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Collectively, mitochondria and caspase members are feasible targets of capsaicin for apoptosis of human cancer cells.
This was associated with cytochrome c release from the mitochondria and caspase 9 activation.
30 ER stress can induce apoptosis through an intrinsic pathway involving cytochrome c release from mitochondria and caspase activation.
Aminoglycoside exposure also results in cytochrome c release from the mitochondria and caspase activation, which suggests that hair cells undergo caspase-mediated cell death.
Essentially similar results were obtained with respect to CB-induced cytochrome c release from the mitochondria and caspase activation including caspase-8 activation.
This is turn, inactivated mitochondrial voltage-dependent anion channel, reduced cytochrome c release from the mitochondria and caspase 9 activation and protected both liver types against mitochondrial damage.
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This cell death pathway involves the mitochondria and caspases, mainly caspase-1 and caspase-10.
Over-expression of wild-type (but not pathogenic variants) in tumour cell lines was subsequently shown to prevent release of cytochrome c from mitochondria and caspase-3 activation during stress [5], [35], [36].
More recent results from the same group demonstrated the release of cytochrome c from mitochondria and caspase-3 activation in differentiated RGC-5 cells measured individually after three days of undergoing 30 mmHg pressure [16].
Initiation of apoptosis provides that mitochondria and caspases engage in a self-amplifying pathway of mutual activation.
Caspase-dependent apoptosis can be mediated by cell membrane death receptors or via mitochondria, and caspase-independent apoptosis has also been described (Lee et al., 2006).
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