Programmed cell death and the caspases.
Members of a family of cysteine proteases known as caspases orchestrate the intracellular biochemical events that enable animal cells to kill themselves by apoptosis. To counteract the apoptotic response to infection, some viruses have adapted and evolved proteins that specifically block caspases. More recently, it has been demonstrated that endogenous proteins belonging to the IAP family can regulate apoptosis by directly inactivating some of the caspases involved in initiating and executing programmed cell death.
Salvesen
G S
GS
The Burnham Institute, La Jolla, California 92037, USA.
D000818:Animals; D017209:Apoptosis; D061945:Caspase Inhibitors; D020169:Caspases / Q000502:physiology*; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000378:metabolism; D006801:Humans; D011506:Proteins / Q000502:physiology; D051636:X-Linked Inhibitor of Apoptosis Protein
D061945:Caspase Inhibitors; D004792:Enzyme Precursors; D011506:Proteins; D051636:X-Linked Inhibitor of Apoptosis Protein; C496866:XIAP protein, human; D020169:Caspases