Novel cellular interacting partners of the human papillomavirus 16 transcription/replication factor E2. (Q52548445)

3 May 2018

title

Novel cellular interacting partners of the human papillomavirus 16 transcription/replication factor E2. (English)

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3 May 2018

main subject

human papillomavirus 16

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Winifred Boner

1

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3 May 2018

Iain M Morgan

series ordinal

2

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3 May 2018

publication date

1 December 2002

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3 May 2018

published in

Virus Research

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3 May 2018

volume

90

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3 May 2018

issue

1-2

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3 May 2018

page(s)

113-118

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3 May 2018

The PKC targeting protein RACK1 interacts with the Epstein-Barr virus activator protein BZLF1

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A Functional interaction between the human papillomavirus 16 transcription/replication factor E2 and the DNA damage response protein TopBP1

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Characterization of the human papillomavirus E2 protein: evidence of trans-activation and trans-repression in cervical keratinocytes.

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Functional interaction of a novel cellular protein with the papillomavirus E2 transactivation domain

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RACK1, a receptor for activated C kinase and a homolog of the beta subunit of G proteins, inhibits activity of src tyrosine kinases and growth of NIH 3T3 cells

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Papillomavirus E2 induces p53-independent apoptosis in HeLa cells

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Expression of human papillomavirus 16 E2 protein in Schizosaccharomyces pombe delays the initiation of mitosis

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Separate domains in E1 and E2 proteins serve architectural and productive roles for cooperative DNA binding

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The papillomavirus E2 protein: a factor with many talents

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Long-term episomal maintenance of bovine papillomavirus type 1 plasmids is determined by attachment to host chromosomes, which Is mediated by the viral E2 protein and its binding sites

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Functional analysis of the papilloma virus E2 trans-activator in Saccharomyces cerevisiae

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cAMP response element-binding protein-binding protein binds to human papillomavirus E2 protein and activates E2-dependent transcription

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Segregation of viral plasmids depends on tethering to chromosomes and is regulated by phosphorylation

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BRCT domain-containing protein TopBP1 functions in DNA replication and damage response

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Degradation of ornithine decarboxylase by the 26S proteasome

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A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A

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The influenza A virus M1 protein interacts with the cellular receptor of activated C kinase (RACK) 1 and can be phosphorylated by protein kinase C.

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RACK1 Interacts with E1A and Rescues E1A-induced Yeast Growth Inhibition and Mammalian Cell Apoptosis

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The beta4 integrin interactor p27(BBP/eIF6) is an essential nuclear matrix protein involved in 60S ribosomal subunit assembly

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The bovine papillomavirus 1 E2 protein contains two activation domains: one that interacts with TBP and another that functions after TBP binding.

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Identification of survival motor neuron as a transcriptional activator-binding protein.

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An enhanced epithelial response of a papillomavirus promoter to transcriptional activators

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7 January 2021

The human papillomavirus (HPV) 16 E2 protein induces apoptosis in the absence of other HPV proteins and via a p53-dependent pathway.

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Characterisation of the newly identified human Ump1 homologue POMP and analysis of LMP7(beta 5i) incorporation into 20 S proteasomes

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A DNA-topoisomerase-II-binding protein with eight repeating regions similar to DNA-repair enzymes and to a cell-cycle regulator

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A DNA damage-regulated BRCT-containing protein, TopBP1, is required for cell survival

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Mapping and characterization of the interaction domains of human papillomavirus type 16 E1 and E2 proteins

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Identifiers

DOI

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3 May 2018

1 reference

3 May 2018