Evidence map›Paper›PMID 32047134›Full record

ArticlemBio2020

Both ADP-Ribosyl-Binding and Hydrolase Activities of the Alphavirus nsP3 Macrodomain Affect Neurovirulence in Mice.

Rachy Abraham, Robert L McPherson, Morgan Dasovich, Mohsen Badiee, Anthony K L Leung, Diane E Griffin

Open access · goldAbstract read
In one paragraph

Article in mBio, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed, 1 pooled it
3.7field-weighted citation impact, top 5% 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

50 citing papers in PubMed, 1 synthesis or guideline pooled it, 61 citations in OpenAlex.

  1. Pooled it
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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

6 authors at 2 institutions in 1 country.

Rachy AbrahamW. Harry Feinstone Department of Molecular Microbiology and Immunology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland, USA.
Robert L McPhersonDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland, USA.
Morgan DasovichDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland, USA.
Mohsen BadieeDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland, USA.
Anthony K L LeungDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland, USA anthony.leung@jhu.edu dgriffi6@jhu.edu.
Diane E GriffinW. Harry Feinstone Department of Molecular Microbiology and Immunology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland, USA anthony.leung@jhu.edu dgriffi6@jhu.edu.
Johns Hopkins University · USJohns Hopkins Medicine · US

Funding

TRAINING IN AREAS FUNDAMENTAL TO CANCER RESEARCHT32CA009110 · NCI · JOHNS HOPKINS UNIVERSITY · PI MATUNIS, MICHAEL J., WEERARATNA, ASHANI T · 1985 to 2025
$13.1M
Role of ADP-Ribosylation in Stress Granules-Equipment SupplementR01GM104135 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Anthony K L Leung · 2015 to 2026
$4.2M
The Chemistry-Biology Interface Program at Johns Hopkins UniversityT32GM080189 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ROKITA, STEVEN E · 2008 to 2022
$3.5M
Role of CD4 T cells in fatal alphavisus encephalomyelitisR01NS087539 · NINDS · JOHNS HOPKINS UNIVERSITY · PI GRIFFIN, DIANE E · 2014 to 2018
$1.9M
Role of the nsP3 macrodomain in alphavirus virulenceR56AI137264 · NIAID · JOHNS HOPKINS UNIVERSITY · PI GRIFFIN, DIANE E, LEUNG, ANTHONY K L · 2019 to 2019
$818k
NCI NIH HHS T32 CA009110NIAID NIH HHS R56 AI137264NIGMS NIH HHS R01 GM104135NIGMS NIH HHS T32 GM080189NINDS NIH HHS R01 NS087539
6 · The paper itself

Abstract

Macrodomain (MD), a highly conserved protein fold present in a subset of plus-strand RNA viruses, binds to and hydrolyzes ADP-ribose (ADPr) from ADP-ribosylated proteins. ADPr-binding by the alphavirus nonstructural protein 3 (nsP3) MD is necessary for the initiation of virus replication in neural cells, whereas hydrolase activity facilitates replication complex amplification. To determine the importance of these activities for pathogenesis of alphavirus encephalomyelitis, mutations were introduced into the nsP3 MD of Sindbis virus (SINV), and the effects on ADPr binding and hydrolase activities, virus replication, immune responses, and disease were assessed. Elimination of ADPr-binding and hydrolase activities (G32E) severely impaired

Indexed as

Adenosine Diphosphate RiboseAnimalsBrainCell LineEncephalomyelitisFemaleHydrolasesMiceMutationNeuronsSignal TransductionSindbis VirusViral Nonstructural ProteinsVirulenceVirus ReplicationAdenosine Diphosphate RiboseHydrolasesViral Nonstructural ProteinsADP-ribosyl-binding activityADP-ribosyl hydrolasealphavirusantibodyencephalomyelitisinnate immune responsemacrodomainnsP3Sindbis virus

Identifiers

PMID32047134
PMCPMC7018654
OpenAlexW3006011238

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.