Evidence map›Paper›PMID 30823509›Full record

ReviewViruses2019

Antiviral Drug Discovery: Norovirus Proteases and Development of Inhibitors.

Kyeong-Ok Chang, Yunjeong Kim, Scott Lovell, Athri D Rathnayake, William C Groutas

Open access · goldAbstract readReview
In one paragraph

Review in Viruses, 2019. 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
7.5field-weighted citation impact, top 2% 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, 75 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
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  9. Article
  10. Article
  11. Potential Antiviral Action of Alkaloids.Molecules (Basel, Switzerland) · 2022
    Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Will curcumin nanosystems be the next promising antiviral alternatives in COVID-19 treatment trials?Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2021
    Review
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 3 institutions in 1 country.

Kyeong-Ok ChangDepartment of Diagnostic Medicine and Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, USA. kchang@vet.ksu.edu.
Yunjeong KimDepartment of Diagnostic Medicine and Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, USA. ykim@vet.ksu.edu.ORCID 0000-0002-2977-4400
Scott LovellProtein Structure Laboratory, The University of Kansas, Lawrence, KS 66047, USA. swlovell@ku.edu.
Athri D RathnayakeDepartment of Chemistry, Wichita State University, Wichita, KS 67260, USA. athridewmina@gmail.com.
William C GroutasDepartment of Chemistry, Wichita State University, Wichita, KS 67260, USA. bill.groutas@wichita.edu.
Kansas State University · USWichita State University · USUniversity of Kansas · US

Funding

Protein Structure Laboratory P30GM110761 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI HANZLIK, ROBERT P · 2014 to 2018
$5.6M
NIGMS NIH HHS P30 GM110761
6 · The paper itself

Abstract

Proteases are a major enzyme group playing important roles in a wide variety of biological processes in life forms ranging from viruses to mammalians. The aberrant activity of proteases can lead to various diseases; consequently, host proteases have been the focus of intense investigation as potential therapeutic targets. A wide range of viruses encode proteases which play an essential role in viral replication and, therefore, constitute attractive targets for the development of antiviral therapeutics. There are numerous examples of successful drug development targeting cellular and viral proteases, including antivirals against human immunodeficiency virus and hepatitis C virus. Most FDA-approved antiviral agents are peptidomimetics and macrocyclic compounds that interact with the active site of a targeted protease. Norovirus proteases are cysteine proteases that contain a chymotrypsin-like fold in their 3D structures. This review focuses on our group's efforts related to the development of norovirus protease inhibitors as potential anti-norovirus therapeutics. These protease inhibitors are rationally designed transition-state inhibitors encompassing dipeptidyl, tripeptidyl and macrocyclic compounds. Highly effective inhibitors validated in X-ray co-crystallization, enzyme and cell-based assays, as well as an animal model, were generated by launching an optimization campaign utilizing the initial hit compounds. A prodrug approach was also explored to improve the pharmacokinetics (PK) of the identified inhibitors.

Indexed as

Drug DiscoveryAntiviral AgentsCaliciviridae InfectionsModels, MolecularNorovirusPeptide HydrolasesPeptidomimeticsProtease InhibitorsProtein ConformationViral ProteinsVirus ReplicationAntiviral AgentsPeptide HydrolasesPeptidomimeticsProtease InhibitorsViral Proteins3C-like proteaseantiviral drug developmentnorovirusesprotease inhibitors

Identifiers

PMID30823509
PMCPMC6410195
OpenAlexW2916113018

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.