caspases

This is done through the binding to caspases directly.

Executioner caspases go on to "digest" the cell from the inside out.

Caspases are an important group of proteases involved in apoptosis.

Caspase-3 shares many of the typical characteristics common to all currently-known caspases.

When a cell is compelled to commit suicide, proteins called caspases go into action.

Some caspases are also required in the immune system for the maturation of lymphocytes.

It is one of the most conserved caspases in different species of animal.

Similar to other caspases, caspase-1 starts off as an inactive precursor called zymogen.

Caspases are regulated at a post-translational level, ensuring that they can be rapidly activated.

Caspases, therefore, were numbered in the order in which they were identified.

They showed that survivin inhibited processing of these two caspases into their active forms.

There are two types of caspases: initiators and effectors.

These molecules respond to stimuli that cause the clustering of the initiator caspases.

This protects the mitochondria from perturbation and the activation of caspases.

This leads to the activation of caspases and apoptosis of the cell.

Increasing the concentration of IAPs works to block specific caspases.

Hair follicles in anaphase express four different caspases.

Bcl-2 proteins prevent the activation of the caspases that lead to programmed cell death (apoptosis).

It is found on chromosome 11 in humans in a locus with other inflammatory caspases.

Caspases cleave keratin 18 at two sites during apoptosis.

Cell death is executed by the activation of a family of proteases termed caspases.

Some of the final targets of caspases include:

This pathway is made up of a series of proteins called initiator and executioner caspases.

Metacaspases are related to caspases and paracaspase.

Although the details are not here, survivin was shown to also inhibit cytochrome c and caspase-8-induced activation of caspases.