ArticleVirus research2013
Structural and inhibitor studies of norovirus 3C-like proteases.
Article in Virus research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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.
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Who cites it
22 citing papers in PubMed, 33 citations in OpenAlex.
- Article
- SARS-CoV-2 MSLAS discovery : advancing life sciences R & D · 2024Article
- Development of FRET and Stress Granule Dual-Based System to Screen for Viral 3C Protease Inhibitors.Molecules (Basel, Switzerland) · 2023Article
- Adaptive Mutation in the Main Protease Cleavage Site of Feline Coronavirus Renders the Virus More Resistant to Main Protease Inhibitors.Journal of virology · 2022Article
- Norovirus Protease Structure and Antivirals Development.Viruses · 2021Review
- Considerations for the discovery and development of 3-chymotrypsin-like cysteine protease inhibitors targeting SARS-CoV-2 infection.Current opinion in virology · 2021Review
- Dual inhibition of SARS-CoV-2 and human rhinovirus with protease inhibitors in clinical development.Antiviral research · 2021Article
- Evaluation of SARS-CoV-2 3C-like protease inhibitors using self-assembled monolayer desorption ionization mass spectrometry.Antiviral research · 2020Article
- Norovirus antivirals: Where are we now?Medicinal research reviews · 2019Review
- Structural and Antiviral Studies of the Human Norovirus GII.4 Protease.Biochemistry · 2019Article
- Fexaramine as an entry blocker for feline caliciviruses.Antiviral research · 2018Article
- Expression, Purification and Characterization of a GII.4 Norovirus Protease from Minerva Virus.Infectious disorders drug targets · 2018Article
- Therapeutics and Immunoprophylaxis Against Noroviruses and Rotaviruses: The Past, Present, and Future.Current drug metabolism · 2018Review
- Structure-based design and synthesis of triazole-based macrocyclic inhibitors of norovirus protease: Structural, biochemical, spectroscopic, and antiviral studies.European journal of medicinal chemistry · 2016Article
- Current tools for norovirus drug discovery.Expert opinion on drug discovery · 2016Review
- Long-Range Communication between Different Functional Sites in the Picornaviral 3C Protein.Structure (London, England : 1993) · 2016Article
- Potent inhibition of enterovirus D68 and human rhinoviruses by dipeptidyl aldehydes and α-ketoamides.Antiviral research · 2016Article
- A Cell-based Fluorescence Resonance Energy Transfer (FRET) Sensor Reveals Inter- and Intragenogroup Variations in Norovirus Protease Activity and Polyprotein Cleavage.The Journal of biological chemistry · 2015Article
- Structure-guided design and optimization of dipeptidyl inhibitors of norovirus 3CL protease. Structure-activity relationships and biochemical, X-ray crystallographic, cell-based, and in vivo studies.Journal of medicinal chemistry · 2015Article
- Norovirus: targets and tools in antiviral drug discovery.Biochemical pharmacology · 2014Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Noroviruses have a single-stranded, positive sense 7-8kb RNA genome, which encodes a polyprotein precursor processed by a virus-encoded 3C-like cysteine protease (3CLpro) to generate mature non-structural proteins. Because processing of the polyprotein is essential for virus replication, norovirus 3CLpro has been targeted for the discovery of anti-norovirus small molecule therapeutics. Thus, we performed functional, structural and inhibition studies of norovirus 3CLpro with fluorescence resonance energy transfer (FRET) assay, X-ray crystallography, and NMR spectroscopy with a synthetic protease inhibitor. Three 3CLpro from Norwalk virus (NV, genogroup I), MD145 (genogroup II) and murine norovirus-1 (MNV-1, genogroup V) were optimized for a FRET assay, and compared for the inhibitory activities of a synthetic protease inhibitor (GC376). The apo 3D structures of NV 3CLpro determined with X-ray crystallography and NMR spectroscopy were further analyzed. In addition, the binding mode of NV 3CLpro-GC376 was compared with X-ray crystallography and NMR spectroscopy. The results of this report provide insight into the interaction of NV 3CLpro with substrate/inhibitor for better understanding of the enzyme and antiviral drug development.
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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.