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040			_cCICY
090			_aB-16816
245	1	0	_aRedox regulation in photosynthetic organisms: focus on glutathionylation
490	0		_vAntioxidants and Redox Signaling, 16(6), p.567-586, 2012
520	3		_aIn photosynthetic organisms, besides the well-established disulfide/dithiol exchange reactions specifically controlled by thioredoxins (TRXs), protein S-glutathionylation is emerging as an alternative redox modification occurring under stress conditions. This modification, consisting of the formation of a mixed disulfide between glutathione and a protein cysteine residue, can not only protect specific cysteines from irreversible oxidation but also modulate protein activities and appears to be specifically controlled by small disulfide oxidoreductases of the TRX superfamily named glutaredoxins (GRXs).
650	1	4	_aGLUTATHIONYLATION
700	1	2	_aZaffagnini M
700	1	2	_aBedhomme M
700	1	2	_aMarchand Ch
700	1	2	_aMorisse S
700	1	2	_aTrost P
700	1	2	_aLemaire Sd
856	4	0	_uhttps://drive.google.com/file/d/1hpjY48nV7NjlB7s88mJTTYjDQrKFUCFH/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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