Title : Nitric oxide inhibits caspase-3 by S-nitrosation in vivo.

Pub. Date : 1999 Mar 12

PMID : 10066732






5 Functional Relationships(s)
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1 To demonstrate that the cysteine residue Cys-163 of caspase-3 is S-nitrosated, cells were transfected with the Myc-tagged p17 subunit of caspase-3. Cysteine caspase 3 Homo sapiens
2 To demonstrate that the cysteine residue Cys-163 of caspase-3 is S-nitrosated, cells were transfected with the Myc-tagged p17 subunit of caspase-3. Cysteine caspase 3 Homo sapiens
3 To demonstrate that the cysteine residue Cys-163 of caspase-3 is S-nitrosated, cells were transfected with the Myc-tagged p17 subunit of caspase-3. Cysteine caspase 3 Homo sapiens
4 To demonstrate that the cysteine residue Cys-163 of caspase-3 is S-nitrosated, cells were transfected with the Myc-tagged p17 subunit of caspase-3. Cysteine caspase 3 Homo sapiens
5 Thus, NO supplied by exogenous NO donors serves in vivo as an antiapoptotic regulator of caspase activity via S-nitrosation of the Cys-163 residue of caspase-3. Cysteine caspase 3 Homo sapiens