ArticleBiochemistry2019
Structural and Antiviral Studies of the Human Norovirus GII.4 Protease.
Article in Biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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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.
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.
Who cites it
13 citing papers in PubMed.
- Conformational flexibility is a critical factor in designing broad-spectrum human norovirus protease inhibitors.Journal of virology · 2025Article
- High-Affinity Peptides for Target Protein Screened in Ultralarge Virtual Libraries.ACS central science · 2024Article
- Activity and cryo-EM structure of the polymerase domain of the human norovirus ProPol precursor.Journal of virology · 2024Article
- CONFORMATIONAL FLEXIBILITY IS A CRITICAL FACTOR IN DESIGNING BROAD-SPECTRUM HUMAN NOROVIRUS PROTEASE INHIBITORS.bioRxiv : the preprint server for biology · 2024Article
- Epidemiological and molecular surveillance of norovirus in the Brazilian Amazon: description of recombinant genotypes and improvement of evolutionary analysis.Revista do Instituto de Medicina Tropical de Sao Paulo · 2024Article
- Article
- Synthesis of 4'-Substituted Carbocyclic Uracil Derivatives and Their Monophosphate Prodrugs as Potential Antiviral Agents.Viruses · 2023Article
- Norovirus Protease Structure and Antivirals Development.Viruses · 2021Review
- Precursors of Viral Proteases as Distinct Drug Targets.Viruses · 2021Review
- Article
- Discovery of Immunoproteasome Inhibitors Using Large-Scale Covalent Virtual Screening.Molecules (Basel, Switzerland) · 2019Article
- GII.4 Norovirus Protease Shows pH-Sensitive Proteolysis with a Unique Arg-His Pairing in the Catalytic Site.Journal of virology · 2019Article
- Molecular Evolution of the Protease Region in Norovirus Genogroup II.Frontiers in microbiology · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors.
Funding
Abstract
Norovirus is the leading cause of acute gastroenteritis worldwide with a yearly reported 700 million cases driving a $60 billion global socioeconomic burden. With no United States Food and Drug Administration approved therapeutics and the chance for severe chronic infection and life-threatening complications, researchers have identified the protease as a potential target. However, drug development has focused on the norovirus GI.1 strain despite its accounting for less than 5% of all outbreaks. Our lab aims to change focus for norovirus drug design from GI.1 to the highly infective GII.4, responsible for more than 50% of all outbreaks worldwide. With the first published crystal structure of the norovirus GII.4 protease, we have identified several significant differences in the structure and active site that have hindered development of a potent inhibitor targeting the norovirus GII.4 protease. With these new insights, we have begun designing compounds that demonstrate increased inhibition of the clinically most relevant norovirus GII.4 strain.
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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.