| http://purl.uniprot.org/citations/17683036 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17683036 | http://www.w3.org/2000/01/rdf-schema#comment | "Nitric oxide (NO) enhances human sperm motility and capacitation associated with increased protein phosphorylation. NO activates soluble guanylyl cyclase, but can also modify protein function covalently via S-nitrosylation of cysteine. Remarkably, this mechanism remains unexplored in sperm although they depend on post-translational protein modification to achieve changes in function required for fertilisation. Our objective was to identify targets for S-nitrosylation in human sperm. Spermatozoa were incubated with NO donors and S-nitrosylated proteins were identified using the biotin switch assay and a proteomic approach using MS/MS. 240 S-nitrosylated proteins were detected in sperm incubated with S-nitroso-glutathione. Minimal levels were observed in glutathione or untreated samples. Proteins identified consistently based on multiple peptides included established targets for S-nitrosylation in other cells e.g. tubulin, GST and HSPs but also novel targets including A-kinase anchoring protein (AKAP) types 3 and 4, voltage-dependent anion-selective channel protein 3 and semenogelin 1 and 2. In situ localisation revealed S-nitrosylated targets on the postacrosomal region of the head and throughout the flagellum. Potential targets for S-nitrosylation in human sperm include physiologically significant proteins not previously reported in other cells. Their identification will provide novel insight into the mechanism of action of NO in spermatozoa."xsd:string |
| http://purl.uniprot.org/citations/17683036 | http://purl.org/dc/terms/identifier | "doi:10.1002/pmic.200700254"xsd:string |
| http://purl.uniprot.org/citations/17683036 | http://purl.uniprot.org/core/author | "Chen Y."xsd:string |
| http://purl.uniprot.org/citations/17683036 | http://purl.uniprot.org/core/author | "Scott J.L."xsd:string |
| http://purl.uniprot.org/citations/17683036 | http://purl.uniprot.org/core/author | "Barratt C.L."xsd:string |
| http://purl.uniprot.org/citations/17683036 | http://purl.uniprot.org/core/author | "Publicover S.J."xsd:string |
| http://purl.uniprot.org/citations/17683036 | http://purl.uniprot.org/core/author | "Lefievre L."xsd:string |
| http://purl.uniprot.org/citations/17683036 | http://purl.uniprot.org/core/author | "Conner S.J."xsd:string |
| http://purl.uniprot.org/citations/17683036 | http://purl.uniprot.org/core/author | "Ford W.C."xsd:string |
| http://purl.uniprot.org/citations/17683036 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17683036 | http://purl.uniprot.org/core/name | "Proteomics"xsd:string |
| http://purl.uniprot.org/citations/17683036 | http://purl.uniprot.org/core/pages | "3066-3084"xsd:string |
| http://purl.uniprot.org/citations/17683036 | http://purl.uniprot.org/core/title | "Human spermatozoa contain multiple targets for protein S-nitrosylation: an alternative mechanism of the modulation of sperm function by nitric oxide?"xsd:string |
| http://purl.uniprot.org/citations/17683036 | http://purl.uniprot.org/core/volume | "7"xsd:string |
| http://purl.uniprot.org/citations/17683036 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17683036 |
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