| Literature DB >> 2981725 |
H W Stürzbecher, M Mörike, M Montenarh, R Henning.
Abstract
The potential significance of the phosphorylation of SV40 large T antigen for oligomers and complexes with the cellular protein p53 was investigated. We observed that T antigen oligomers remain stable after enzymatic dephosphorylation by alkaline phosphatase up to 80%. Separate analysis of free and p53-bound T antigen revealed a considerably lower phosphorylation of the p53-bound subclass. Therefore, a simple correlation between the overall phosphorylation of T antigen and the formation of oligomers and T-p53 complexes is highly unlikely.Entities:
Mesh:
Substances:
Year: 1985 PMID: 2981725 DOI: 10.1016/0014-5793(85)81087-5
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124