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- W2103487477 endingPage "11475" @default.
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- W2103487477 abstract "ABSTRACT Human cytomegalovirus (HCMV) encodes several proteins that can modulate components of the cell cycle machinery. The UL123 gene product, IE1-72, binds the Rb-related, p107 protein and relieves its repression of E2F-responsive promoters; however, it is unable to induce quiescent cells to enter S phase in wild-type ( p53 +/+ ) cells. IE1-72 also induces p53 accumulation through an unknown mechanism. We present here evidence suggesting that IE1-72 may activate the p53 pathway by increasing the levels of p19 Arf and by inducing the phosphorylation of p53 at Ser15. Phosphorylation of this residue by IE1-72 expression alone or HCMV infection is found to be dependent on the ataxia-telangiectasia mutated kinase. IE2-86 expression leads to p53 phosphorylation and may contribute to this phenotype in HCMV-infected cells. We also found that IE1-72 promotes p53 nuclear accumulation by abrogating p53 nuclear shuttling. These events result in the stimulation of p53 activity, leading to a p53- and p21-dependent inhibition of cell cycle progression from G 1 to S phase in cells transiently expressing IE1-72. Thus, like many of the small DNA tumor viruses, the first protein expressed upon HCMV infection activates a p53 response by the host cell." @default.
- W2103487477 created "2016-06-24" @default.
- W2103487477 creator A5007765169 @default.
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- W2103487477 creator A5069624995 @default.
- W2103487477 creator A5069800498 @default.
- W2103487477 date "2005-09-01" @default.
- W2103487477 modified "2023-10-03" @default.
- W2103487477 title "Human Cytomegalovirus IE1-72 Activates Ataxia Telangiectasia Mutated Kinase and a p53/p21-Mediated Growth Arrest Response" @default.
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- W2103487477 doi "https://doi.org/10.1128/jvi.79.17.11467-11475.2005" @default.
- W2103487477 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1193638" @default.
- W2103487477 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16103197" @default.
- W2103487477 hasPublicationYear "2005" @default.
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