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In Vitro Strand Exchange Promoted by the Herpes Simplex Virus Type-1 Single Strand DNA-binding Protein (ICP8) and DNA Helicase-Primase

https://doi.org/10.1074/jbc.m109988200
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/(sici)1099-1654(199907/09)9:3<171::aid-rmv243>3.0.co;2-aopenalex-snapshot
Mechanism and application of genetic recombination in herpesviruses
inferredcites →https://doi.org/10.1002/j.1460-2075.1996.tb00552.xopenalex-snapshot
Single‐stranded DNA binding protein and DNA helicase of bacteriophage T7 mediate homologous DNA strand exchange.
inferredcites →https://doi.org/10.1006/jmbi.1993.1279openalex-snapshot
Herpes Simplex Virus 1 Single-strand DNA-binding Protein (ICP8) Will Promote Homologous Pairing and Strand Transfer
inferredcites →https://doi.org/10.1006/viro.1993.1612openalex-snapshot
Demonstration of Circularization of Herpes Simplex Virus DNA Following infection Using Pulsed Field Gel Electrophoresis
inferredcites →https://doi.org/10.1006/viro.1994.1206openalex-snapshot
Study of the Structure of Replicative Intermediates of HSV-1 DNA by Pulsed-Field Gel Electrophoresis
inferredcites →https://doi.org/10.1016/0022-2836(86)90453-5openalex-snapshot
Structure of helical RecA-DNA complexes
inferredcites →https://doi.org/10.1016/0042-6822(81)90161-6openalex-snapshot
Construction of a double-jointed herpes simplex viral DNA molecule: Inverted repeats are required for segment inversion, and direct repeats promote deletions
inferredcites →https://doi.org/10.1016/0092-8674(80)90172-5openalex-snapshot
Molecular engineering of the herpes simplex virus genome: Insertion of a second L-S junction into the genome causes additional genome inversions
inferredcites →https://doi.org/10.1016/0092-8674(88)90200-0openalex-snapshot
Inversion events in the HSV-1 genome are directly mediated by the viral DNA replication machinery and lack sequence specificity
inferredcites →https://doi.org/10.1016/0092-8674(92)90446-jopenalex-snapshot
DMC1: A meiosis-specific yeast homolog of E. coli recA required for recombination, synaptonemal complex formation, and cell cycle progression
inferredcites →https://doi.org/10.1016/0092-8674(92)90447-kopenalex-snapshot
Rad51 protein involved in repair and recombination in S. cerevisiae is a RecA-like protein
inferredcites →https://doi.org/10.1016/0092-8674(95)90057-8openalex-snapshot
Phage T4 homologous strand exchange: A DNA helicase, not the strand transferase, drives polar branch migration
inferredcites →https://doi.org/10.1016/s0021-9258(18)54063-1openalex-snapshot
The herpes simplex virus type-1 origin binding protein. DNA helicase activity.
inferredcites →https://doi.org/10.1016/s0921-8777(99)00033-6openalex-snapshot
Rad51/RecA protein families and the associated proteins in eukaryotes
inferredcites →https://doi.org/10.1016/s0959-437x(00)00059-9openalex-snapshot
Replication and recombination intersect
inferredcites →https://doi.org/10.1016/s0968-0004(00)01569-3openalex-snapshot
Initiation of genetic recombination and recombination-dependent replication
inferredcites →https://doi.org/10.1073/pnas.74.12.5463openalex-snapshot
DNA sequencing with chain-terminating inhibitors
inferredcites →https://doi.org/10.1073/pnas.78.10.6018openalex-snapshot
Directionality and polarity in recA protein-promoted branch migration.
inferredcites →https://doi.org/10.1073/pnas.79.18.5626openalex-snapshot
Herpesvirus-dependent amplification and inversion of cell-associated viral thymidine kinase gene flanked by viral a sequences and linked to an origin of viral DNA replication.
inferredcites →https://doi.org/10.1073/pnas.86.7.2186openalex-snapshot
Herpes simplex virus 1 helicase-primase: a complex of three herpes-encoded gene products.
inferredcites →https://doi.org/10.1073/pnas.90.18.8444openalex-snapshot
Physical interaction between the herpes simplex virus 1 origin-binding protein and single-stranded DNA-binding protein ICP8.
