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In pathological conditions associated with chronic oxidative stress, such as sickle cell anemia [143], this fragile balance is severely compromised, as in the case of a redox imbalance promoting glutathionation (a covalent binding between GSH and proteins via a thioether bond) of reactive cysteine residues of spectrin, thus disrupting its E2/E3 function and preventing both auto-ubiquitination and the modification of other cytoskeletal partners, particularly ankyrin [144]