ArticleProceedings of the National Academy of Sciences of the United States of America2003
Origin-specific unwinding of herpes simplex virus 1 DNA by the viral UL9 and ICP8 proteins: visualization of a specific preunwinding complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 37 citations in OpenAlex.
- Structure and mechanism of the HSV-1 origin-binding protein UL9.Journal of virology · 2026Article
- Structural insights into HSV-1 origin unwinding by the viral proteins UL9 and ICP8.Nucleic acids research · 2026Article
- The herpes simplex origin-binding protein: mechanisms for sequence-specific DNA binding and dimerization revealed by Cryo-EM.Nucleic acids research · 2025Article
- Control of HSV-1 Infection: Directions for the Development of CRISPR/Cas-Based Therapeutics and Diagnostics.International journal of molecular sciences · 2024Review
- Herpes simplex virus 1 ICP8 mutant lacking annealing activity is deficient for viral DNA replication.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The HIV Integrase Inhibitor Raltegravir Inhibits Felid Alphaherpesvirus 1 Replication by Targeting both DNA Replication and Late Gene Expression.Journal of virology · 2018Article
- Many ways to loop DNA.The Journal of biological chemistry · 2013Article
- Herpes simplex viruses: mechanisms of DNA replication.Cold Spring Harbor perspectives in biology · 2012Review
- Replication and recombination of herpes simplex virus DNA.The Journal of biological chemistry · 2011Review
- The Kaposi's sarcoma-associated herpesvirus ORF6 DNA binding protein forms long DNA-free helical protein filaments.Journal of structural biology · 2011Article
- Interaction of Kaposi's sarcoma-associated herpesvirus ORF59 with oriLyt is dependent on binding with K-Rta.Journal of virology · 2011Article
- Herpes simplex virus type 1 helicase-primase: DNA binding and consequent protein oligomerization and primase activation.Journal of virology · 2011Article
- Association between the herpes simplex virus-1 DNA polymerase and uracil DNA glycosylase.The Journal of biological chemistry · 2010Article
- Evidence for DNA hairpin recognition by Zta at the Epstein-Barr virus origin of lytic replication.Journal of virology · 2010Article
- Initiation of lytic DNA replication in Epstein-Barr virus: search for a common family mechanism.Future virology · 2010Article
- Structural and biophysical characterization of the proteins interacting with the herpes simplex virus 1 origin of replication.The Journal of biological chemistry · 2009Article
- Stepwise evolution of the herpes simplex virus origin binding protein and origin of replication.The Journal of biological chemistry · 2009Article
- The bipolar filaments formed by herpes simplex virus type 1 SSB/recombination protein (ICP8) suggest a mechanism for DNA annealing.Journal of molecular biology · 2009Article
- Kaposi's sarcoma-associated herpesvirus ori-Lyt-dependent DNA replication: involvement of host cellular factors.Journal of virology · 2008Article
- Fast-scan atomic force microscopy reveals that the type III restriction enzyme EcoP15I is capable of DNA translocation and looping.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 3 countries.
Funding
Abstract
Herpes simplex virus 1 contains three origins of replication; two copies of oriS and one of a similar sequence, oriL. Here, the combined action of multiple factors known or thought to influence the opening of oriS are examined. These include the viral origin-binding protein, UL9, and single-strand binding protein ICP8, host cell topoisomerase I, and superhelicity of the DNA template. By using electron microscopy, it was observed that when ICP8 and UL9 proteins were added together to oriS-containing supertwisted DNA, a discrete preunwinding complex was formed at oriS on 40% of the molecules, which was shown by double immunolabeling electron microscopy to contain both proteins. This complex was relatively stable to extreme dilution. Addition of ATP led to the efficient unwinding of approximately 50% of the DNA templates. Unwinding proceeded until the acquisition of a high level of positive supertwists in the remaining duplex DNA inhibited further unwinding. Addition of topoisomerase I allowed further unwinding, opening >1 kb of DNA around oriS.
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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.