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Alnemri, Emad
One or more keywords matched the following items that are connected to
Alnemri, Emad
Item Type
Name
Concept
Substrate Specificity
Academic Article
Overexpression and characterization of the human mineralocorticoid receptor.
Academic Article
Interaction of the baculovirus anti-apoptotic protein p35 with caspases. Specificity, kinetics, and characterization of the caspase/p35 complex.
Academic Article
Identification and characterization of murine caspase-14, a new member of the caspase family.
Academic Article
Crystal structure of a procaspase-7 zymogen: mechanisms of activation and substrate binding.
Academic Article
Inhibitor of apoptosis proteins are substrates for the mitochondrial serine protease Omi/HtrA2.
Academic Article
Tim50, a component of the mitochondrial translocator, regulates mitochondrial integrity and cell death.
Academic Article
Mch2, a new member of the apoptotic Ced-3/Ice cysteine protease gene family.
Academic Article
DNA-dependent protein kinase catalytic subunit: a target for an ICE-like protease in apoptosis.
Academic Article
Cleavage of lamin A by Mch2 alpha but not CPP32: multiple interleukin 1 beta-converting enzyme-related proteases with distinct substrate recognition properties are active in apoptosis.
Academic Article
The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32.
Academic Article
THAP5 is a human cardiac-specific inhibitor of cell cycle that is cleaved by the proapoptotic Omi/HtrA2 protease during cell death.
Academic Article
Mammalian cell death proteases: a family of highly conserved aspartate specific cysteine proteases.
Academic Article
Activation of CPP32 and Mch3 alpha in wild-type p53-induced apoptosis.
Academic Article
Heteronuclear ribonucleoproteins C1 and C2, components of the spliceosome, are specific targets of interleukin 1beta-converting enzyme-like proteases in apoptosis.
Academic Article
Purification of the death substrate poly(ADP-ribose) polymerase.
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