Evidence map›Paper›PMID 26726314›Full record

ArticleACS infectious diseases2015

Identification and Characterization of Novel Broad-Spectrum Inhibitors of the Flavivirus Methyltransferase.

Matthew Brecher, Hui Chen, Zhong Li, Nilesh K Banavali, Susan A Jones, Jing Zhang, Laura D Kramer, Hongmin Li

Abstract read
In one paragraph

Article in ACS infectious diseases, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
5.0field-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

34 citing papers in PubMed, 62 citations in OpenAlex.

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  14. Journal of traditional and complementary medicine · 2023
    Article
  15. Zika Virus Inhibitors Based on a 1,3-Disubstituted 1Molecules (Basel, Switzerland) · 2022
    Article
  16. Article
  17. Article
  18. Review
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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

8 authors at 2 institutions in 1 country.

Matthew BrecherWadsworth Center, New York State Department of Health , 120 New Scotland Avenue, Albany, New York 12208, United States.
Hui ChenWadsworth Center, New York State Department of Health , 120 New Scotland Avenue, Albany, New York 12208, United States.
Zhong LiWadsworth Center, New York State Department of Health , 120 New Scotland Avenue, Albany, New York 12208, United States.
Nilesh K BanavaliWadsworth Center, New York State Department of Health , 120 New Scotland Avenue, Albany, New York 12208, United States.
Susan A JonesWadsworth Center, New York State Department of Health , 120 New Scotland Avenue, Albany, New York 12208, United States.
Jing ZhangWadsworth Center, New York State Department of Health , 120 New Scotland Avenue, Albany, New York 12208, United States.
Laura D KramerWadsworth Center, New York State Department of Health , 120 New Scotland Avenue, Albany, New York 12208, United States.
Hongmin LiWadsworth Center, New York State Department of Health , 120 New Scotland Avenue, Albany, New York 12208, United States.
New York State Department of Health · USWadsworth Center · US

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Inhibition and mechanism of flavivirus methyltransferaseR01AI094335 · NIAID · WADSWORTH CENTER · PI GHOSH, ARUN K, KRAMER, LAURA D · 2011 to 2015
$3.2M
Training in Biodefense and Emerging Infectious DiseaseT32AI055429 · NIAID · WADSWORTH CENTER · PI MCDONOUGH, KATHLEEN A · 2004 to 2014
$2.2M
NIAID NIH HHS R01 AI094335NIAID NIH HHS T32 AI055429NIGMS NIH HHS P41 GM103393
6 · The paper itself

Abstract

Flavivirus methyltransferase (MTase) is essential for viral replication. Here we report the identification of small molecules through virtual screening that putatively bind to the SAM-binding site of flavivirus MTase and inhibit its function. Six of these computationally predicted binders were identified to show significant MTase inhibition with low micromolar inhibitory activity. The most active compounds showed broad-spectrum activity against the MTase proteins of other flaviviruses. Two of these compounds also showed low cytotoxicity and high antiviral efficacy in cell-based assays. Competitive binding analyses indicated that the inhibitors performed their inhibitory function through competitive binding to the SAM cofactor binding site of the MTase. The crystal structure of the MTase-inhibitor complex further supports the mode of action and provides routes for their further optimization as flavivirus MTase inhibitors.

Indexed as

antiviral developmentflavivirus NS5methyltransferaseRNA cap methylationWest Nile virus

Identifiers

PMID26726314
PMCPMC4696607
OpenAlexW2323091040

What OpenQuestion 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 OpenQuestion graph.