Abstract
Ubiquitin-dependent proteolysis of cellular proteins is one of the major pathways to regulate protein function posttranslationally. Here we demonstrate a potentially general method of degrading any targeted proteins by the ubiquitin-dependent proteolysis in living cells, using small-molecule proteolysis inducer (SMPI).
| Original language | English |
|---|---|
| Pages (from-to) | 645-648 |
| Number of pages | 4 |
| Journal | Bioorganic and Medicinal Chemistry Letters |
| Volume | 14 |
| Issue number | 3 |
| DOIs | |
| State | Published - Feb 9 2004 |
Bibliographical note
Funding Information:We are grateful to the Division of Pharmaceutical Sciences (Univ. of Kentucky) for generous start-up fund and COBRE (NIH NCRR P20 RR15592) and the Kentucky Lung Cancer Research Program for financial support. We also thank Dr. Rohr for comments on the manuscript.
Funding
We are grateful to the Division of Pharmaceutical Sciences (Univ. of Kentucky) for generous start-up fund and COBRE (NIH NCRR P20 RR15592) and the Kentucky Lung Cancer Research Program for financial support. We also thank Dr. Rohr for comments on the manuscript.
| Funders | Funder number |
|---|---|
| Corporacion Nacional del Cobre | |
| Pharmaceutical Sciences Division | |
| Kentucky Lung Cancer Research Program | |
| NIH/NCRR | P20 RR15592 |
| National Center for Research Resources | P20RR015592 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Medicine
- Molecular Biology
- Pharmaceutical Science
- Drug Discovery
- Clinical Biochemistry
- Organic Chemistry