%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