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Gel‐based fluorescent proteomic tools for investigating cell redox signaling. A mini‐review
Author(s) -
Majewska Anna M.,
Mostek Agnieszka
Publication year - 2021
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.202000389
Subject(s) - proteome , redox , proteomics , reactive oxygen species , posttranslational modification , chemistry , reactive nitrogen species , biochemistry , computational biology , biology , enzyme , organic chemistry , gene
The specific chemical reactivity of thiol groups makes protein cysteines susceptible to reactions with reactive oxygen species (ROS) and reactive nitrogen species (RNS) resulting in the formation of various reversible and irreversible oxidative post‐translational modifications (oxPTMs). This review highlights a number of gel‐based redox proteomic approaches to detect protein oxPTMs, with particular emphasis on S‐nitrosylation, which we believe are currently one of the most accurate way to analyze changes in the redox status of proteins. The information collected in this review relates to the recent progress regarding methods for the enrichment and identification of redox‐modified proteins, with an emphasis on fluorescent gel proteomics. Gel‐based fluorescent proteomic strategies are low‐cost and easy‐to‐use tools for investigating the thiol proteome and can provide substantial information on redox signaling.