Abstract
P53 and mdm2 are linked to each other through a negative feedback loop. P53 transactivates mdm2, but mdm2, in turn, is a major opponent of p53. Mdm2 promotes p53 degradation through a ubiquitin-dependent pathway on 26S proteasomes and is thought to be largely responsible for the very low levels of p53 protein in unstressed cells. The rationale for targeting the p53-mdm2 interaction therapeutically lies in the ability to activate p53 in all those tumors that retain wild type p53. (C) 2000 Harcourt Publishers Ltd.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 217-221 |
| Number of pages | 5 |
| Journal | Drug Resistance Updates |
| Volume | 3 |
| Issue number | 4 |
| DOIs | |
| State | Published - Jan 1 2000 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Oncology
- Pharmacology
- Cancer Research
- Infectious Diseases
- Pharmacology (medical)
Cite this
Disrupting the p53-mdm2 interaction as a potential therapeutic modality. / Moll, Ute M.; Zaika, Alexander.
In: Drug Resistance Updates, Vol. 3, No. 4, 01.01.2000, p. 217-221.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Disrupting the p53-mdm2 interaction as a potential therapeutic modality
AU - Moll, Ute M.
AU - Zaika, Alexander
PY - 2000/1/1
Y1 - 2000/1/1
N2 - P53 and mdm2 are linked to each other through a negative feedback loop. P53 transactivates mdm2, but mdm2, in turn, is a major opponent of p53. Mdm2 promotes p53 degradation through a ubiquitin-dependent pathway on 26S proteasomes and is thought to be largely responsible for the very low levels of p53 protein in unstressed cells. The rationale for targeting the p53-mdm2 interaction therapeutically lies in the ability to activate p53 in all those tumors that retain wild type p53. (C) 2000 Harcourt Publishers Ltd.
AB - P53 and mdm2 are linked to each other through a negative feedback loop. P53 transactivates mdm2, but mdm2, in turn, is a major opponent of p53. Mdm2 promotes p53 degradation through a ubiquitin-dependent pathway on 26S proteasomes and is thought to be largely responsible for the very low levels of p53 protein in unstressed cells. The rationale for targeting the p53-mdm2 interaction therapeutically lies in the ability to activate p53 in all those tumors that retain wild type p53. (C) 2000 Harcourt Publishers Ltd.
UR - http://www.scopus.com/inward/record.url?scp=0033835043&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033835043&partnerID=8YFLogxK
U2 - 10.1054/drup.2000.0160
DO - 10.1054/drup.2000.0160
M3 - Article
AN - SCOPUS:0033835043
VL - 3
SP - 217
EP - 221
JO - Drug Resistance Updates
JF - Drug Resistance Updates
SN - 1368-7646
IS - 4
ER -