On the involvement of calpains in the degradation of the tumor suppressor protein p53
Open Access
- 7 April 1997
- journal article
- Published by Wiley in FEBS Letters
- Vol. 406 (1-2) , 17-22
- https://doi.org/10.1016/s0014-5793(97)00225-1
Abstract
A crude fraction that contains ubiquitin–protein ligases contains also a proteolytic activity of ∼100 kDa that cleaves p53 to several fragments. The protease does not require ATP and is inhibited in ...Keywords
This publication has 25 references indexed in Scilit:
- Ubiquitin, proteasomes, and the regulation of intracellular protein degradationPublished by Elsevier ,2002
- Proteolytic Cleavage of Human p53 by Calpain: a Potential Regulator of Protein StabilityMolecular and Cellular Biology, 1997
- Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2ACell, 1995
- The ubiquitin-proteasome proteolytic pathwayCell, 1994
- Accumulation of p53 in a mutant cell line defective in the ubiquitin pathway.Molecular and Cellular Biology, 1994
- The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53Cell, 1993
- Degradation of nuclear oncoproteins by the ubiquitin system in vitro.Proceedings of the National Academy of Sciences, 1991
- The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53Published by Elsevier ,1990
- Calpain‐calpastatin and fusionFEBS Letters, 1986
- Energy requirement for degradation of tumor-associated protein p53.Molecular and Cellular Biology, 1984