ChemInform Abstract: Biomimetic Models for Cysteine Proteases. Part 3. Acylation of Imidazolium-Thiolate Zwitterions by p-Nitrophenylacetate as a Model for the Acylation Step and Demonstration of Intramolecular General-Base-Catalyzed Delivery of H2O by Im

1986 ◽  
Vol 17 (13) ◽  
Author(s):  
J. P. STREET ◽  
K. I. SKOREY ◽  
R. S. BROWN ◽  
R. G. BALL
2002 ◽  
Vol 38 ◽  
pp. 9-19 ◽  
Author(s):  
Guy S Salvesen

The ability of metazoan cells to undergo programmed cell death is vital to both the precise development and long-term survival of the mature adult. Cell deaths that result from engagement of this programme end in apoptosis, the ordered dismantling of the cell that results in its 'silent' demise, in which packaged cell fragments are removed by phagocytosis. This co-ordinated demise is mediated by members of a family of cysteine proteases known as caspases, whose activation follows characteristic apoptotic stimuli, and whose substrates include many proteins, the limited cleavage of which causes the characteristic morphology of apoptosis. In vertebrates, a subset of caspases has evolved to participate in the activation of pro-inflammatory cytokines, and thus members of the caspase family participate in one of two very distinct intracellular signalling pathways.


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