inferredcites →https://doi.org/10.1073/pnas.94.7.2987openalex-snapshot
Gene 4 helicase of bacteriophage T7 mediates strand transfer through pyrimidine dimers, mismatches, and nonhomologous regions
inferredcites →https://doi.org/10.1074/jbc.271.35.21645openalex-snapshot
The UL8 Subunit of the Herpes Simplex Virus Type-1 DNA Helicase-Primase Optimizes Utilization of DNA Templates Covered by the Homologous Single-strand DNA-binding Protein ICP8
inferredcites →https://doi.org/10.1074/jbc.272.36.22766openalex-snapshot
The UL8 Subunit of the Heterotrimeric Herpes Simplex Virus Type 1 Helicase-Primase Is Required for the Unwinding of Single Strand DNA-binding Protein (ICP8)-coated DNA Substrates
inferredcites →https://doi.org/10.1074/jbc.273.5.2676openalex-snapshot
The Herpes Simplex Virus Type-1 Single-strand DNA-binding Protein, ICP8, Increases the Processivity of the UL9 Protein DNA Helicase
inferredcites →https://doi.org/10.1074/jbc.275.15.10864openalex-snapshot
Equilibrium Binding of Single-stranded DNA with Herpes Simplex Virus Type I-coded Single-stranded DNA-binding Protein, ICP8
inferredcites →https://doi.org/10.1074/jbc.275.4.2931openalex-snapshot
Cysteine 111 Affects Coupling of Single-stranded DNA Binding to ATP Hydrolysis in the Herpes Simplex Virus Type-1 Origin-binding Protein
inferredcites →https://doi.org/10.1074/jbc.m005627200openalex-snapshot
Recombination during Early Herpes Simplex Virus Type 1 Infection Is Mediated by Cellular Proteins
inferredcites →https://doi.org/10.1074/jbc.m007219200openalex-snapshot
Modulation of the Herpes Simplex Virus Type-1 UL9 DNA Helicase by Its Cognate Single-strand DNA-binding Protein, ICP8
inferredcites →https://doi.org/10.1093/nar/16.14.6585openalex-snapshot
A DNA helicase induced by herpes simplex virus type 1
inferredcites →https://doi.org/10.1093/nar/21.8.1719openalex-snapshot
Processing of recombination intermediates by the RecG and RuvAB proteins ofEscherichia coli
inferredcites →https://doi.org/10.1093/nar/25.9.1753openalex-snapshot
Herpes simplex virus: selection of origins of DNA replication
inferredcites →https://doi.org/10.1099/0022-1317-34-2-223openalex-snapshot
In vitro Synthesis of Herpes Simplex Virus DNA in Nuclei Isolated from Infected BSC 1 Cells
inferredcites →https://doi.org/10.1099/0022-1317-34-3-507openalex-snapshot
Electron Microscopy of Herpes Simplex Virus DNA Molecules Isolated from Infected Cells by Centrifugation in CsCl Density Gradients
inferredcites →https://doi.org/10.1099/00221287-13-2-346openalex-snapshot
Recombination with Herpes Simplex Virus
inferredcites →https://doi.org/10.1101/gad.12.9.1248openalex-snapshot
RadA protein is an archaeal RecA protein homolog that catalyzes DNA strand exchange
inferredcites →https://doi.org/10.1101/gad.14.15.1971openalex-snapshot
RecE/RecT and Redα/Redβ initiate double-stranded break repair by specifically interacting with their respective partners
inferredcites →https://doi.org/10.1111/j.1432-1033.1985.tb08816.xopenalex-snapshot
Purification and some of the functions of the products of bacteriophage T4 recombination genes, uvs X and uvs Y
inferredcites →https://doi.org/10.1128/jvi.66.1.277-285.1992openalex-snapshot
Herpes simplex virus type 1 recombination: role of DNA replication and viral a sequences
inferredcites →https://doi.org/10.1128/jvi.66.2.1152-1161.1992openalex-snapshot
Association between the herpes simplex virus major DNA-binding protein and alkaline nuclease
inferredcites →https://doi.org/10.1128/jvi.67.12.6945-6949.1993openalex-snapshot
Renaturation of complementary DNA strands by herpes simplex virus type 1 ICP8
