Residues of human cytomegalovirus DNA polymerase catalytic subunit UL54 that are necessary and sufficient for interaction with the accessory protein UL44 (Q40377200)

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scientific article published on January 2004

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English	Residues of human cytomegalovirus DNA polymerase catalytic subunit UL54 that are necessary and sufficient for interaction with the accessory protein UL44	scientific article published on January 2004

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scholarly article

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21 December 2019

Residues of human cytomegalovirus DNA polymerase catalytic subunit UL54 that are necessary and sufficient for interaction with the accessory protein UL44 (English)

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21 December 2019

Brent A Appleton

2

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21 December 2019

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21 December 2019

author name string

Donald M Coen

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21 December 2019

Arianna Loregian

1

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21 December 2019

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publication date

1 January 2004

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21 December 2019

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10

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Journal of Virology

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21 December 2019

78

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21 December 2019

158-167

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21 December 2019

1

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21 December 2019

Inhibition of human cytomegalovirus DNA polymerase by C-terminal peptides from the UL54 subunit

1 reference

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Identification of crucial hydrogen-bonding residues for the interaction of herpes simplex virus DNA polymerase subunits via peptide display, mutational, and calorimetric approaches

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The crystal structure of an unusual processivity factor, herpes simplex virus UL42, bound to the C terminus of its cognate polymerase

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Open reading frames UL44, IRS1/TRS1, and UL36-38 are required for transient complementation of human cytomegalovirus oriLyt-dependent DNA synthesis.

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Sequences at the C-terminus of the herpes simplex virus type 1 UL30 protein are dispensable for DNA polymerase activity but not for viral origin-dependent DNA replication

1 reference

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22 September 2017

Mutations in the C terminus of herpes simplex virus type 1 DNA polymerase can affect binding and stimulation by its accessory protein UL42 without affecting basal polymerase activity.

1 reference

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22 September 2017

The extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replication.

1 reference

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22 September 2017

Eleven loci encoding trans-acting factors are required for transient complementation of human cytomegalovirus oriLyt-dependent DNA replication.

1 reference

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22 September 2017

Cytomegalovirus-mediated induction of antisense mRNA expression to UL44 inhibits virus replication in an astrocytoma cell line: identification of an essential gene

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22 September 2017

Specific inhibition of herpes simplex virus DNA polymerase by helical peptides corresponding to the subunit interface

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22 September 2017

Sequence and transcription analysis of the human cytomegalovirus DNA polymerase gene

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22 September 2017

Genomic localization, sequence analysis, and transcription of the putative human cytomegalovirus DNA polymerase gene

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22 September 2017

Human cytomegalovirus-induced DNA polymerase and its interaction with the triphosphates of 1-(2'-deoxy-2'-fluoro-beta-D-arabinofuranosyl)-5-methyluracil, -5-iodocytosine, and -5-methylcytosine

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Purification of the herpes simplex virus type 1 65-kilodalton DNA-binding protein: properties of the protein and evidence of its association with the virus-encoded DNA polymerase.

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22 September 2017

The herpes simplex virus type 1 UL42 gene product: a subunit of DNA polymerase that functions to increase processivity

1 reference

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22 September 2017

Physical and functional interaction of human cytomegalovirus DNA polymerase and its accessory protein (ICP36) expressed in insect cells

1 reference

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Role of the carboxy terminus of herpes simplex virus type 1 DNA polymerase in its interaction with UL42.

1 reference

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25 September 2017

Expression of the catalytic subunit (UL54) and the accessory protein (UL44) of human cytomegalovirus DNA polymerase in a coupled in vitro transcription/translation system

1 reference

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A novel functional domain of an alpha-like DNA polymerase. The binding site on the herpes simplex virus polymerase for the viral UL42 protein

1 reference

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High level expression of DNA polymerases from herpesviruses

1 reference

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15 June 2018

The herpes simplex virus processivity factor, UL42, binds DNA as a monomer

1 reference

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20 August 2018

The herpes simplex virus type 1 DNA polymerase accessory protein, UL42, contains a functional protease-resistant domain

1 reference

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20 August 2018

Functional analysis of human cytomegalovirus polymerase accessory protein.

1 reference

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20 August 2018

Identifiers

10.1128/JVI.78.1.158-167.2004

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21 December 2019

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Europe PubMed Central

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21 December 2019

1 reference

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21 December 2019

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