ArticleProceedings of the National Academy of Sciences of the United States of America2010
Structure and inhibition of herpesvirus DNA packaging terminase nuclease domain.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. It is linked to trial NCT01767701 (A Phase II Baseline Versus Treatment Study to Determine the Efficacy of Raltegravir), which is not on this map. Cited by 78 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.
A Phase II Baseline Versus Treatment Study to Determine the Efficacy of Raltegravir (Isentress) in Preventing Progression of Relapsing Remitting Multiple Sclerosis as Determined by Gadolinium-enhanced MRI
Who cites it
78 citing papers in PubMed, 117 citations in OpenAlex.
- Something old, something new? Herpesvirus genome packaging examined in light of lessons from the tailed bacteriophages.Journal of virology · 2026Review
- Dissecting the dsDNA viral packaging machinery: structural evolution and potential for therapeutics.Journal of virology · 2026Review
- Conserved assembly architecture of the essential herpesvirus packaging accessory factor.PLoS pathogens · 2026Article
- Conserved assembly architecture of the essential herpesvirus packaging accessory factor.bioRxiv : the preprint server for biology · 2026Article
- The HCMV terminase as an antiviral target: structural insights, inhibitory mechanisms, and the era of letermovir.Frontiers in microbiology · 2026Review
- Key domains involved in the interaction and assembly of the HCMV terminase complex.Scientific reports · 2025Article
- Discovery of a Baloxavir-Inspired Endonuclease Inhibitor That Prevents Herpes Simplex Virus 1 Replication in Cell Culture and In Vivo.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Duck Plague Virus Full-Length UL15 Protein Is a Multifunctional Enzyme Which Not Only Possesses Nuclease Activity but Also Exerts ATPase and DNA-Binding Activity.Veterinary sciences · 2025Article
- Exploring the Potential of HIV Integrase Inhibitors as Therapeutic Agents Against HSV and HCMV: A Molecular Docking Study.Journal of experimental pharmacology · 2025Article
- Mechanism of Viral DNA Packaging in Phage T4 Using Single-Molecule Fluorescence Approaches.Viruses · 2024Review
- Viral Genomic DNA Packaging Machinery.Sub-cellular biochemistry · 2024Review
- Inhibiting HCMV pUL89-C Endonuclease with Metal-Binding Compounds.Journal of medicinal chemistry · 2023Review
- Identification of Small Molecule Inhibitors of Human Cytomegalovirus pUL89 Endonuclease Using Integrated Computational Approaches.Molecules (Basel, Switzerland) · 2023Article
- The viral packaging motor potentiates Kaposi's sarcoma-associated herpesvirus gene expression late in infection.PLoS pathogens · 2023Article
- Repurposing N-hydroxy thienopyrimidine-2,4-diones (HtPD) as inhibitors of human cytomegalovirus pUL89 endonuclease: Synthesis and biological characterization.Bioorganic chemistry · 2022Article
- Terminase Subunits from the Pseudomonas-Phage E217.Journal of molecular biology · 2022Article
- Viral Small Terminase: A Divergent Structural Framework for a Conserved Biological Function.Viruses · 2022Review
- 8-Hydroxy-1,6-naphthyridine-7-carboxamides as Inhibitors of Human Cytomegalovirus pUL89 Endonuclease.ChemMedChem · 2022Article
- Self-Repairing Herpesvirus Saimiri Deletion Variants.Viruses · 2022Article
- 4,5-Dihydroxypyrimidine Methyl Carboxylates, Carboxylic Acids, and Carboxamides as Inhibitors of Human Cytomegalovirus pUL89 Endonuclease.Journal of medicinal chemistry · 2022Article
18 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issuedMas, Phillipe J [corrected to Mas, Philippe J]
Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During viral replication, herpesviruses package their DNA into the procapsid by means of the terminase protein complex. In human cytomegalovirus (herpesvirus 5), the terminase is composed of subunits UL89 and UL56. UL89 cleaves the long DNA concatemers into unit-length genomes of appropriate length for encapsidation. We used ESPRIT, a high-throughput screening method, to identify a soluble purifiable fragment of UL89 from a library of 18,432 randomly truncated ul89 DNA constructs. The purified protein was crystallized and its three-dimensional structure was solved. This protein corresponds to the key nuclease domain of the terminase and shows an RNase H/integrase-like fold. We demonstrate that UL89-C has the capacity to process the DNA and that this function is dependent on Mn(2+) ions, two of which are located at the active site pocket. We also show that the nuclease function can be inactivated by raltegravir, a recently approved anti-AIDS drug that targets the HIV integrase.
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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.