 of the C protein was necessary for the rescue of DeltaNotI deletion mutants and substituted for an arginine-rich motif between aa 731 and 735 of the P150 protein when the C protein was introduced into P150. Possible common functions shared by these arginine-rich motifs include RNA binding and interaction with cell proteins.

Indexed as

Recombination, GeneticVirus ReplicationCapsid ProteinsMutagenesis, InsertionalProtein Structure, TertiaryRNA-Dependent RNA PolymeraseRubella virusSequence DeletionCapsid ProteinsRNA-Dependent RNA Polymerase

Identifiers

PMID19176617
PMCPMC2663237
OpenAlexW2152065613

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.