Correction for 'Clickable glutathione using tetrazine-alkene bioorthogonal chemistry for detecting protein glutathionylation' by Dilini N. Kekulandara et al., Org. Biomol. Chem., 2016, 14, 10886-10893.
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Correction: Clickable glutathione using tetrazine-alkene bioorthogonal chemistry for detecting protein glutathionylation.
Org Biomol Chem
April 2018
Department of Chemistry, Wayne State University, Detroit, Michigan 48202, USA.
Correction for 'Clickable glutathione using tetrazine-alkene bioorthogonal chemistry for detecting protein glutathionylation' by Dilini N. Kekulandara et al., Org.
View Article and Find Full Text PDFClickable glutathione using tetrazine-alkene bioorthogonal chemistry for detecting protein glutathionylation.
Org Biomol Chem
November 2016
Department of Chemistry, Wayne State University, Detroit, Michigan 48202, USA.
Protein glutathionylation is one of the major cysteine oxidative modifications in response to reactive oxygen species (ROS). We recently developed a clickable glutathione approach for detecting glutathionylation by using a glutathione synthetase mutant (GS M4) that synthesizes azido-glutathione (γGlu-Cys-azido-Ala) in situ in cells. In order to demonstrate the versatility of clickable glutathione and to increase the chemical tools for detecting glutathionylation, we sought to develop clickable glutathione that uses tetrazine-alkene bioorthogonal chemistry.
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