Article
Cysteine 202 of cyclophilin D is a site of multiple post-translational modifications and plays a role in cardioprotection.
Cardiovascular research - 1 Jan 2021
Amanakis Georgios, Sun Junhui, Fergusson Maria M, McGinty Shane, Liu Chengyu, Molkentin Jeffery D, Murphy Elizabeth
Abstract excerpt
AIMS: Cyclophilin-D is a well-known regulator of the mitochondrial permeability transition pore (PTP), the main effector of cardiac ischaemia/reperfusion injury. However, the binding of CypD to the PTP is poorly understood. Cysteine 202 (C202) of CypD is highly conserved among species and can undergo redox-sensitive post-translational modifications. We investigated whether C202 regulates the opening of PTP....
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