http://purl.uniprot.org/citations/16408020 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16408020 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16408020 | http://www.w3.org/2000/01/rdf-schema#comment | "Nitric oxide (NO) signaling through the formation of cGMP is well established; however, there seems to be an increasing role for cGMP-independent NO signaling. Although key molecular details remain unanswered, S-nitrosation represents an example of cGMP-independent NO signaling. This modification has garnered recent attention as it has been shown to modulate the function of several important biochemical pathways. Although an analogy to O-phosphorylation can be drawn, little is known about protein nitrosothiol regulation in vivo. In solution, NO readily reacts with oxygen to yield a nitrosating agent, but this process alone provides no specificity for nitrosation. This lack of specificity is exemplified by the in vitro poly-S-nitrosation of caspase-3 (Casp-3, ref. 6) and the ryanodine receptor. Previous in vivo work with Casp-3 suggests that a protein-assisted process may be responsible for selective S-nitrosation of the catalytic cysteine (Cys163). We demonstrated that a single cysteine in thioredoxin (Trx) is capable of a targeted, reversible transnitrosation reaction with Cys163 of Casp-3. A greater understanding of how S-nitrosation is mediated has broad implications for cGMP-independent signaling. The example described here also suggests a new role for Trx in the regulation of apoptosis."xsd:string |
http://purl.uniprot.org/citations/16408020 | http://purl.org/dc/terms/identifier | "doi:10.1038/nchembio720"xsd:string |
http://purl.uniprot.org/citations/16408020 | http://purl.org/dc/terms/identifier | "doi:10.1038/nchembio720"xsd:string |
http://purl.uniprot.org/citations/16408020 | http://purl.uniprot.org/core/author | "Marletta M.A."xsd:string |
http://purl.uniprot.org/citations/16408020 | http://purl.uniprot.org/core/author | "Marletta M.A."xsd:string |
http://purl.uniprot.org/citations/16408020 | http://purl.uniprot.org/core/author | "Mitchell D.A."xsd:string |
http://purl.uniprot.org/citations/16408020 | http://purl.uniprot.org/core/author | "Mitchell D.A."xsd:string |
http://purl.uniprot.org/citations/16408020 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/16408020 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/16408020 | http://purl.uniprot.org/core/name | "Nat. Chem. Biol."xsd:string |
http://purl.uniprot.org/citations/16408020 | http://purl.uniprot.org/core/name | "Nat. Chem. Biol."xsd:string |
http://purl.uniprot.org/citations/16408020 | http://purl.uniprot.org/core/pages | "154-158"xsd:string |
http://purl.uniprot.org/citations/16408020 | http://purl.uniprot.org/core/pages | "154-158"xsd:string |
http://purl.uniprot.org/citations/16408020 | http://purl.uniprot.org/core/title | "Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine."xsd:string |
http://purl.uniprot.org/citations/16408020 | http://purl.uniprot.org/core/title | "Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine."xsd:string |
http://purl.uniprot.org/citations/16408020 | http://purl.uniprot.org/core/volume | "1"xsd:string |
http://purl.uniprot.org/citations/16408020 | http://purl.uniprot.org/core/volume | "1"xsd:string |
http://purl.uniprot.org/citations/16408020 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16408020 |
http://purl.uniprot.org/citations/16408020 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16408020 |
http://purl.uniprot.org/citations/16408020 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16408020 |
http://purl.uniprot.org/citations/16408020 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16408020 |
http://purl.uniprot.org/uniprot/P10599 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/16408020 |
http://purl.uniprot.org/uniprot/P10599#attribution-58EDDDDA29DA2CFF36382D12AD9BE367 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/16408020 |