Evidence map›Paper›PMID 34696498›Full record

ReviewViruses2021

Norovirus Protease Structure and Antivirals Development.

Boyang Zhao, Liya Hu, Yongcheng Song, Ketki Patil, Sasirekha Ramani, Robert L Atmar, Mary K Estes, B V Venkataram Prasad

Open access · goldAbstract readReview
In one paragraph

Review in Viruses, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.5field-weighted citation impact, top 33% 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

9 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
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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 1 institution in 1 country.

Boyang ZhaoDepartment of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX 77030, USA.
Liya HuVerna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.ORCID 0000-0002-8340-8911
Yongcheng SongDepartment of Pharmacology and Chemical Biology, Baylor College of Medicine, Houston, TX 77030, USA.
Ketki PatilDepartment of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX 77030, USA.
Sasirekha RamaniDepartment of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX 77030, USA.ORCID 0000-0001-5631-8534
Robert L AtmarDepartment of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX 77030, USA.
Mary K EstesDepartment of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX 77030, USA.
B V Venkataram PrasadDepartment of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX 77030, USA.ORCID 0000-0002-1172-2071
Baylor College of Medicine · US

Funding

X-ray Crystallographic Studies on CalicivirusesP01AI057788 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI PRASAD, BIDADI VENKATARAM · 2004 to 2024
$34.4M
Tissue Analysis & Molecular Imaging CoreP30DK056338 · NIDDK · BAYLOR COLLEGE OF MEDICINE · PI James Versalovic · 2001 to 2026
$28.3M
National Institute of Health PO1 AI 057788NIAID NIH HHS P01 AI057788NIDDK NIH HHS P30 DK056338
6 · The paper itself

Abstract

Human norovirus (HuNoV) infection is a global health and economic burden. Currently, there are no licensed HuNoV vaccines or antiviral drugs available. The protease encoded by the HuNoV genome plays a critical role in virus replication by cleaving the polyprotein and is an excellent target for developing small-molecule inhibitors. The current strategy for developing HuNoV protease inhibitors is by targeting the enzyme's active site and designing inhibitors that bind to the substrate-binding pockets located near the active site. However, subtle differential conformational flexibility in response to the different substrates in the polyprotein and structural differences in the active site and substrate-binding pockets across different genogroups, hamper the development of effective broad-spectrum inhibitors. A comparative analysis of the available HuNoV protease structures may provide valuable insight for identifying novel strategies for the design and development of such inhibitors. The goal of this review is to provide such analysis together with an overview of the current status of the design and development of HuNoV protease inhibitors.

Indexed as

Drug DevelopmentAnimalsAntiviral AgentsBinding SitesCaliciviridae InfectionsCatalytic DomainGenotypeHumansModels, MolecularNorovirusPeptide HydrolasesPolyproteinsProtease InhibitorsProtein ConformationProtein Interaction Domains and MotifsViral ProteinsAntiviral AgentsPeptide HydrolasesPolyproteinsProtease InhibitorsViral Proteinsantiviralsnorovirusproteasestructure

Identifiers

PMID34696498
PMCPMC8537771
OpenAlexW3207632885

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.