Evidence map›Paper›PMID 26473910›Full record

ReviewViruses2015

Phosphorylation of Single Stranded RNA Virus Proteins and Potential for Novel Therapeutic Strategies.

Forrest Keck, Pouya Ataey, Moushimi Amaya, Charles Bailey, Aarthi Narayanan

Open access · goldAbstract readReview
In one paragraph

Review in Viruses, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

31 citing papers in PubMed, 59 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

5 authors at 1 institution in 1 country.

Forrest KeckNational Center for Biodefense and Infectious Disease, School of Systems Biology, George Mason University, 10650 Pyramid Place, Manassas, VA 20110, USA. fkeck@masonlive.gmu.edu.
Pouya AtaeyNational Center for Biodefense and Infectious Disease, School of Systems Biology, George Mason University, 10650 Pyramid Place, Manassas, VA 20110, USA. pataey@gmu.edu.
Moushimi AmayaNational Center for Biodefense and Infectious Disease, School of Systems Biology, George Mason University, 10650 Pyramid Place, Manassas, VA 20110, USA. mamaya3@gmu.edu.
Charles BaileyNational Center for Biodefense and Infectious Disease, School of Systems Biology, George Mason University, 10650 Pyramid Place, Manassas, VA 20110, USA. cbailey2@gmu.edu.
Aarthi NarayananNational Center for Biodefense and Infectious Disease, School of Systems Biology, George Mason University, 10650 Pyramid Place, Manassas, VA 20110, USA. anaraya1@gmu.edu.
George Mason University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post translational modification of proteins is a critical requirement that regulates function. Among the diverse kinds of protein post translational modifications, phosphorylation plays essential roles in protein folding, protein:protein interactions, signal transduction, intracellular localization, transcription regulation, cell cycle progression, survival and apoptosis. Protein phosphorylation is also essential for many intracellular pathogens to establish a productive infection cycle. Preservation of protein phosphorylation moieties in pathogens in a manner that mirrors the host components underscores the co-evolutionary trajectory of pathogens and hosts, and sheds light on how successful pathogens have usurped, either in part or as a whole, the host enzymatic machinery. Phosphorylation of viral proteins for many acute RNA viruses including Flaviviruses and Alphaviruses has been demonstrated to be critical for protein functionality. This review focuses on phosphorylation modifications that have been documented to occur on viral proteins with emphasis on acutely infectious, single stranded RNA viruses. The review additionally explores the possibility of repurposing Food and Drug Administration (FDA) approved inhibitors as antivirals for the treatment of acute RNA viral infections.

Indexed as

Host-Pathogen InteractionsProtein Processing, Post-TranslationalAnimalsAntiviral AgentsHumansPhosphorylationProtein Kinase InhibitorsRNA VirusesViral ProteinsAntiviral AgentsProtein Kinase InhibitorsViral Proteinsantiviralskinasephosphorylationpost translational modificationtherapeuticsviral protein

Identifiers

PMID26473910
PMCPMC4632380
OpenAlexW2136367022

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.