Evidence map›Paper›PMID 32284326›Full record

ArticleThe Journal of biological chemistry2020

Remdesivir is a direct-acting antiviral that inhibits RNA-dependent RNA polymerase from severe acute respiratory syndrome coronavirus 2 with high potency.

Calvin J Gordon, Egor P Tchesnokov, Emma Woolner, Jason K Perry, Joy Y Feng, Danielle P Porter, Matthias Götte

Registry-linked trialOpen access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT04596839 (Antiviral Activity and Safety of Remdesivir in Bangladeshi Patients With Severe Coronavirus Disease), which is not on this map. Cited by 570 papers.

0numbers the graph read from it
0cells of the map it votes in
570citing papers in PubMed
21.0field-weighted citation impact, top 1% 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.

NCT04596839 phase2completednot on this map

Antiviral Activity and Safety of Remdesivir in Bangladeshi Patients With Severe Coronavirus Disease (COVID-19): An Open Label, Multi-Center, Randomized Controlled Trial

TypeinterventionalSponsorDr. Md. Alimur RezaRan2020 to 2021Enrolled60ConditionsCovid19ArmsRemdesivir, Standard of Care
3 · Its place in the literature

Who cites it

570 citing papers in PubMed, 1,006 citations in OpenAlex.

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510 more citing papers are in PubMed but not listed here.

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

7 authors at 1 institution in 2 countries.

Calvin J GordonDepartment of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta T6G 2R3, Canada.
Egor P TchesnokovDepartment of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta T6G 2R3, Canada.ORCID 0000-0003-1698-2961
Emma WoolnerDepartment of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta T6G 2R3, Canada.ORCID 0000-0002-8697-7802
Jason K PerryLi Ka Shing Institute of Virology, University of Alberta, Edmonton, Alberta T6G 2R3, Canada.ORCID 0000-0001-5492-0652
Joy Y FengLi Ka Shing Institute of Virology, University of Alberta, Edmonton, Alberta T6G 2R3, Canada.
Danielle P PorterLi Ka Shing Institute of Virology, University of Alberta, Edmonton, Alberta T6G 2R3, Canada.
Matthias GötteDepartment of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta T6G 2R3, Canada gotte@ualberta.ca.
University of Alberta · CA

Funding

CIHR 170343
6 · The paper itself

Abstract

Effective treatments for coronavirus disease 2019 (COVID-19) are urgently needed to control this current pandemic, caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Replication of SARS-CoV-2 depends on the viral RNA-dependent RNA polymerase (RdRp), which is the likely target of the investigational nucleotide analogue remdesivir (RDV). RDV shows broad-spectrum antiviral activity against RNA viruses, and previous studies with RdRps from Ebola virus and Middle East respiratory syndrome coronavirus (MERS-CoV) have revealed that delayed chain termination is RDV's plausible mechanism of action. Here, we expressed and purified active SARS-CoV-2 RdRp composed of the nonstructural proteins nsp8 and nsp12. Enzyme kinetics indicated that this RdRp efficiently incorporates the active triphosphate form of RDV (RDV-TP) into RNA. Incorporation of RDV-TP at position

Indexed as

Adenosine MonophosphateAlanineAnimalsAntiviral AgentsBetacoronavirusModels, MolecularRNA-Dependent RNA PolymeraseSARS-CoV-2Sf9 CellsSpodopteraVirus ReplicationAdenosine MonophosphateAlanineAntiviral AgentsremdesivirRNA-Dependent RNA Polymerasecoronavirus (CoV)COVID-19drug actiondrug developmentdrug discoveryEbola virusfavipiravirLassa virusMERSplus-stranded RNA virusremdesivirreplicationribavirinRNA-dependent RNA polymerase (RdRp)RNA polymeraseSARSSARS-CoV-2sofosbuvir

Identifiers

PMID32284326
PMCPMC7242698
OpenAlexW3015554176

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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.