EC Number   |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Reference |
|---|
   3.4.22.62 | -999 |
- |
analysis of apoptosome inhibitors, improvement by chemical modifications for better increase of cellular penetration and efficient prevention of cell death, evaluation of cellular apoptosis by flow cytometry, immunohistochemistry, caspase activation assay |
699440 |
| 3.4.22.62 | -999 |
- |
analysis of oocytes from prophase I onwards, inhibition of caspase activity accelerates transition from metaphase I to metaphase II, caspase-9 and caspase-3 detected along the meiotic spindle, similar amounts of cleaved caspases in healthy and fragmented oocytes, caspase inhibition does not prevent doxorubicin-induced apoptosis, cleaved caspases probably dispensable for final oocyte death, potential involvement in the regulation of oocyte maturation |
697541 |
| 3.4.22.62 | -999 |
- |
apoptotic mechanism of the flavanoid isorhamnetin, isorhamnetin induces mitochondria-dependent caspase activation cascade, caspase inhibitors block isorhamnetin-induced apoptosis, increased cleavage of caspase-9 shown by Western blot analyses of isorhamnetin-treated cells, cytotoxicity assay, TUNEL assay, DNA fragmentation assay, measurement of mitochondrial membrane potential |
697082 |
| 3.4.22.62 | -999 |
- |
atorvastatin induces apoptosis in hepatic stellate cells (HSCs), atorvastatin-mediated apoptosis is blocked by co-application of mevalonic acid and U0126, an activator of the extracellular signal-regulated protein kinase (ERK1/2), increased activity of caspase-9 to 407% and of caspase-3 to 540% in cells treated with atorvastatin, flow cytometry, laser-scanning microscopy, Western blot, electrophoresis mobility shift assay, pathway of apoptosis induced by atorvastatin in hepatic stellate cells (HSCs) summarized |
699949 |
| 3.4.22.62 | -999 |
- |
caspase-9 identified as a substrate of the protein kinase DYRK1A, in vitro translation and immunoprecipitation of FLAG-DYRK1A in absence or presence of kinase inhibitors analyzed, the kinase inhibitor harmine prevents inhibitory phosphorylation of caspase-9 on threonine residue 125, depletion of DYRK1A by RNA silencing inhibits phosphorylation of caspase-9 on Thr125 in cellular assays, co-expression analysis shows interaction between DYRK1A with caspase-9 |
697888 |
| 3.4.22.62 | -999 |
- |
caspase-9 is responsible for the activation of caspase-3 in differentiating myoblasts, decreased caspase-9 levels due to RNA interference prevents caspase-3 activation and impairs muscle differentiation, release of cytochrome c not observed, novel mechanism of caspase-9 activation during muscle differentiation, apoptotic nuclear morphology assessed by DAPI staining, quantification of muscle-cell differentiation, mitochondrial-membrane depolarisation, cell fractionation, immunoblotting |
699106 |
| 3.4.22.62 | -999 |
- |
contribution of the death receptor and mitochondrial (intrinsic) pathways to apoptosis in follicular lymphoma cells induced by the chimeric mouse-human anti-CD20 antibody rituximab, time course of caspase activation, overexpression of caspase-9 inhibits the rituximab-induced activation of effector proteases (caspase-3, caspase-6 and caspase-7), rituximab-induced release of cytochrome c and collapse of mitochondrial membrane potential regulated by caspase-9 |
695657 |
| 3.4.22.62 | -999 |
- |
cytotoxiciy of Vibrio vulnificus cytolysin (VVC) analyzed by treatment of cell cultures with recombinant VVC protein (rVVC), recombinant Vibrio vulnificus cytolysin (rVVC) induces apoptosis in a time- and dose-dependent manner, apoptosis induced by recombinant Vibrio vulnificus cytolysin (rVVC) mediated by caspase-9 activation rather than caspase-8 activation |
700016 |
| 3.4.22.62 | -999 |
- |
determination of caspase-9 auto-processing in a cell-free system, phosphorylation of caspase-9 analyzed by Western blot, phosphorylation of caspase-9 by casein kinase 2 (CK2) on a serine near the site of caspase-8 cleavage, CK2 modification of Ser348 on caspase-9 lowers the susceptibility of caspase-9 to cleavage but does not affect caspase-9 auto-processing, substitution of Ser348 abolishes phosphorylation but not cleavage, phosphatase inhibitors delay apoptosis induced by tumor necrosis factor (TNF)-alpha, inhibition of kinase activity or loss of the kinase accelerates apoptosis and promotes early caspase-9 activation in response to TNF-alpha, modification of pro-caspase-9 in the vicinity of its processing motif protects the protease from inappropriate activation by other caspases |
698775 |
| 3.4.22.62 | -999 |
- |
genotyping of caspase-9 by PCR analysis, control and patient sample genotype frequencies distributed according to Hardy-Weinberg equilibrium, clinical characteristics and genotypes, evaluation of a single nucleotide polymorphism (SNP) in the caspase-9 gene of multiple sclerosis patients from Southern Italy, presence of the G/G genotype identified as a higher risk factor in the analyzed multiple sclerosis (MS) population, differential caspase-9 production related to the severity of multiple sclerosis |
699671 |
