2023
DOI: 10.1016/j.redox.2023.102642
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Mapping protein direct interactome of oxidoreductases with small molecular chemical cross-linkers in live cells

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Cited by 2 publications
(1 citation statement)
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“…TrxRs are NADPH-dependent because they transfer electrons from NADPH to the active disulfide site on the oxidized Trx protein in order to enable Trx to function. In this way, Trx catalyses the reduction of ROS from oxidized cysteines of proteins and in the process, Trx itself becomes oxidized [85]. The interaction between the active site dithiol in reduced Trx and oxidized cysteines of many proteins induces the process of thiol/disulfide exchange reaction to form an oxidized Trx.…”
Section: Breast Cancermentioning
confidence: 99%
“…TrxRs are NADPH-dependent because they transfer electrons from NADPH to the active disulfide site on the oxidized Trx protein in order to enable Trx to function. In this way, Trx catalyses the reduction of ROS from oxidized cysteines of proteins and in the process, Trx itself becomes oxidized [85]. The interaction between the active site dithiol in reduced Trx and oxidized cysteines of many proteins induces the process of thiol/disulfide exchange reaction to form an oxidized Trx.…”
Section: Breast Cancermentioning
confidence: 99%