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Literature summary for 3.4.24.83 extracted from
- Killing of macrophages by anthrax lethal toxin: involvement of the N-end rule pathway (2008), Cell. Microbiol., 10, 1352-1362.
Application
| Application | Comment | Organism |
|---|---|---|
| molecular biology | proteasome inhibitors block anthrax lethal toxin-mediated caspase-1 activation and can protect against cell death, indicating that the degradation of at least one cellular protein is required for cell death. Proteins can be degraded by the proteasome via the N-end rule. Using amino acid derivatives that act as inhibitors of this pathway, it is shown that the N-end rule is required for anthrax lethal toxin-mediated caspase-1 activation and cell death. The Streptomyces olivoreti peptide bestatin, which inhibits leucine, alanine and arginine aminopeptidases, protects macrophages against anthrax lethal toxin. c-IAP1, a mammalian member of the inhibitor of apoptosis protein (IAP) family is identified, as a novel N-end rule substrate degraded in macrophages treated with anthrax lethal toxin | Bacillus anthracis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus anthracis | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| anthrax lethal toxin | - |
Bacillus anthracis |
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Release 2023.1 (January 2023)
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