The article by Beni B. Wolf and Douglas R. Green reviews the role of caspase proteinases in apoptotic cell death. Caspases are cysteine proteinases that exist as latent zymogens and are activated by apoptotic signals, leading to the systematic dismantling and packaging of the cell. The authors highlight the sequence similarity between the *Caenorhabditis elegans* cell death gene *ced-3* and mammalian caspase-1, which was a pivotal discovery in understanding the role of caspases in apoptosis. Over a dozen caspase family members have been identified, each with specific functions in apoptosis and inflammation. Caspases are activated through autoactivation, transactivation, or proteolysis by other proteinases. Autoactivation occurs when caspase zymogens oligomerize, leading to proteolysis of the interdomain linker and the removal of the prodomain. Transactivation involves the activation of other procaspases, while proteolysis by non-caspase proteinases, such as granzyme B, can also activate caspases. The article discusses the structure of caspases, which share a common core structure with an N-terminal prodomain, a large subunit containing the active site cysteine, and a C-terminal small subunit. The active enzymes function as tetramers, and their substrate specificity is determined by the S1 subsite, which binds aspartate residues. Caspases play a crucial role in the apoptotic mechanism by cleaving and activating various cellular proteins. These proteins include pro- and anti-apoptotic proteins, structural proteins of the nucleus and cytoskeleton, and proteins involved in cellular signaling and repair. The proteolysis of these substrates promotes cellular packaging and subsequent engulfment by phagocytes. The authors conclude that caspases are essential mediators of apoptosis and that their dysfunction can lead to human diseases such as cancer and neurodegenerative disorders. Further research is needed to understand the precise mechanisms and implications of caspase activation in these diseases.The article by Beni B. Wolf and Douglas R. Green reviews the role of caspase proteinases in apoptotic cell death. Caspases are cysteine proteinases that exist as latent zymogens and are activated by apoptotic signals, leading to the systematic dismantling and packaging of the cell. The authors highlight the sequence similarity between the *Caenorhabditis elegans* cell death gene *ced-3* and mammalian caspase-1, which was a pivotal discovery in understanding the role of caspases in apoptosis. Over a dozen caspase family members have been identified, each with specific functions in apoptosis and inflammation. Caspases are activated through autoactivation, transactivation, or proteolysis by other proteinases. Autoactivation occurs when caspase zymogens oligomerize, leading to proteolysis of the interdomain linker and the removal of the prodomain. Transactivation involves the activation of other procaspases, while proteolysis by non-caspase proteinases, such as granzyme B, can also activate caspases. The article discusses the structure of caspases, which share a common core structure with an N-terminal prodomain, a large subunit containing the active site cysteine, and a C-terminal small subunit. The active enzymes function as tetramers, and their substrate specificity is determined by the S1 subsite, which binds aspartate residues. Caspases play a crucial role in the apoptotic mechanism by cleaving and activating various cellular proteins. These proteins include pro- and anti-apoptotic proteins, structural proteins of the nucleus and cytoskeleton, and proteins involved in cellular signaling and repair. The proteolysis of these substrates promotes cellular packaging and subsequent engulfment by phagocytes. The authors conclude that caspases are essential mediators of apoptosis and that their dysfunction can lead to human diseases such as cancer and neurodegenerative disorders. Further research is needed to understand the precise mechanisms and implications of caspase activation in these diseases.