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Title:
Cardiolipin oxidation sets cytochrome c free | Nature Chemical Biology
Description:
Cytochrome c release from the mitochondria is a critical component of the apoptotic cell-death program. Cytochrome c–catalyzed peroxidation of cardiolipin, a mitochondrial phospholipid, has now been shown to lessen the binding of cytochrome c to the mitochondrial inner membrane and facilitate permeabilization of the outer membrane. These results describe a new and earlier pro-apoptotic role for cytochrome c.
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nature portfolio permissions reprints privacy policy medical research advertising nature 389 nature social media earlier pro-apoptotic role apoptotic cell-death program springerlink instant access personal data data protection permissions european economic area article orrenius privacy content cytochrome cardiolipin oxygenase required ion channel assembly institutional subscriptions read polyamine regulation wild-type mice maldi msi william explore content subscription content accepting optional cookies journals search log proapoptotic factors valerian manage preferences access critical component environmental medicine journal publish article purchase content issue learn article cite institution buy optional cookies choices nat chem biol essential cookies cookies skip institution subscribe zhivotovsky article free articles cell biol
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headline:Cardiolipin oxidation sets cytochrome c free
description:Cytochrome c release from the mitochondria is a critical component of the apoptotic cell-death program. Cytochrome câcatalyzed peroxidation of cardiolipin, a mitochondrial phospholipid, has now been shown to lessen the binding of cytochrome c to the mitochondrial inner membrane and facilitate permeabilization of the outer membrane. These results describe a new and earlier pro-apoptotic role for cytochrome c.
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