{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Qi Q"],"funding":["national natural science foundation of china","natural science foundation of tianjin municipal science and technology commission","Shanghai Municipal Science and Technology Commission","shanghai municipal commission of economy and informatization","shanghai municipal health and health commission clinical research project"],"pagination":["3175-3193"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8666411"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["38(12)"],"pubmed_abstract":["Oxidative stress is one of the major causes leading to male infertility including asthenozoospermia. Hydrogen sulfide (H<sub>2</sub>S) has been widely recognized to be a potent antioxidant whose role is partially implemented by protein S-sulfhydration. However, protein S-sulfhydration has not been reported in germ cells. Therefore, we investigated whether asthenozoospermia could be associated with sperm protein S-sulfhydration. S-sulfhydrated proteins in human sperm were enriched via biotin-switch assay and analyzed using LC-MS/MS spectrometry. Two hundred forty-four S-sulfhydrated proteins were identified. Importantly, we validated that sperm histones H3.1 and H3.3 were the S-sulfhydrated proteins. Their S-sulfhydrated amino acid residue was Cysteine111. Abundances of S-sulfhydrated H3 (s"],"journal":["Journal of assisted reproduction and genetics"],"pubmed_title":["A novel posttranslational modification of histone, H3 S-sulfhydration, is down-regulated in asthenozoospermic sperm."],"pmcid":["PMC8666411"],"funding_grant_id":["20194Y0237","21140903600","81571495","81971443","21S11901000"],"pubmed_authors":["Pan H","Zhang F","Diao H","Sun S","Zhang M","Wan X","Zhang L","Li R","Jiang N","Wang J","Qi Q"],"additional_accession":[]},"is_claimable":false,"name":"A novel posttranslational modification of histone, H3 S-sulfhydration, is down-regulated in asthenozoospermic sperm.","description":"Oxidative stress is one of the major causes leading to male infertility including asthenozoospermia. Hydrogen sulfide (H<sub>2</sub>S) has been widely recognized to be a potent antioxidant whose role is partially implemented by protein S-sulfhydration. However, protein S-sulfhydration has not been reported in germ cells. Therefore, we investigated whether asthenozoospermia could be associated with sperm protein S-sulfhydration. S-sulfhydrated proteins in human sperm were enriched via biotin-switch assay and analyzed using LC-MS/MS spectrometry. Two hundred forty-four S-sulfhydrated proteins were identified. Importantly, we validated that sperm histones H3.1 and H3.3 were the S-sulfhydrated proteins. Their S-sulfhydrated amino acid residue was Cysteine111. Abundances of S-sulfhydrated H3 (s","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Dec","modification":"2026-04-08T17:54:20.543Z","creation":"2025-04-05T15:23:23.49Z"},"accession":"S-EPMC8666411","cross_references":{"pubmed":["34664184"],"doi":["10.1007/s10815-021-02314-x"]}}