Literature DB >> 2981725

Relationship of phosphorylation to the oligomerization of SV40 T antigen and its association with p53.

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.

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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


  2 in total

1.  Complex formation of simian virus 40 large T antigen with cellular protein p53.

Authors:  M Montenarh; M Kohler; R Henning
Journal:  J Virol       Date:  1986-11       Impact factor: 5.103

2.  Linker insertion mutants of simian virus 40 large T antigen that show trans-dominant interference with wild-type large T antigen map to multiple sites within the T-antigen gene.

Authors:  J Y Zhu; C N Cole
Journal:  J Virol       Date:  1989-11       Impact factor: 5.103

  2 in total

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