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Literature summary for 3.4.22.55 extracted from

  • Upton, J.P.; Austgen, K.; Nishino, M.; Coakley, K.M.; Hagen, A.; Han, D.; Papa, F.R.; Oakes, S.A.
    Caspase-2 cleavage of BID is a critical apoptotic signal downstream of endoplasmic reticulum stress (2008), Mol. Cell. Biol., 28, 3943-3951.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.55

Inhibitors

Inhibitors Comment Organism Structure
Cbzl-VDVAD-fluoromethylketone caspase-2 cleaves BID in response 16 to endoplasmic reticulum stress. Resistance to endoplasmic reticulum stress-induced apoptosis can be conferred by inhibiting caspase-2 activity Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
BID + H2O Mus musculus caspase-2 cleaves BID in response 16 to endoplasmic reticulum stress. Resistance to endoplasmic reticulum stress-induced apoptosis can be conferred by inhibiting caspase-2 activity ?
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
fibroblast
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
BID + H2O
-
 Mus musculus ?
-
 ?
BID + H2O caspase-2 cleaves BID in response 16 to endoplasmic reticulum stress. Resistance to endoplasmic reticulum stress-induced apoptosis can be conferred by inhibiting caspase-2 activity Mus musculus ?
-
 ?