{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Qin G"],"funding":["NIA NIH HHS"],"pagination":["3268"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10241878"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(1)"],"pubmed_abstract":["Reversible protein S-nitrosylation regulates a wide range of biological functions and physiological activities in plants. However, it is challenging to quantitively determine the S-nitrosylation targets and dynamics in vivo. In this study, we develop a highly sensitive and efficient fluorous affinity tag-switch (FAT-switch) chemical proteomics approach for S-nitrosylation peptide enrichment and detection. We quantitatively compare the global S-nitrosylation profiles in wild-type Arabidopsis and gsnor1/hot5/par2 mutant using this approach, and identify 2,121 S-nitrosylation peptides in 1,595 protein groups, including many previously unrevealed S-nitrosylated proteins. These are 408 S-nitrosylated sites in 360 protein groups showing an accumulation in hot5-4 mutant when compared to wild type"],"journal":["Nature communications"],"pubmed_title":["FAT-switch-based quantitative S-nitrosoproteomics reveals a key role of GSNOR1 in regulating ER functions."],"pmcid":["PMC10241878"],"funding_grant_id":["RF1 AG064250"],"pubmed_authors":["Wang P","Song CP","Luo Z","Qu M","Jia B","Tao WA","Wang W","Qin G"],"additional_accession":[]},"is_claimable":false,"name":"FAT-switch-based quantitative S-nitrosoproteomics reveals a key role of GSNOR1 in regulating ER functions.","description":"Reversible protein S-nitrosylation regulates a wide range of biological functions and physiological activities in plants. However, it is challenging to quantitively determine the S-nitrosylation targets and dynamics in vivo. In this study, we develop a highly sensitive and efficient fluorous affinity tag-switch (FAT-switch) chemical proteomics approach for S-nitrosylation peptide enrichment and detection. We quantitatively compare the global S-nitrosylation profiles in wild-type Arabidopsis and gsnor1/hot5/par2 mutant using this approach, and identify 2,121 S-nitrosylation peptides in 1,595 protein groups, including many previously unrevealed S-nitrosylated proteins. These are 408 S-nitrosylated sites in 360 protein groups showing an accumulation in hot5-4 mutant when compared to wild type","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jun","modification":"2026-05-29T03:03:54.993Z","creation":"2025-02-19T02:38:10.115Z"},"accession":"S-EPMC10241878","cross_references":{"pubmed":["37277371"],"doi":["10.1038/s41467-023-39078-0"]}}