ArticleAntimicrobial agents and chemotherapy2011
Identification of protein-protein interaction inhibitors targeting vaccinia virus processivity factor for development of antiviral agents.
Article in Antimicrobial agents and chemotherapy, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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Who cites it
16 citing papers in PubMed, 21 citations in OpenAlex.
- Article
- Identification of core therapeutic targets for Monkeypox virus and repurposing potential of drugs: A WEB prediction approach.PloS one · 2024Article
- Correlated Target Search by Vaccinia Virus Uracil-DNA Glycosylase, a DNA Repair Enzyme and a Processivity Factor of Viral Replication Machinery.International journal of molecular sciences · 2023Article
- Review
- A 3D structural SARS-CoV-2-human interactome to explore genetic and drug perturbations.Nature methods · 2021Article
- A New Class of Uracil-DNA Glycosylase Inhibitors Active against Human and Vaccinia Virus Enzyme.Molecules (Basel, Switzerland) · 2021Article
- Inhibitors of DNA Glycosylases as Prospective Drugs.International journal of molecular sciences · 2020Review
- Mutation and structure guided discovery of an antiviral small molecule that mimics an essential C-Terminal tripeptide of the vaccinia D4 processivity factor.Antiviral research · 2019Article
- Defining Pharmacological Targets by Analysis of Virus-Host Protein Interactions.Advances in protein chemistry and structural biology · 2018Review
- The French Armed Forces Virology Unit: A Chronological Record of Ongoing Research on Orthopoxvirus.Viruses · 2017Review
- The vaccinia virus DNA polymerase and its processivity factor.Virus research · 2017Review
- Poxvirus uracil-DNA glycosylase-An unusual member of the family I uracil-DNA glycosylases.Protein science : a publication of the Protein Society · 2016Review
- Structural analysis of point mutations at the Vaccinia virus A20/D4 interface.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Crystal structure of the vaccinia virus DNA polymerase holoenzyme subunit D4 in complex with the A20 N-terminal domain.PLoS pathogens · 2014Article
- Design of potent poxvirus inhibitors of the heterodimeric processivity factor required for viral replication.Journal of medicinal chemistry · 2013Article
- Orthopoxvirus targets for the development of new antiviral agents.Antiviral research · 2012Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Poxvirus uracil DNA glycosylase D4 in association with A20 and the catalytic subunit of DNA polymerase forms the processive polymerase complex. The binding of D4 and A20 is essential for processive polymerase activity. Using an AlphaScreen assay, we identified compounds that inhibit protein-protein interactions between D4 and A20. Effective interaction inhibitors exhibited both antiviral activity and binding to D4. These results suggest that novel antiviral agents that target the protein-protein interactions between D4 and A20 can be developed for the treatment of infections with poxviruses, including smallpox.
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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.