Prediction of the tertiary structure and substrate binding site of caspase‐8
Open Access
- 8 December 1997
- journal article
- Published by Wiley in FEBS Letters
- Vol. 419 (1), 49-54
- https://doi.org/10.1016/s0014-5793(97)01246-5
Abstract
The caspases represent a family of sulfhydryl proteases that play important regulatory roles in the cell. The tertiary structure of the protease domain of caspase‐8, also called FLICE, has been predi...Keywords
This publication has 33 references indexed in Scilit:
- FLICE, A Novel FADD-Homologous ICE/CED-3–like Protease, Is Recruited to the CD95 (Fas/APO-1) Death-Inducing Signaling ComplexCell, 1996
- Involvement of MACH, a Novel MORT1/FADD-Interacting Protease, in Fas/APO-1- and TNF Receptor–Induced Cell DeathCell, 1996
- ICE-LAP3, a Novel Mammalian Homologue of the Caenorhabditis elegans Cell Death Protein Ced-3 Is Activated during Fas- and Tumor Necrosis Factor-induced ApoptosisJournal of Biological Chemistry, 1996
- Identification and Characterization of CPP32/Mch2 Homolog 1, a Novel Cysteine Protease Similar to CPP32Published by Elsevier BV ,1996
- CrmA, a Poxvirus-encoded Serpin, Inhibits Cytotoxic T-lymphocyte-mediated ApoptosisPublished by Elsevier BV ,1995
- Fas- and Tumor Necrosis Factor-induced Apoptosis Is Inhibited by the Poxvirus crmA Gene ProductJournal of Biological Chemistry, 1995
- Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1 beta-converting enzyme.Genes & Development, 1994
- Induction of apoptosis in fibroblasts by IL-1β-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3Cell, 1993
- Accurate modeling of protein conformation by automatic segment matchingJournal of Molecular Biology, 1992
- Viral inhibition of inflammation: Cowpox virus encodes an inhibitor of the interleukin-1β converting enzymeCell, 1992