3.4.22.55	2-chloro-2'-deoxyadenosine	-	663875	
3.4.22.55	amyloid beta1-42	the levels of activated caspase-2 in cultured hippocampal neurons significantly increase within 30 min of treatment with 0.003 mM amyloid beta1-42	731274	
3.4.22.55	ATM/ATR	caspase-2 is activated by ATM/ATR independently of p53 when Chk1 activity is repressed	717458	
3.4.22.55	caspase-10	is required for effective processing of caspase-2	666511	
3.4.22.55	CD95-death-inducing signaling complex	-	732592	
3.4.22.55	cyclin D3	-	663875	
3.4.22.55	lovastatin	0.05 mM for 24 h, increases caspase-2 gene expression	666351	
3.4.22.55	additional information	caspase-2 is activated by dimerization	717458	
3.4.22.55	additional information	caspase-2 is activated by proximity-induced oligomerization and trans-cleavage in vitro. Caspase-2 activation is possibly also mediated by caspase-8 in the death-inducing signaling complex	732220	
3.4.22.55	additional information	caspase-2 is rapidly activated by nerve growth factor deprivation	731274	
3.4.22.55	additional information	etoposide, staurosporine, pacritaxel and cyclohexamide treatment promotes exon 9-inclusion, increasing the ratio of caspase-2S to caspase-2L	665952	
3.4.22.55	additional information	genotoxic stress	665588	
3.4.22.55	additional information	heat shock, UV irradiation and anti-Fas treatment activate caspase-2	666419	
3.4.22.55	additional information	photodynamic treatment, incubation with zinc(II)-phthalocyanine (0.0005 mM and 0.001 mM)and irradiated with red light	665247	
3.4.22.55	additional information	the enzyme is activated during apoptosis by a caspase-3 (CPP32)-like protease. When cells are induced to undergo apoptosis, endogenous caspase-2 is first cleaved into three fragments of 32000-33000 Da and 14000 Da, which are then further processed into 18000 Da and 12000 Da active subunits	647763	
3.4.22.55	additional information	the topoisomerase-II inhibitor etoposide induces processing of procaspase-2	717457	
3.4.22.55	additional information	when protein kinase CK2 activity is low, procaspase-2 is dephosphorylated, dimerized, and activated in a PIDDosome-independent manner	664753	
3.4.22.55	P53	p53 induces PIDD expression resulting in a feed-forward loop	717458	
3.4.22.55	p53-induced protein with a death domain	PIDD, caspase-2 is activated by the p53 target gene product PIDD, i.e. LRDD or leucine-rich repeats and death domain containing, in a complex called the caspase-2-PIDDosome	718112	
3.4.22.55	p53-inducible death domain-containing protein	PIDD	663875	
3.4.22.55	p73	-	663875	
3.4.22.55	palmitate	caspase-2 is activated by an overabundance of saturated long-chain fatty acids like palmitate. Inhibition of amino acid transamination by 10 mM aminooxyacetate blocks caspase activation	732099	
3.4.22.55	PIDD protein	-	732220	
3.4.22.55	PIDDosome	-	732592	
3.4.22.55	protein phosphatase 1	-	731596, 732220	
3.4.22.55	RAIDD	adapter molecule, is required for caspase-2 activation after heat shock in splenocytes	666419	
3.4.22.55	RAIDD	caspase-2 activation is dependent on the adaptor protein RAIDD	731274	
3.4.22.55	RAIDD	in response to cellular stresses, processed PIDD-CC binds to RAIDD in the cytoplasm, which recruits and activates caspase-2, overview	717458	
3.4.22.55	RAIDD protein	-	732220	
3.4.22.55	silibinin	caspase-2 and caspase-8 can activate each other in response to silibinin	664533	
3.4.22.55	sterol regulatory element binding protein 2	increases caspase-2 gene expression	666351