An acidic amphipathic helix in the Bovine Papillomavirus E2 protein is critical for DNA replication and interaction with the E1 protein. (Q51820242)

13 April 2018

title

An acidic amphipathic helix in the Bovine Papillomavirus E2 protein is critical for DNA replication and interaction with the E1 protein. (English)

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13 April 2018

author

Alison A. McBride

series ordinal

2

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13 April 2018

author name string

Michael K Baxter

series ordinal

1

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13 April 2018

language of work or name

English

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publication date

1 February 2005

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13 April 2018

published in

Virology

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13 April 2018

volume

332

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13 April 2018

issue

1

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13 April 2018

page(s)

78-88

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13 April 2018

The X-ray structure of the papillomavirus helicase in complex with its molecular matchmaker E2.

cites work

1 reference

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Structure of the intact transactivation domain of the human papillomavirus E2 protein

7 January 2021

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The mitotic chromosome binding activity of the papillomavirus E2 protein correlates with interaction with the cellular chromosomal protein, Brd4.

7 January 2021

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Identification of Single Amino Acids in the Human Papillomavirus 11 E2 Protein Critical for the Transactivation or Replication Functions

7 January 2021

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The acidic transcriptional activation domains of VP16 and p53 bind the cellular replication protein A and stimulate in vitro BPV-1 DNA replication

7 January 2021

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Acidic transcription factors alleviate nucleosome-mediated repression of DNA replication of bovine papillomavirus type 1.

7 January 2021

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E2 polypeptides encoded by bovine papillomavirus type 1 form dimers through the common carboxyl-terminal domain: transactivation is mediated by the conserved amino-terminal domain

7 January 2021

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Targeting the E1 replication protein to the papillomavirus origin of replication by complex formation with the E2 transactivator

7 January 2021

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Domains of the BPV-1 E1 Replication Protein Required for Origin-Specific DNA Binding and Interaction with the E2 Transactivator

7 January 2021

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Bovine papilloma virus (BPV)-encoded E2 protein enhances binding of E1 protein to the BPV replication origin.

7 January 2021

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Binding of bovine papillomavirus E1 to the origin is not sufficient for DNA replication

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A novel technique with enhanced detection and quantitation of HPV-16 E1- and E2-mediated DNA replication

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DNA replicative functions of highly-expressed, codon-optimized human papillomavirus proteins E1 and E2.

7 January 2021

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The transactivation and DNA binding domains of the BPV-1 E2 protein have different roles in cooperative origin binding with the E1 protein

7 January 2021

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Transcriptional and replicational activation functions in the bovine papillomavirus type 1 E2 protein are encoded by different structural determinants.

7 January 2021

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Amino acids critical for the functions of the bovine papillomavirus type 1 E2 transactivator

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Genetic analysis of the activation domain of bovine papillomavirus protein E2: its role in transcription and replication.

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A fifteen-amino-acid peptide inhibits human papillomavirus E1-E2 interaction and human papillomavirus DNA replication in vitro

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Identifiers

DOI

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13 April 2018

release_ydxtow76lzhvlfktk32kzhezha

Fatcat ID

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Fatcat

https://api.fatcat.wiki/v0/release/ydxtow76lzhvlfktk32kzhezha

24 November 2022

mapped directly with Wikidata item

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13 April 2018