Evidence map›Paper›PMID 36257129›Full record

ArticleVirology2022

In vitro particle-associated uridyltransferase activity of the rotavirus VP1 polymerase.

Mackenzie L Anderson, Sarah McDonald Esstman

Abstract read
In one paragraph

Article in Virology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Mackenzie L AndersonDepartment of Biology, Wake Forest University, Winston-Salem, NC, USA.
Sarah McDonald EsstmanDepartment of Biology, Wake Forest University, Winston-Salem, NC, USA. Electronic address: mcdonasm@wfu.edu.

Funding

Rotavirus Genome Replication and Virion AssemblyR01AI116815 · NIAID · WAKE FOREST UNIVERSITY · PI Sarah Marie McDonald Esstman · 2015 to 2026
$3.7M
NIAID NIH HHS R01 AI116815
6 · The paper itself

Abstract

Rotaviruses are 11-segmented, double-stranded RNA (dsRNA) viruses with a unique intra-particle RNA synthesis mechanism. During genome replication, the RNA-dependent RNA polymerase (VP1) performs minus-strand RNA (-ssRNA) synthesis on positive-strand RNA (+ssRNA) templates to create dsRNA segments. Recombinant VP1 catalyzes -ssRNA synthesis using substrate NTPs in vitro, but only when the VP2 core shell protein or virus-like particles made of VP2 and VP6 (2/6-VLPs) are included in the reaction. The dsRNA product can be labeled using [α

Indexed as

RotavirusCapsid ProteinsRNA-Dependent RNA PolymeraseRNA, Double-StrandedRNA, ViralUridine TriphosphateCapsid ProteinsRNA-Dependent RNA PolymeraseRNA, Double-StrandedRNA, ViralUridine TriphosphateCore shell proteinNucleotidyltransferaseRNA-Dependent RNA polymeraseRotavirusUridyltransferaseVirus-like particlesVP1VP2

Identifiers

PMID36257129
PMCPMC10728782

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.