Fast, qualitative analysis of p53 phosphorylation by protein kinases

BioTechniques

Volumn 28, Issue 2, 2000, Pages 240-242

  Chène, Patrick ^a  

^a NOVARTIS PHARMA AG   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; ENZYME ACTIVITY; HUMAN; PROTEIN DETERMINATION; PROTEIN PHOSPHORYLATION; SIGNAL PROCESSING; TRANSCRIPTION REGULATION; TUMOR SUPPRESSOR GENE;

ANIMALS; BIOTECHNOLOGY; CASEIN KINASE II; CATALYTIC DOMAIN; GENES, P53; MUTATION; PHOSPHORYLATION; PROTEIN-SERINE-THREONINE KINASES; RABBITS; RECOMBINANT PROTEINS; RETICULOCYTES; SUBSTRATE SPECIFICITY; TUMOR SUPPRESSOR PROTEIN P53;

EID: 0342615062     PISSN: 07366205     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (5)

1. Appel, K., P. Wagner, B. Boldyreff, O.G. Issinger and M. Montenarh. 1995. Mapping of the interaction sites of the growth suppressor protein p53 with the regulatory beta-subunit of protein kinase CK2. Oncogene 11:1971-1978.
2. Götz, C., P. Scholtes, A. Prowald, N. Schuster, W. Nastainczyk and M. Montenarh. 1999. Protein kinase CK2 interacts with a multi-protein binding domain of p53. Mol. Cell. Biochem. 191:111-120.
3. Meek, D.W. 1998. New developments in the multi-site phosphorylation and integration of stress signaling at p53. Int. J. Radiat. Biol. 74:729-737.
4. Meek, D.W., S. Simon, U. Kikkawa and W. Eckhart. 1990. The p53 tumour suppressor protein is phosphorylated at serine 389 by casein kinase II. EMBO J. 9:3253-3260.
5. Rollenhagen, C. and P. Chene. 1998. Characterization of p53 mutants identified in human tumors with a missense mutation in the tetramerization domain. Int. J. Cancer 78:372-376.