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Thiol Redox

"Protein thiol redox plays an important role in numerous cellular processes and stress responses. The thiol moiety of cysteine residue is easily altered to various redox isoforms that play critical roles in regulation of both structure and function of proteins. In the present study, a quantitative thiol redox proteomic method, termed OxNSIL has been developed, which integrates the chemical labeling by biotin-tagged alkylating reagents with the heavy nitrogen stable isotope-coded salt metabolic labeling and acquires both advantages of biotin-avidin enrichment and MS-based quantitation of cysteine residue-containing peptides. Both the reduced and the reversibly oxidized cysteine thiol moieties are finally identified in a site-specific manner and measured in a single experiment. OMICS Group International is one of the leading Open Access Publishers which is publishing 700+ peer-reviewed journals with the support of 50,000+ editorial board members as editorial team and aimed to disseminate the scholarly knowledge to the scientific society. OMICS Group also organizing 3000+ International Scientific Conferences and events yearly all over the world with the support of 1000+ Scientific associations worldwide. Citation: Hu Q, Guo G, Yang Z, Li Y, Xia Y (2014) Stable Isotope Metabolic Labeling-Based Quantitative Thiol Redox Proteomic Analysis of Hydrogen Peroxide-treated Arabidopsis plant. J Proteomics Bioinform 7: 121-133."
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Last date updated on July, 2014

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