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S-Glutathionylation

S-Glutathionylation is the posttranslational modification of protein cysteine residues by the addition of glutathione, the most abundant and important low-molecular-mass thiol within most cell types.[1]

Protein S-glutathionylation is involved in

References edit

  1. ^ a b c d e Dalle-Donne, Isabella; Rossi, Ranieri; Colombo, Graziano; Giustarini, Daniela; Milzani, Aldo (2009). "Protein S-glutathionylation: A regulatory device from bacteria to humans". Trends in Biochemical Sciences. 34 (2): 85–96. doi:10.1016/j.tibs.2008.11.002. PMID 19135374.

glutathionylation, posttranslational, modification, protein, cysteine, residues, addition, glutathione, most, abundant, important, molecular, mass, thiol, within, most, cell, types, protein, glutathionylation, involved, oxidative, stress, nitrosative, stress, . S Glutathionylation is the posttranslational modification of protein cysteine residues by the addition of glutathione the most abundant and important low molecular mass thiol within most cell types 1 Protein S glutathionylation is involved in oxidative stress 1 nitrosative stress 1 preventing irreversible oxidation of protein thiols 1 control of cell signalling pathways by modulating protein function 1 References edit a b c d e Dalle Donne Isabella Rossi Ranieri Colombo Graziano Giustarini Daniela Milzani Aldo 2009 Protein S glutathionylation A regulatory device from bacteria to humans Trends in Biochemical Sciences 34 2 85 96 doi 10 1016 j tibs 2008 11 002 PMID 19135374 Retrieved from https en wikipedia org w index php title S Glutathionylation amp oldid 1031459149, wikipedia, wiki, book, books, library,

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