• Publications
  • Influence
Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
A potent peptide aldehyde inhibitor has been developed and shown to prevent apoptotic events in vitro, suggesting that apopain/CPP32 is important for the initiation of apoptotic cell death. Expand
A Combinatorial Approach Defines Specificities of Members of the Caspase Family and Granzyme B
A novel method employing a positional scanning substrate combinatorial library to rigorously define individual specificities of caspase and granzyme B proteases divides these proteases into three distinct groups and suggests that several have redundant functions. Expand
Caspases: killer proteases.
Caspases (cysteinyl aspartate-specific proteinases) mediate highly specific proteolytic cleavage events in dying cells, which collectively manifest the apoptotic phenotype. The key and central roleExpand
Human ICE/CED-3 Protease Nomenclature
A committee of several scientists who have been involved in the identification and characterization of these enzymes have formed a committee, with the objective of proposing a nomenclature for the human members of this protease family that is sensible and easy to use. Expand
Inhibition of Human Caspases by Peptide-based and Macromolecular Inhibitors*
  • Margarita Garcia-Calvo, Erin P. Peterson, Barbara Leiting, Rejean Ruel, D. Nicholson, Nancy A. Thornberry
  • Biology, Medicine
  • The Journal of Biological Chemistry
  • 4 December 1998
The results obtained with peptide-based inhibitors are in accord with those predicted from the substrate specificity studies described earlier, and the cowpox serpin CrmA is a potent and selective inhibitor of Group I and most Group III caspases, suggesting that this virus facilitates infection through inhibition of both apoptosis and the host inflammatory response. Expand
Ordering the Cytochrome c–initiated Caspase Cascade: Hierarchical Activation of Caspases-2, -3, -6, -7, -8, and -10 in a Caspase-9–dependent Manner
Six additional caspases (caspases-2, -3, -6, -7, -8, and -10) are processed in cell-free extracts in response to cytochrome c, and that three others failed to be activated under the same conditions. Expand
Cleavage at the Caspase-6 Site Is Required for Neuronal Dysfunction and Degeneration Due to Mutant Huntingtin
Caspase-6-resistant mutant htt mice are protected against neurotoxicity induced by multiple stressors including NMDA, quinolinic acid (QA), and staurosporine and highlight the significant role of htt proteolysis and excitotoxicity in HD. Expand
Involvement of Caspases in Proteolytic Cleavage of Alzheimer’s Amyloid-β Precursor Protein and Amyloidogenic Aβ Peptide Formation
Caspases appear to play a dual role in proteolytic processing of APP and the resulting propensity for Aβ peptide formation, as well as in the ultimate apoptotic death of neurons in Alzheimer's disease. Expand
Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract
The results show that huntingtin is cleaved by cysteine proteases and suggest that HD might be a disorder of inappropriate apoptosis, providing an explanation for the gain–of–function associated with GAG expansion. Expand
Caspase-2 Is Localized at the Golgi Complex and Cleaves Golgin-160 during Apoptosis
It is proposed that the Golgi complex, like mitochondria, senses and integrates unique local conditions, and transduces pro-apoptotic signals through local caspases, which regulate local effectors. Expand