caspase

Researchers decided upon the nomenclature of the caspase in 1996.

The role of Hip-1 in caspase mediated cell death remains unclear.

Once more, both cell lines produced activated caspase 3 by 1 h after treatment.

However, there has been evidence that the protein carries a caspase recruiting domain on it.

In many instances, a particular caspase had been identified simultaneously by more than one laboratory, who would each give the protein a different name.

A caspase 9 knock-out leads to a severe brain malformation.

The initiation of this cascade reaction is regulated by caspase inhibitors.

It most likely acts upon caspase 3.

Degradation of full length DFF45 was used to indicate caspase 3 activity.

Genetic abnormalities frequently occur in a tumor-suppressor gene called caspase 8.

This allows normal caspase activity to proceed.

Such substrates have been used to detect caspase activity and cytochrome P450 activity, among others.

A caspase 8 knock-out leads to cardiac failure and thus embryonic lethality.

When activated, Fas turns on what is called a "Caspase Cascade."

This release of cytochrome c in turn activates caspase 9, a cysteine protease.

We thus measured caspase activity after bile acid treatment in CHO.

The caspase cascade can be activated by:

The role of caspase substrate cleavage in the morphology of apoptosis is not clear.

ICE was, therefore, renamed as caspase 1.

Mitochondria mediated apoptosis induction was confirmed by the increased activity of caspase cascade.

Apoptosis Video Demonstrates a model of a caspase cascade as it occurs in vivo.

Caspase-9 is an initiator caspase, encoded by the CASP9 gene.

Fas and Fas-ligand interact to trigger the caspase cascade, leading to cell apoptosis.

Activation of caspase 8 was detected in CHO.