Purification and Characterization of an Interleukin-1β-converting Enzyme Family Protease That Activates Cysteine Protease P32 (CPP32)
Open Access
- 1 June 1996
- journal article
- Published by Elsevier BV
- Vol. 271 (23), 13371-13376
- https://doi.org/10.1074/jbc.271.23.13371
Abstract
No abstract availableThis publication has 23 references indexed in Scilit:
- Sterol Regulation of Fatty Acid Synthase PromoterJournal of Biological Chemistry, 1995
- Inhibition of ICE Family Proteases by Baculovirus Antiapoptotic Protein p35Science, 1995
- Inhibition of the Caenorhabditis elegans cell-death protease CED-3 by a CED-3 cleavage site in baculovirus p35 proteinNature, 1995
- Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosisNature, 1995
- Purification of an Interleukin-1β Converting Enzyme-related Cysteine Protease That Cleaves Sterol Regulatory Element-binding Proteins between the Leucine Zipper and Transmembrane DomainsJournal of Biological Chemistry, 1995
- Yama/CPP32β, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymeraseCell, 1995
- Dual DNA Binding Specificity of ADD1/SREBP1 Controlled by a Single Amino Acid in the Basic Helix-Loop-Helix DomainMolecular and Cellular Biology, 1995
- Mice deficient in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxic shockCell, 1995
- SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysisCell, 1994
- SREBP-2, a second basic-helix-loop-helix-leucine zipper protein that stimulates transcription by binding to a sterol regulatory element.Proceedings of the National Academy of Sciences, 1993