In a cell-free apoptosis system, mitochondria spontaneously released cytochrome c, which
activated DEVD-specific caspases, leading to fodrin cleavage and apoptotic nuclear …

Bcl-2 is an integral membrane protein located mainly on the outer membrane of
mitochondria. Overexpression of Bcl-2 prevents cells from undergoing apoptosis in …

The current model of apoptosis holds that upstream signals lead to activation of downstream
effector caspases. We generated mice deficient in the two effectors, caspase 3 and caspase …

REVIEW A variety of key events in apoptosis focus on mitochondria, including the release of
caspase activators (such as cytochrome c), changes in electron transport, loss of …

A current view is that cytotoxic stress, such as DNA damage, induces apoptosis by
regulating the permeability of mitochondria. Mitochondria sequester several proteins that, if …

Following exposure of cells to stimuli that trigger programmed cell death (apoptosis),
cytochrome c is rapidly released from mitochondria into the cytoplasm where it activates …

In the mitochondrial pathway of apoptosis, caspase activation is closely linked to
mitochondrial outer membrane permeabilization (MOMP). Numerous pro-apoptotic signal …

Apoptosis is an evolutionarily conserved cell suicide process executed by cysteine
proteases (caspases) and regulated by the opposing factions of the Bcl-2 protein family …

Mitochondrial cytochrome c, which functions as an electron carrier in the respiratory chain,
translocates to the cytosol in cells undergoing apoptosis, where it participates in the …

Mitochondria, the cell's energy-producing organelles, are thought to play a central role in
mediating apoptosis, or programmed cell death. Mitochondrial morphology remains intact …