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protein but facilitates its loading onto

Kelly S. Trego
Yali Zhu
Deborah S. Parris

Publication date

January 2004

Abstract

The herpes simplex virus type 1 DNA polymerase processivity factor, UL42, does not alter the catalytic activity of the UL9 origin-bindin

Extracted data

Related items

Nuclear import of HSV-1 DNA polymerase processivity factor UL42 is mediated by a C-terminally located bipartite nuclear localization signal

Alvisi, Gualtiero
Avanzi, S
Musiani, D
Camozzi, D
Leoni, V
LY HUYNH, Jd
Ripalti, A.

January 2008

The polymerase accessory protein of the human herpes simplex virus type 1 (HSV-1) DNA polymerase UL4...

Binding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: implications for the processivity mechanism

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Sinigalia, Elisa
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The mechanisms of processivity factors of herpesvirus DNA polymerases remain poorly understood. The ...

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Appleton, B. A.
Hogle, J. M.
Coen, D. M.

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The human cytomegalovirus DNA polymerase includes an accessory protein, UL44, which has been propose...

protein but facilitates its loading onto

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Yali Zhu
Deborah S. Parris

January 2004

The herpes simplex virus type 1 DNA polymerase processivity factor, UL42, does not alter the catalyt...

The effect of the UL42 protein on the DNA polymerase activity of the catalytic subunit of the DNA polymerase encoded by herpes simplex virus type 1

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AbstractThe effect that the UL42 protein of herpes simplex virus type 1 has on the DNA polymerase ac...

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Genetic and biochemical studies have shown that the products of the herpes simplex virus type 1 (HSV...

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

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William R. Bebrin
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The herpes simplex virus DNA polymerase is composed of two subunits, a large catalytic subunit (Pol)...

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Kühn, Frank J.P.
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AbstractHerpes simplex virus DNA polymerase (HSV pol) holoenzyme consists of a large catalytic (UL30...

Analysis of in Vitro Activities of Herpes Simplex Virus Type 1 UL42 Mutant Proteins: Correlation with in Vivo Function

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AbstractThe DNA polymerase (pol) catalytic subunit of herpes simplex virus type 1, encoded by UL30, ...

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January 1994

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Interaction between the Herpes Simplex Virus Type 1 Origin-Binding and DNA Polymerase Accessory Proteins

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Grinstead, Lynn A.
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February 1998

AbstractInteractions between the herpes simplex virus type 1 (HSV-1) origin (ori)-binding protein (U...

Analysis of in Vitro Activities of Herpes Simplex Virus Type 1 UL42 Mutant Proteins: Correlation with in Vivo Function

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Chaudhuri, Murari
Monahan, Steven J.
Grinstead, Lynn A.
Parris, Deborah S.

September 2000

AbstractThe DNA polymerase (pol) catalytic subunit of herpes simplex virus type 1, encoded by UL30, ...

The catalytic subunit of herpes simplex virus type 1 DNA polymerase contains a nuclear localization signal in the UL42-binding region

LOREGIAN, ARIANNA
CANCELLOTTI, ENRICO
PAPINI, EMANUELE
PIAIA E.
MARSDEN H. S.
PALU', GIORGIO

January 2000

The herpes simplex virus type 1 DNA polymerase consists of a catalytic subunit (POL or UL30) and a p...

Nuclear import of HSV-1 DNA polymerase processivity factor UL42 is mediated by a C-terminally located bipartite nuclear localization signal

Alvisi, Gualtiero
Avanzi, S
Musiani, D
Camozzi, D
Leoni, V
LY HUYNH, Jd
Ripalti, A.

January 2008

The polymerase accessory protein of the human herpes simplex virus type 1 (HSV-1) DNA polymerase UL4...

Binding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: implications for the processivity mechanism

Loregian, Arianna
Sinigalia, Elisa
Mercorelli, Beatrice
Palu', Giorgio
Coen, Dm

January 2007

The mechanisms of processivity factors of herpesvirus DNA polymerases remain poorly understood. The ...

Specific residues in the connector loop of the human cytomegalovirus DNA polymerase accessory protein, UL44, are crucial for interaction with the UL54 catalytic subunit.

Loregian, Arianna
Appleton, B. A.
Hogle, J. M.
Coen, D. M.

January 2004

The human cytomegalovirus DNA polymerase includes an accessory protein, UL44, which has been propose...

protein but facilitates its loading onto

Kelly S. Trego
Yali Zhu
Deborah S. Parris

January 2004

The herpes simplex virus type 1 DNA polymerase processivity factor, UL42, does not alter the catalyt...

