Zobrazeno 1 - 10
of 28
pro vyhledávání: '"D. M. Milne"'
Autor:
D M Milne, C. Hogan, Caroline Hutchison, David W. Meek, John R. Goodlad, Mark K. Saville, Neil M. Kernohan, Lynnette Marcar
Publikováno v:
Journal of Biological Chemistry. 283:18012-18023
Mutation of the p53 gene is a common event during tumor pathogenesis. Other mechanisms, such as mdm2 amplification, provide alternative routes through which dysfunction of the p53 pathway is promoted. Here, we address the hypothesis that elevated exp
Publikováno v:
Molecular and Cellular Biochemistry. 274:85-90
The Murine double-minute clone 2 (Mdm2) onco-protein is the principal regulator of the tumour suppressor, p53. Mdm2 acts as an E3-type ubiquitin ligase that mediates the ubiquitylation and turnover of p53 under normal, unstressed circumstances. In re
Publikováno v:
Oncogene. 18:7602-7607
The p53 tumour suppressor protein is tightly regulated by protein-protein association, protein turnover and a variety of post-translational modifications. Multisite phosphorylation plays a major role in activating and in finely tuning p53 function. T
Publikováno v:
Biochemical Society Transactions. 25:416-419
Publikováno v:
Journal of Biological Chemistry. 270:5511-5518
The p53 tumor suppressor protein is thought to play a major role in the defense of the cell against agents that damage DNA. In this report, we describe the identification and characterization of a protein kinase that phosphorylates mouse p53 at a sin
Autor:
J. Hopkins, F. J. Bryant, G. D. Johnson, D. S. A. Sanders, Michael A. Kerr, C. A. Wilson, D. M. Milne
Publikováno v:
Gut. 35:1022-1025
Using a panel of carcinoembryonic antigen (CEA) related antibodies in normal oesophageal squamous mucosa CEA expression is present on suprabasal squames localised to the cell membrane. Immunoblotting shows that this positivity is predominantly due to
Publikováno v:
Journal of Biological Chemistry. 269:9253-9260
The p53 tumor suppressor protein is tightly regulated in the cell and is phosphorylated at multiple sites by several different protein kinases. We have investigated the phosphorylation of p53 by mitogen-activated protein (MAP) kinase, a protein kinas
Publikováno v:
Oncogene. 25(50)
The p53 tumour-suppressor protein is tightly regulated through its association with the Hdm2 E3 ligase. Activation of p53 by DNA strand breaks is orchestrated by the ataxia-telangiectasia mutated (ATM) protein kinase and involves interruption of Hdm2
Autor:
R. Kulikov, Christine Blattner, D M Milne, David W. Meek, Uwe Knippschild, Sylvia Dias, Markus Winter
Publikováno v:
Biochemistry. 43(51)
Murine double-minute clone 2 protein (MDM2) is an E3 ubiquitin ligase that regulates the turnover of several cellular factors including the p53 tumor suppressor protein. As part of the mechanism of p53 induction in response to DNA damage, a cluster o
Autor:
Samantha M. Nicol, David W. Meek, Petros Kampanis, Frances V. Fuller-Pace, Sylvia Dias, David G. Campbell, D M Milne
Publikováno v:
FEBS letters. 577(1-2)
MDM2 is an E3 ubiquitin ligase which mediates ubiquitylation and proteasome-dependent degradation of the p53 tumor suppressor protein. Phosphorylation of MDM2 by the protein kinase AKT is thought to regulate MDM2 function in response to survival sign