inferredcites →https://doi.org/10.1128/jvi.67.2.711-715.1993openalex-snapshot
Herpes simplex virus type 1 ICP8: helix-destabilizing properties
inferredcites →https://doi.org/10.1128/jvi.68.1.34-47.1994openalex-snapshot
Requirement for double-strand breaks but not for specific DNA sequences in herpes simplex virus type 1 genome isomerization events
inferredcites →https://doi.org/10.1128/jvi.68.6.3733-3741.1994openalex-snapshot
Herpes simplex virus type 1 recombination: the Uc-DR1 region is required for high-level a-sequence-mediated recombination
inferredcites →https://doi.org/10.1128/jvi.69.5.3084-3089.1995openalex-snapshot
Herpes simplex virus type 1 DNA replication is specifically required for high-frequency homologous recombination between repeated sequences
inferredcites →https://doi.org/10.1128/jvi.70.12.8801-8812.1996openalex-snapshot
The a sequence is dispensable for isomerization of the herpes simplex virus type 1 genome
inferredcites →https://doi.org/10.1128/jvi.70.4.2075-2085.1996openalex-snapshot
Herpes simplex virus type 1 alkaline nuclease is required for efficient processing of viral DNA replication intermediates
inferredcites →https://doi.org/10.1128/jvi.70.5.3169-3175.1996openalex-snapshot
Branched structures in the intracellular DNA of herpes simplex virus type 1
inferredcites →https://doi.org/10.1128/jvi.71.9.6842-6849.1997openalex-snapshot
Direct repeats of the herpes simplex virus a sequence promote nonconservative homologous recombination that is not dependent on XPF/ERCC4

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.3155811openalex-extracted
Crystal Structure of a New Single-Stranded DNA-Binding Protein Encoded by Staphylococcal Cassette Chromosome Elements
inferred← citeshttps://doi.org/10.1016/j.bbapap.2004.06.006openalex-snapshot
Two-dimensional crystallization of herpes simplex virus type 1 single-stranded DNA-binding protein, ICP8, on a lipid monolayer
inferred← citeshttps://doi.org/10.1016/j.bbrc.2014.10.145openalex-snapshot
Ligand induced stabilization of the melting temperature of the HSV-1 single-strand DNA binding protein using the thermal shift assay
inferred← citeshttps://doi.org/10.1016/j.jmb.2004.07.012openalex-snapshot
Catalysis of Strand Exchange by the HSV-1 UL12 and ICP8 Proteins: Potent ICP8 Recombinase Activity is Revealed upon Resection of dsDNA Substrate by Nuclease
inferred← citeshttps://doi.org/10.1016/j.str.2018.05.016openalex-snapshot
Crystal Structure of an Unusual Single-Stranded DNA-Binding Protein Encoded by Staphylococcal Cassette Chromosome Elements
inferred← citeshttps://doi.org/10.1016/j.virusres.2011.06.009openalex-snapshot
Recombination-dependent concatemeric viral DNA replication
inferred← citeshttps://doi.org/10.1016/s0079-6603(03)75005-3openalex-snapshot
Herpes Simplex Virus Type-1: A Model for Genome Transactions
inferred← citeshttps://doi.org/10.1073/pnas.1534569100openalex-snapshot
Reconstitution of recombination-dependent DNA synthesis in herpes simplex virus 1
inferred← citeshttps://doi.org/10.1073/pnas.1817642116openalex-snapshot
Herpes simplex virus 1 ICP8 mutant lacking annealing activity is deficient for viral DNA replication
inferred← citeshttps://doi.org/10.1074/jbc.m109.010413openalex-snapshot
Reconstitution of Uracil DNA Glycosylase-initiated Base Excision Repair in Herpes Simplex Virus-1
inferred← citeshttps://doi.org/10.1074/jbc.m110.131235openalex-snapshot
Association between the Herpes Simplex Virus-1 DNA Polymerase and Uracil DNA Glycosylase
inferred← citeshttps://doi.org/10.1074/jbc.m212555200openalex-snapshot
The Herpes Simplex Virus Type-1 Single-strand DNA-binding Protein (ICP8) Promotes Strand Invasion