The effect of the UL42 protein on the DNA polymerase activity of the catalytic subunit of the DNA polymerase encoded by herpes simplex virus type 1

Hart, Graham J.
Boehme, Richard E.

June 1992

AbstractThe effect that the UL42 protein of herpes simplex virus type 1 has on the DNA polymerase ac...

Interaction of herpes simplex virus type 1 DNA polymerase and the UL42 accessory protein with a model primer template

J. Gottlieb
M. D. Challberg

January 1994

Genetic and biochemical studies have shown that the products of the herpes simplex virus type 1 (HSV...

UL42, contains a functional protease-resistant domain

Robert K. Hamatake
Marc Bifano
Daniel J. Tenney
Warren W. Hurlburt
Michael G. Cordingleyl

July 2015

Herpes simplex virus type 1 encodes its own DNA polymerase (Pol), the product of the UL30 gene, and ...

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

Paul Digard
William R. Bebrin
Klaus Weisshart
Donald
M. Coen

January 1993

The herpes simplex virus DNA polymerase is composed of two subunits, a large catalytic subunit (Pol)...

DNA and Protein Interactions of the Small Subunit of Herpes Simplex Virus Type 1 DNA Polymerase

Franz, Cornelia
Kühn, Frank J.P.
Knopf, Charles W.

January 1999

AbstractHerpes simplex virus DNA polymerase (HSV pol) holoenzyme consists of a large catalytic (UL30...

Analysis of in Vitro Activities of Herpes Simplex Virus Type 1 UL42 Mutant Proteins: Correlation with in Vivo Function

Thornton, Keith E.
Chaudhuri, Murari
Monahan, Steven J.
Grinstead, Lynn A.
Parris, Deborah S.

September 2000

AbstractThe DNA polymerase (pol) catalytic subunit of herpes simplex virus type 1, encoded by UL30, ...

The effect of the UL42 protein on the DNA polymerase activity of the catalytic subunit of the DNA polymerase encoded by herpes simplex virus type 1

Hart, Graham J.
Boehme, Richard E.

June 1992

AbstractThe effect that the UL42 protein of herpes simplex virus type 1 has on the DNA polymerase ac...

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

H. S. Marsden
M. Murphy
G. L. Mcvey
K. A. Maceachran
A. M. Owsianka
N. D. Stow

January 1994

Several recent reports implicate sequences at or near the C terminus of the catalytic subunit (POL) ...

Interaction between the Herpes Simplex Virus Type 1 Origin-Binding and DNA Polymerase Accessory Proteins

Monahan, Steven J.
Grinstead, Lynn A.
Olivieri, Wilma
Parris, Deborah S.

February 1998

AbstractInteractions between the herpes simplex virus type 1 (HSV-1) origin (ori)-binding protein (U...

Analysis of in Vitro Activities of Herpes Simplex Virus Type 1 UL42 Mutant Proteins: Correlation with in Vivo Function

Thornton, Keith E.
Chaudhuri, Murari
Monahan, Steven J.
Grinstead, Lynn A.
Parris, Deborah S.

September 2000

AbstractThe DNA polymerase (pol) catalytic subunit of herpes simplex virus type 1, encoded by UL30, ...

The catalytic subunit of herpes simplex virus type 1 DNA polymerase contains a nuclear localization signal in the UL42-binding region

LOREGIAN, ARIANNA
CANCELLOTTI, ENRICO
PAPINI, EMANUELE
PIAIA E.
MARSDEN H. S.
PALU', GIORGIO

January 2000

The herpes simplex virus type 1 DNA polymerase consists of a catalytic subunit (POL or UL30) and a p...

Nuclear import of HSV-1 DNA polymerase processivity factor UL42 is mediated by a C-terminally located bipartite nuclear localization signal

Alvisi, Gualtiero
Avanzi, S
Musiani, D
Camozzi, D
Leoni, V
LY HUYNH, Jd
Ripalti, A.

January 2008

The polymerase accessory protein of the human herpes simplex virus type 1 (HSV-1) DNA polymerase UL4...

Binding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: implications for the processivity mechanism

Loregian, Arianna
Sinigalia, Elisa
Mercorelli, Beatrice
Palu', Giorgio
Coen, Dm

January 2007

The mechanisms of processivity factors of herpesvirus DNA polymerases remain poorly understood. The ...

Specific residues in the connector loop of the human cytomegalovirus DNA polymerase accessory protein, UL44, are crucial for interaction with the UL54 catalytic subunit.

Loregian, Arianna
Appleton, B. A.
Hogle, J. M.
Coen, D. M.

January 2004

The human cytomegalovirus DNA polymerase includes an accessory protein, UL44, which has been propose...