ReviewOpen biology2021
The three-component helicase/primase complex of herpes simplex virus-1.
Review in Open biology, 2021. 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
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.
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
22 citing papers in PubMed, 33 citations in OpenAlex.
- Genomic comparison reveals single-nucleotide polymorphic sites and attenuation-associated site combinations specific to Chinese live attenuated varicella-zoster virus vaccines.Human vaccines & immunotherapeutics · 2026Article
- DNA damage responses in HCMV infection: emerging mechanisms and outstanding questions.Journal of virology · 2026Review
- Motif V is an allosteric couple between the SARS-CoV-2 nsp13 nucleotide triphosphatase and helicase active sites.The Journal of biological chemistry · 2026Article
- Structure, Function and Inhibition of Helicases Involved in Virus Infection.Biomolecules · 2026Review
- Article
- Mechanisms of HSV-1 helicase-primase inhibition and replication fork complex assembly.bioRxiv : the preprint server for biology · 2025Article
- Structural and mechanistic insights into the herpes simplex virus type 1 helicase-primase primosome.Cell discovery · 2025Article
- Structural and mechanistic insights into herpesvirus helicase-primase and its therapeutic inhibitors.Nature microbiology · 2025Article
- Endogenized polinton-like viruses in the dinoflagellateThe Journal of general virology · 2025Article
- In vitro antiviral efficacy of amenamevir against feline herpesvirus 1.The Journal of veterinary medical science · 2025Article
- Review
- A proteome-wide structural systems approach reveals insights into protein families of all human herpesviruses.Nature communications · 2024Article
- Control of HSV-1 Infection: Directions for the Development of CRISPR/Cas-Based Therapeutics and Diagnostics.International journal of molecular sciences · 2024Review
- Article
- Article
- Clinical Application of Metagenomic Next-Generation Sequencing (mNGS) in Patients with Early Pulmonary Infection After Liver Transplantation.Infection and drug resistance · 2024Article
- Viral replication organelles: the highly complex and programmed replication machinery.Frontiers in microbiology · 2024Review
- Primase-polymerases: how to make a primer from scratch.Bioscience reports · 2023Review
- A Comprehensive Overview of Epidemiology, Pathogenesis and the Management of Herpes Labialis.Viruses · 2023Review
- Discovery, Chemistry, and Preclinical Development of Pritelivir, a Novel Treatment Option for Acyclovir-Resistant Herpes Simplex Virus Infections.Journal of medicinal chemistry · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Herpes simplex virus type 1 (HSV-1) is one of the nine herpesviruses that infect humans. HSV-1 encodes seven proteins to replicate its genome in the hijacked human cell. Among these are the herpes virus DNA helicase and primase that are essential components of its replication machinery. In the HSV-1 replisome, the helicase-primase complex is composed of three components including UL5 (helicase), UL52 (primase) and UL8 (non-catalytic subunit). UL5 and UL52 subunits are functionally interdependent, and the UL8 component is required for the coordination of UL5 and UL52 activities proceeding in opposite directions with respect to the viral replication fork. Anti-viral compounds currently under development target the functions of UL5 and UL52. Here, we review the structural and functional properties of the UL5/UL8/UL52 complex and highlight the gaps in knowledge to be filled to facilitate molecular characterization of the structure and function of the helicase-primase complex for development of alternative anti-viral treatments.
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What OpenQuestion holds
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.