inferred← citeshttps://doi.org/10.1074/jbc.m311658200openalex-snapshot
Specificity of the Endonuclease Activity of the Baculovirus Alkaline Nuclease for Single-stranded DNA
inferred← citeshttps://doi.org/10.1074/jbc.m503235200openalex-snapshot
The Redox State of the Baculovirus Single-stranded DNA-binding Protein LEF-3 Regulates Its DNA Binding, Unwinding, and Annealing Activities
inferred← citeshttps://doi.org/10.1074/jbc.r111.233981openalex-snapshot
Replication and Recombination of Herpes Simplex Virus DNA
inferred← citeshttps://doi.org/10.1080/15216540310001612237openalex-snapshot
The Role of DNA Recombination in Herpes Simplex Virus DNA Replication
inferred← citeshttps://doi.org/10.1093/nar/gkg740openalex-snapshot
On the mechanism of strand assimilation by the herpes simplex virus type-1 single-strand DNA-binding protein (ICP8)
inferred← citeshttps://doi.org/10.1093/nar/gkg827openalex-snapshot
ssDNA-dependent colocalization of adeno-associated virus Rep and herpes simplex virus ICP8 in nuclear replication domains
inferred← citeshttps://doi.org/10.1093/nar/gkh797openalex-snapshot
RNA binding and R-loop formation by the herpes simplex virus type-1 single-stranded DNA-binding protein (ICP8)
inferred← citeshttps://doi.org/10.1093/nar/gkw098openalex-snapshot
Homologous DNA strand exchange activity of the human mitochondrial DNA helicase TWINKLE
inferred← citeshttps://doi.org/10.1099/vir.0.80403-0openalex-snapshot
Replication, recombination and packaging of amplicon DNA in cells infected with the herpes simplex virus type 1 alkaline nuclease null mutant ambUL12
inferred← citeshttps://doi.org/10.1128/jb.184.17.4891-4905.2002openalex-snapshot
Imbroglios of Viral Taxonomy: Genetic Exchange and Failings of Phenetic Approaches
inferred← citeshttps://doi.org/10.1128/jvi.00374-12openalex-snapshot
Identification of a Divalent Metal Cation Binding Site in Herpes Simplex Virus 1 (HSV-1) ICP8 Required for HSV Replication
inferred← citeshttps://doi.org/10.1128/jvi.00994-18openalex-snapshot
The HIV Integrase Inhibitor Raltegravir Inhibits Felid Alphaherpesvirus 1 Replication by Targeting both DNA Replication and Late Gene Expression
inferred← citeshttps://doi.org/10.1128/jvi.01213-07openalex-snapshot
Herpes Simplex Virus Type 1 C-Terminal Variants of the Origin Binding Protein (OBP), OBPC-1 and OBPC-2, Cooperatively Regulate Viral DNA Levels In Vitro, and OBPC-2 Affects Mortality in Mice
inferred← citeshttps://doi.org/10.1128/jvi.02718-05openalex-snapshot
Role of the Herpes Simplex Virus Helicase-Primase Complex during Adeno-Associated Virus DNA Replication
inferred← citeshttps://doi.org/10.1128/jvi.77.13.7425-7433.2003openalex-snapshot
The Herpes Simplex Virus Type 1 Alkaline Nuclease and Single-Stranded DNA Binding Protein Mediate Strand Exchange In Vitro
inferred← citeshttps://doi.org/10.1128/jvi.77.7.4237-4247.2003openalex-snapshot
Recruitment of Polymerase to Herpes Simplex Virus Type 1 Replication Foci in Cells Expressing Mutant Primase (UL52) Proteins
inferred← citeshttps://doi.org/10.1128/jvi.78.9.4783-4796.2004openalex-snapshot
Recruitment of Cellular Recombination and Repair Proteins to Sites of Herpes Simplex Virus Type 1 DNA Replication Is Dependent on the Composition of Viral Proteins within Prereplicative Sites and Correlates with the Induction of the DNA Damage Response
inferred← citeshttps://doi.org/10.1371/journal.ppat.1002862openalex-snapshot
The HSV-1 Exonuclease, UL12, Stimulates Recombination by a Single Strand Annealing Mechanism
inferred← citeshttps://doi.org/10.5772/23548openalex-snapshot
DNA Replication Fidelity of Herpes Simplex Virus
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