Evidence map›Paper›PMID 30076219›Full record

ArticleThe Journal of biological chemistry2018

Structural analyses reveal the mechanism of inhibition of influenza virus NS1 by two antiviral compounds.

Alex B Kleinpeter, Alexander S Jureka, Sally M Falahat, Todd J Green, Chad M Petit

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 29 citations in OpenAlex.

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  15. Molecular recognition of a host protein by NS1 of pandemic and seasonal influenza A viruses.Proceedings of the National Academy of Sciences of the United States of America · 2020
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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

5 authors at 2 institutions in 2 countries.

Alex B KleinpeterFrom the Departments of Biochemistry and Molecular Genetics and.
Alexander S JurekaFrom the Departments of Biochemistry and Molecular Genetics and.
Sally M FalahatFrom the Departments of Biochemistry and Molecular Genetics and.
Todd J GreenMicrobiology, University of Alabama at Birmingham, Birmingham, Alabama 35294.
Chad M PetitFrom the Departments of Biochemistry and Molecular Genetics and cpetit@uab.edu.ORCID 0000-0003-4933-6245
University of Alabama at Birmingham · USLaboratory of Molecular Genetics · PL

Funding

XRAY CRYSTALLOGRAPHYP30CA013148 · NCI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI Robert S Welner · 1985 to 2026
$165.9M
Training Program in Cell, Molecular, and Developmental BiologyT32GM008111 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI YODER, BRADLEY K. · 1985 to 2022
$5.4M
800 MHz NMR Spectrometer for the Central Alabama High-Field NMR FacilityS10RR022994 · NCRR · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI KRISHNA, NEPALLI RAMA · 2009 to 2009
$2.0M
Strain Dependent Structure and Function of the Influenza NS1 ProteinR01AI134693 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI PETIT, CHAD · 2018 to 2022
$1.9M
Transcription and replication in nonsegmented negative-strand RNA virusesR01AI116738 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI GREEN, TODD JASON · 2015 to 2019
$1.8M
NCI NIH HHS P30 CA013148NCRR NIH HHS S10 RR022994NIAID NIH HHS R01 AI116738NIAID NIH HHS R01 AI134693NIGMS NIH HHS T32 GM008111
6 · The paper itself

Abstract

The influenza virus is a significant public health concern causing 250,000-500,000 deaths worldwide each year. Its ability to change quickly results in the potential for rapid generation of pandemic strains for which most individuals would have no antibody protection. This pandemic potential highlights the need for the continuous development of new drugs against influenza virus. As an essential component and well established virulence determinant, NS1 (nonstructural protein 1) of influenza virus is a highly prioritized target for the development of anti-influenza compounds. Here, we used NMR to determine that the NS1 effector domain (NS1

Indexed as

Antiviral AgentsBinding SitesCleavage And Polyadenylation Specificity FactorCrystallography, X-RayDimerizationDrug DevelopmentHumansHydrophobic and Hydrophilic InteractionsInfluenza A Virus, H1N1 SubtypeNuclear Magnetic Resonance, BiomolecularProtein ConformationProteolysisViral Nonstructural ProteinsVirus ReplicationAntiviral AgentsCleavage And Polyadenylation Specificity FactorCPSF4 protein, humanINS1 protein, influenza virusViral Nonstructural Proteins1918 H1N12013 H7N9antiviral agentCPSF30influenzainfluenza virusnonstructural protein 1NS1nuclear magnetic resonance (NMR)protein structureviral proteinviral replication

Identifiers

PMID30076219
PMCPMC6153301
OpenAlexW2887053565

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.