A multicomponent system that degrades proteins conjugated to ubiquitin. Resolution of factors and evidence for ATP-dependent complex formation.
Open Access
- 1 September 1988
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 263 (25) , 12412-12419
- https://doi.org/10.1016/s0021-9258(18)37771-8
Abstract
No abstract availableThis publication has 37 references indexed in Scilit:
- Ubiquitin-Mediated Pathways for Intracellular ProteolysisAnnual Review of Cell Biology, 1987
- ATP activates dnaA protein in initiating replication of plasmids bearing the origin of the E. coli chromosomeCell, 1987
- Role of arginine-tRNA in protein degradation by the ubiquitin pathwayNature, 1987
- The ubiquitin system: functions and mechanismsTrends in Biochemical Sciences, 1985
- Occurrence of a polyubiquitin structure in ubiquitin-protein conjugatesBiochemical and Biophysical Research Communications, 1985
- Proteolysis of mitochondria in reticulocytes during maturation is ubiquitin‐dependent and is accompanied by a high rate of ATP hydrolysisFEBS Letters, 1985
- Relevance of protease “inhibitor” to the ATP-ubiquitin proteolytic systemBiochemical and Biophysical Research Communications, 1984
- Mechanisms of Intracellular Protein BreakdownAnnual Review of Biochemistry, 1982
- Intracellular Protein Degradation in Mammalian and Bacterial Cells: Part 2Annual Review of Biochemistry, 1976
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976