(Q34471081)

English

Helicase motif Ia is involved in single-strand DNA-binding and helicase activities of the herpes simplex virus type 1 origin-binding protein, UL9.

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

Helicase motif Ia is involved in single-strand DNA-binding and helicase activities of the herpes simplex virus type 1 origin-binding protein, UL9. (English)

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

Herpes simplex virus type 1

1 reference

based on heuristic

inferred from title

author name string

Boriana Marintcheva

1

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

Sandra K Weller

2

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

language of work or name

0 references

publication date

1 February 2003

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

Journal of Virology

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

77

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

4

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

2477-2488

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

Modularity and specialization in superfamily 1 and 2 helicases

1 reference

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6 July 2018

Helicase structure and mechanism

1 reference

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CDD: a database of conserved domain alignments with links to domain three-dimensional structure

1 reference

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A tale of two HSV-1 helicases: roles of phage and animal virus helicases in DNA replication and recombination

1 reference

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Defining the roles of individual residues in the single-stranded DNA binding site of PcrA helicase

1 reference

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6 July 2018

Residues within the conserved helicase motifs of UL9, the origin-binding protein of herpes simplex virus-1, are essential for helicase activity but not for dimerization or origin binding activity

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=141079

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DNA helicases: 'inching forward'.

1 reference

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Helicase motifs: the engine that powers DNA unwinding

1 reference

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Structure-based mutagenesis study of hepatitis C virus NS3 helicase

1 reference

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Simple version of "megaprimer" PCR for site-directed mutagenesis

1 reference

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Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism

1 reference

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Site-directed mutagenesis of the AcMNPV p143 gene: effects on baculovirus DNA replication

1 reference

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The nucleoside triphosphatase and helicase activities of vaccinia virus NPH-II are essential for virus replication

1 reference

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Comparisons between the structures of HCV and Rep helicases reveal structural similarities between SF1 and SF2 super-families of helicases

1 reference

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Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding

1 reference

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Interaction between the herpes simplex virus type 1 origin-binding and DNA polymerase accessory proteins

1 reference

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Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP

1 reference

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Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

1 reference

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Biochemical analyses of mutations in the HSV-1 helicase-primase that alter ATP hydrolysis, DNA unwinding, and coupling between hydrolysis and unwinding

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=141079

6 July 2018

Use of transdominant mutants of the origin-binding protein (UL9) of herpes simplex virus type 1 to define functional domains.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=141079

6 July 2018

Intracellular localization of the herpes simplex virus type-1 origin binding protein, UL9.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=141079

6 July 2018

The origin-binding domain of the herpes simplex virus type 1 UL9 protein is not required for DNA helicase activity

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=141079

6 July 2018

Thermosensitive UL9 gene function is required for early stages of herpes simplex virus type 1 DNA synthesis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=141079

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A double-filter method for nitrocellulose-filter binding: application to protein-nucleic acid interactions

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=141079

6 July 2018

Physical interaction between the herpes simplex virus 1 origin-binding protein and single-stranded DNA-binding protein ICP8.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=141079

6 July 2018

A mutational analysis of the DNA-binding domain of the herpes simplex virus type 1 UL9 protein

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=141079

6 July 2018

The herpes simplex virus type 1 origin-binding protein interacts specifically with the viral UL8 protein

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=141079

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RNA helicase activity of the plum pox potyvirus CI protein expressed in Escherichia coli. Mapping of an RNA binding domain

1 reference

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Genetic analysis of temperature-sensitive mutants which define the gene for the major herpes simplex virus type 1 DNA-binding protein

1 reference

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Isolation and characterization of herpes simplex virus type 1 host range mutants defective in viral DNA synthesis

1 reference

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Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes

1 reference

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The herpes simplex virus 1 origin binding protein: a DNA helicase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=141079

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The conserved helicase motifs of the herpes simplex virus type 1 origin-binding protein UL9 are important for function

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=141079

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Genetic analysis of the herpes simplex virus type 1 UL9 gene: isolation of a LacZ insertion mutant and expression in eukaryotic cells

1 reference

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Purification and characterization of UL9, the herpes simplex virus type 1 origin-binding protein

1 reference

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An improved assay for nanomole amounts of inorganic phosphate

1 reference

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Inhibition of herpes simplex virus type 1 DNA replication by mutant forms of the origin-binding protein

1 reference

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Helicase motifs V and VI of the Escherichia coli UvrB protein of the UvrABC endonuclease are essential for the formation of the preincision complex.

1 reference

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The RNA helicase CI from plum pox potyvirus has two regions involved in binding to RNA

1 reference

https://pubmed.ncbi.nlm.nih.gov/12551986

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1128/JVI.77.4.2477-2488.2003

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

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