Interleukin-1b converting enzyme (ICE) processes the inactive proIL-1b to the proinflammatory mature IL-1b. ICE belongs to a family of cysteine proteases that have been implicated in apoptosis. To address the biological functions of ICE, we generated ICE-deficient mice through gene targeting technol
Structure and mechanism of interleukin-lβ converting enzyme
✍ Scribed by Wilson, Keith P.; Black, Jo-Anne F.; Thomson, John A.; Kim, Eunice E.; Griffith, James P.; Navia, Manuel A.; Murcko, Mark A.; Chambers, Stephen P.; Aldape, Robert A.; Raybuck, Scott A.
- Book ID
- 109789261
- Publisher
- Nature Publishing Group
- Year
- 1994
- Tongue
- English
- Weight
- 753 KB
- Volume
- 370
- Category
- Article
- ISSN
- 0028-0836
- DOI
- 10.1038/370270a0
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
Interleukin-1b converting enzyme (ICE) is the first enzyme of a new family of cysteine endoproteinases to be isolated and characterized. An overview of the structure and activity of ICE is outlined together with highlights of salient features common to members of each of the family members.
IL-8 is produced by various cells, and the NH(2)-terminal amino acid sequence of IL-8 displays heterogeneity among cell types. The mature form of IL-8 has 72 amino acids (72IL-8), while a precursor form (77IL-8) of IL-8 has five additional amino acids to the 72IL-8 NH(2)-terminal. However, it has be