Journal
MOLECULAR CELL
Volume 6, Issue 3, Pages 751-756Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(00)00074-5
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Funding
- NCI NIH HHS [R01-CA64888-06] Funding Source: Medline
- NATIONAL CANCER INSTITUTE [R01CA064888] Funding Source: NIH RePORTER
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The functional characterization of a specific gene, or its protein product, often relies on assessing the consequences of its elimination, usually accomplished by gene knockout, ribozyme, antisense, or RNA-mediated interference (RNAi) technologies. The selective degradation of cellular proteins is mediated primarily by the ubiquitin-proteasome pathway. Manipulation of the ubiquitin-dependent proteolytic machinery to eliminate specific gene products at the protein level has been previously attempted with some success in vitro; however, the in vivo efficacy of this approach has not yet been achieved. Here we report successful engineering of the substrate receptor of a major ubiquitin-proteolytic machinery to direct the degradation of otherwise stable cellular proteins both in yeast and in mammalian cells.
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