Pub. Date : 2019 Jul 17
PMID : 31168542
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Grx2 catalyzes protein glutathionylation/de-glutathionylation and can coordinate an iron-sulfur cluster, forming inactive dimers stabilized by two molecules of glutathione. | Iron | glutaredoxin 2 | Homo sapiens |
| 2 | In addition, Grx2 monomerization led to an increase free iron ions concentration in the mitochondrial matrix, induction of lipid peroxidation and decrease of the mitochondrial membrane potential, indicating that the disassembly of Grx2 dimer involved the release of the iron-sulfur cluster in the mitochondrial matrix. | Iron | glutaredoxin 2 | Homo sapiens |
| 3 | In addition, Grx2 monomerization led to an increase free iron ions concentration in the mitochondrial matrix, induction of lipid peroxidation and decrease of the mitochondrial membrane potential, indicating that the disassembly of Grx2 dimer involved the release of the iron-sulfur cluster in the mitochondrial matrix. | Iron | glutaredoxin 2 | Homo sapiens |
| 4 | In addition, Grx2 monomerization led to an increase free iron ions concentration in the mitochondrial matrix, induction of lipid peroxidation and decrease of the mitochondrial membrane potential, indicating that the disassembly of Grx2 dimer involved the release of the iron-sulfur cluster in the mitochondrial matrix. | Iron | glutaredoxin 2 | Homo sapiens |
| 5 | Thus, by sensing the overall cellular redox conditions, mitochondrial Grx2 dimers become active monomers upon oxidative stress induced by sodium selenite with the consequent release of the iron-sulfur cluster, leading to activation of the intrinsic apoptotic pathway. | Iron | glutaredoxin 2 | Homo sapiens |