Phosphorylation of SV40 large T antigen at threonine residues results in conversion to a lower apparent molecular weight form-Reference-Cited by-同舟云学术

Phosphorylation of SV40 large T antigen at threonine residues results in conversion to a lower apparent molecular weight form

Published:1992-03 Issue:1-4 Volume:126 Page:313-320
ISSN:0304-8608
Container-title:Archives of Virology
language:en
Short-container-title:Archives of Virology

Author:

Gr�sser F. A.,K�nig S.

Publisher

Springer Science and Business Media LLC

Subject

Virology,General Medicine

Link

http://link.springer.com/content/pdf/10.1007/BF01309704.pdf

Reference27 articles.

1. Baumann EA (1985) DNA-binding properties of phosphorylated and dephosphorylated D2-T antigen, a simian-virus-40 T-antigen-related protein. Eur J Biochem 147: 495?501

2. Butel JS (1986) SV40 large T-antigen: dual oncogene. Cancer Surv 5: 343?365

3. Chen YR, Lees-Miller SP, Tegtmeyer P, Anderson CW (1991) The human DNA-activated protein kinase phosphorylates simian virus 40 T antigen at amino-and carboxy-terminal sites. J Virol 65: 5131?5140

4. DePamphilis ML, Bradley MK (1986) Replication of SV40 and polyoma virus chromosomes. In: Salzmann NP (ed) The papovaviridae. Plenum Press, New York, pp 929?946

5. Gluzman Y, Reichl H, Solnick D (1982) Helper-free adenovirus type-5 vectors. In: Gluzman Y (ed) Eucaryotic viral vectors. Cold Sping Harbor, New York, pp 187?192

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