Schotte et al., 1998 - Google Patents
Cathepsin B-mediated activation of the proinflammatory caspase-11Schotte et al., 1998
View PDF- Document ID
- 11426654601387177496
- Author
- Schotte P
- Van Criekinge W
- Van de Craen M
- Van Loo G
- Desmedt M
- Grooten J
- Cornelissen M
- De Ridder L
- Vandekerckhove J
- Fiers W
- Vandenabeele P
- Beyaert R
- Publication year
- Publication venue
- Biochemical and biophysical research communications
External Links
Snippet
Members of the caspase (CASP) family of cysteine proteases can be subdivided in proapoptotic caspases and proinflammatory caspases. Whereas the apical activation pathways for the caspases that are involved in the execution of the apoptotic process are …
- 108090000712 Cathepsin B 0 title abstract description 36
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6472—Cysteine endopeptidases (3.4.22)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Schotte et al. | Cathepsin B-mediated activation of the proinflammatory caspase-11 | |
| Samejima et al. | Transition from caspase-dependent to caspase-independent mechanisms at the onset of apoptotic execution | |
| Alam et al. | Early activation of caspases during T lymphocyte stimulation results in selective substrate cleavage in nonapoptotic cells | |
| Dimmeler et al. | Suppression of apoptosis by nitric oxide via inhibition of interleukin-1β–converting enzyme (ice)-like and cysteine protease protein (cpp)-32–like proteases | |
| Zhivotovsky et al. | Caspases: their intracellular localization and translocation during apoptosis | |
| Desautels et al. | Demonstration of an ATP-dependent, vanadate-sensitive endoprotease in the matrix of rat liver mitochondria. | |
| Waterhouse et al. | Calpain activation is upstream of caspases in radiation-induced apoptosis | |
| Belizário et al. | Cleavage of caspases-1,-3,-6,-8 and-9 substrates by proteases in skeletal muscles from mice undergoing cancer cachexia | |
| Kalousek et al. | Rat liver mitochondrial intermediate peptidase (MIP): purification and initial characterization. | |
| Gajate et al. | Involvement of mitochondria and caspase‐3 in ET‐18‐OCH3‐induced apoptosis of human leukemic cells | |
| Vancompernolle et al. | Atractyloside-induced release of cathepsin B, a protease with caspase-processing activity | |
| Jänicke et al. | Caspase-3 is required for α-fodrin cleavage but dispensable for cleavage of other death substrates in apoptosis | |
| Cain et al. | The Apaf-1 apoptosome: a large caspase-activating complex | |
| Van De Craen et al. | The proteolytic procaspase activation network: an in vitro analysis | |
| Stefanis et al. | Caspase-2 (Nedd-2) processing and death of trophic factor-deprived PC12 cells and sympathetic neurons occur independently of caspase-3 (CPP32)-like activity | |
| Anuradha et al. | Fluoride induces apoptosis by caspase-3 activation in human leukemia HL-60 cells | |
| LONSDALE‐ECCLES et al. | Lysosomal and non‐lysosomal peptidyl hydrolases of the bloodstream forms of Trypanosoma brucei brucei | |
| Dong et al. | Serine protease inhibitors suppress cytochrome c-mediated caspase-9 activation and apoptosis during hypoxia–reoxygenation | |
| Rickers et al. | Inhibition of CPP32 blocks surface IgM‐mediated apoptosis and D4‐GDI cleavage in human BL60 Burkitt lymphoma cells | |
| Marrakchi et al. | Cerastocytin, a new thrombin-like platelet activator from the venom of the Tunisian viper Cerastes cerastes | |
| Söderhäll | Properties of carrot polyphenoloxidase | |
| Kim et al. | Pan-caspase inhibitor zVAD enhances cell death in RAW246. 7 macrophages | |
| Joy Huang-Yang et al. | Purification of rabbit testis proacrosin and studies of its active form | |
| Liebetrau et al. | Increased intracellular calpain detection in experimental focal cerebral ischemia | |
| WO1998002579A1 (en) | Regulation of apoptosis and in vitro model for studies thereof |