%0 Journal Article %T Strategies and Tools for Detection of Protein S-Nitrosylation and S-Sulfhydration %A Guangdong Yang %A Lingyun Wu %A Ming Fu %A YoungJun Ju %J Open Journal of Immunology %D -1 %R 10.4172/2161-1009.1000224 %X H2S interacts with the free thiol group in the active cysteine residues from target proteins and forms a hydropersulfide moiety (-SSH), termed as S-sulfhydration, which is similar to nitric oxide (NO) regulation of protein by S-nitrosylation. Protein S-sulfhydration now is proposed to mediate most of H2S bioactivities in various cellular functions. A number of methods have been developed for detection of S-nitrosylation and S-sulfhydration. Selective recognition of hydropersulfide (SSH) is a main target for the detection of S-sulfhydration. Protein Ssulfhydration can be detected by biotin switch assay, which is developed and further modified based on the detection approaches for protein S-nitrosylation. Here we highlight the different tools for detection of protein S-sulfhydration and S-nitrosylation, and provide strategies for developing new methods to locate the modified cysteine residues. %K YoungJun Ju %K Ming Fu %K Lingyun Wu and Guangdong Yang %K S-sulfhydration %K S-nitrosylation %K H2S %K NO %K Biotin switch assay %K Hydropersulfide %U https://www.longdom.org/abstract/strategies-and-tools-for-detection-of-protein-snitrosylation-andssulfhydration-35102.html