In GFP with high risk HPV-18E6 fusion protein expressed 293T and MCF-7 cells, the endogenous wild-type p53 could be transiently phosphorylated at multiple sites
نویسندگان
چکیده
منابع مشابه
In GFP with high risk HPV-18E6 fusion protein expressed 293T and MCF-7 cells, the endogenous wild-type p53 could be transiently phosphorylated at multiple sites
BACKGROUND Infected cells recognize viral replication as a DNA damage stress and elicit the host surveillance mechanism to anti-virus infection. Modulation of the activity of tumor suppressor p53 is a key event in the replication of many viruses. They could manipulate p53 function through phosphorylation modification for their own purpose. But there is rarely research about p53 phosphorylation ...
متن کاملGFP/HPV-16E6 fusion protein induces apoptosis in MCF-7 and 293T cells using a transient expression system.
Since mucosal high-risk human papillomavirus (HPV) E6 can target and degrade the tumor suppressor p53, it is recognized as a major causative agent of cervical cancer. However, to date the distribution of high-risk HPV-E6 protein remains elusive. Thus, in the present study we used a mammalian green fluorescent protein (GFP) expression system to exp...
متن کاملHPV-16E6 can induce multiple site phosphorylation of p53.
Modulation of the activity of tumor suppressor p53 is a key event in the replication of many viruses. They could manipulate p53 function through modification of phosphorylation for their own purpose. However, there are scarce data on the relationship between high risk human papillomavirus (HPV) E6 protein and p53 phosphorylation status. Therefore, we used a mammalian green fluorescence protein ...
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Production and Evaluation of Polyclonal Rabbit Anti-Human p53 Antibody Using Bacterially Expressed Glutathione S-transferase-p53 fusion protein
p53 is a key tumor suppressor gene that is targeted for inactivation during human tumorigenesis. In this study, we produced and characterized polyclonal antihuman p53 antibody. The cDNA encoding the completehuman p53 protein was cloned into pGEX-4T-1 and expressed in Escherichia coli as a fusion protein with Schistosoma japonicum glutathione S-transferase (GST). The rabbits were immunized...
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ژورنال
عنوان ژورنال: Journal of Experimental & Clinical Cancer Research
سال: 2008
ISSN: 1756-9966
DOI: 10.1186/1756-9966-27-35