Advanced search
1 file | 240.04 KB Add to list

Mdm2-mediated ubiquitylation: p53 and beyond

Author
Organization
Abstract
The really interesting genes (RING)-finger-containing oncoprotein, Mdm2, is a promising drug target for cancer therapy. A key Mdm2 function is to promote ubiquitylation and proteasomal-dependent degradation of the tumor suppressor protein p53. Recent reports provide novel important insights into Mdm2-mediated regulation of p53 and how the physical and functional interactions between these two proteins are regulated. Moreover, a p53-independent role of Mdm2 has recently been confirmed by genetic data. These advances and their potential implications for the development of new cancer therapeutic strategies form the focus of this review. Cell Death and Differentiation (2010) 17, 93-102; doi:10.1038/cdd.2009.68; published online 5 June 2009
Keywords
ubiquitylation, p53, cancer therapy, P53-DEPENDENT MANNER, P53-MDM2 FEEDBACK LOOP, UBIQUITIN LIGASE ACTIVITY, SOFT-TISSUE SARCOMAS, LI-FRAUMENI-SYNDROME, DNA-DAMAGE, IN-VIVO, NUCLEAR EXPORT, MDM2, RING DOMAIN, PROTEASOMAL DEGRADATION

Downloads

  • (...).pdf
    • full text
    • |
    • UGent only
    • |
    • PDF
    • |
    • 240.04 KB

Citation

Please use this url to cite or link to this publication:

MLA
Marine, Jean-Christophe, and G Lozano. “Mdm2-mediated Ubiquitylation: P53 and Beyond.” CELL DEATH AND DIFFERENTIATION 17.1 (2010): 93–102. Print.
APA
Marine, J.-C., & Lozano, G. (2010). Mdm2-mediated ubiquitylation: p53 and beyond. CELL DEATH AND DIFFERENTIATION, 17(1), 93–102.
Chicago author-date
Marine, Jean-Christophe, and G Lozano. 2010. “Mdm2-mediated Ubiquitylation: P53 and Beyond.” Cell Death and Differentiation 17 (1): 93–102.
Chicago author-date (all authors)
Marine, Jean-Christophe, and G Lozano. 2010. “Mdm2-mediated Ubiquitylation: P53 and Beyond.” Cell Death and Differentiation 17 (1): 93–102.
Vancouver
1.
Marine J-C, Lozano G. Mdm2-mediated ubiquitylation: p53 and beyond. CELL DEATH AND DIFFERENTIATION. 2010;17(1):93–102.
IEEE
[1]
J.-C. Marine and G. Lozano, “Mdm2-mediated ubiquitylation: p53 and beyond,” CELL DEATH AND DIFFERENTIATION, vol. 17, no. 1, pp. 93–102, 2010.
@article{927203,
  abstract     = {The really interesting genes (RING)-finger-containing oncoprotein, Mdm2, is a promising drug target for cancer therapy. A key Mdm2 function is to promote ubiquitylation and proteasomal-dependent degradation of the tumor suppressor protein p53. Recent reports provide novel important insights into Mdm2-mediated regulation of p53 and how the physical and functional interactions between these two proteins are regulated. Moreover, a p53-independent role of Mdm2 has recently been confirmed by genetic data. These advances and their potential implications for the development of new cancer therapeutic strategies form the focus of this review. Cell Death and Differentiation (2010) 17, 93-102; doi:10.1038/cdd.2009.68; published online 5 June 2009},
  author       = {Marine, Jean-Christophe and Lozano, G},
  issn         = {1350-9047},
  journal      = {CELL DEATH AND DIFFERENTIATION},
  keywords     = {ubiquitylation,p53,cancer therapy,P53-DEPENDENT MANNER,P53-MDM2 FEEDBACK LOOP,UBIQUITIN LIGASE ACTIVITY,SOFT-TISSUE SARCOMAS,LI-FRAUMENI-SYNDROME,DNA-DAMAGE,IN-VIVO,NUCLEAR EXPORT,MDM2,RING DOMAIN,PROTEASOMAL DEGRADATION},
  language     = {eng},
  number       = {1},
  pages        = {93--102},
  title        = {Mdm2-mediated ubiquitylation: p53 and beyond},
  url          = {http://dx.doi.org/10.1038/cdd.2009.68},
  volume       = {17},
  year         = {2010},
}

Altmetric
View in Altmetric
Web of Science
Times cited: