Journal article
Synthesizing Clickable Glutathione by Glutathione Synthetase Mutant for Detecting Protein Glutathionylation
Synlett, v 26(3), pp 285-293
01 Feb 2015
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
In response to reactive oxygen species (ROS), glutathione plays an important role in redox signaling by forming a disulfide bond with protein cysteine residues, known as glutathionylation. We briefly review the roles of glutathione, ROS, and glutathionylation in redox regulation. We then introduce common biochemical methods for identifying glutathionylation and highlight our recent chemical method for selective detection of glutathionylation. The merits, limitations, and future applications of our approach are also discussed.
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Details
- Title
- Synthesizing Clickable Glutathione by Glutathione Synthetase Mutant for Detecting Protein Glutathionylation
- Creators
- Kusal T. G. Samarasinghe - Wayne State UniversityYoung-Hoon Ahn - Wayne State University
- Publication Details
- Synlett, v 26(3), pp 285-293
- Publisher
- Thieme Medical Publishers
- Number of pages
- 9
- Grant note
- Wayne State University Start-up funds WSU University Research Grant
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- College of Arts and Sciences; Chemistry; Drexel University
- Web of Science ID
- WOS:000350056800002
- Scopus ID
- 2-s2.0-84921038642
- Other Identifier
- 991020111243604721
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- Web of Science research areas
- Chemistry, Organic