pubmed-article:18497292 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18497292 | lifeskim:mentions | umls-concept:C1383501 | lld:lifeskim |
pubmed-article:18497292 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:18497292 | lifeskim:mentions | umls-concept:C1456398 | lld:lifeskim |
pubmed-article:18497292 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:18497292 | pubmed:issue | 5879 | lld:pubmed |
pubmed-article:18497292 | pubmed:dateCreated | 2008-5-23 | lld:pubmed |
pubmed-article:18497292 | pubmed:abstractText | Nitric oxide acts substantially in cellular signal transduction through stimulus-coupled S-nitrosylation of cysteine residues. The mechanisms that might subserve protein denitrosylation in cellular signaling remain uncharacterized. Our search for denitrosylase activities focused on caspase-3, an exemplar of stimulus-dependent denitrosylation, and identified thioredoxin and thioredoxin reductase in a biochemical screen. In resting human lymphocytes, thioredoxin-1 actively denitrosylated cytosolic caspase-3 and thereby maintained a low steady-state amount of S-nitrosylation. Upon stimulation of Fas, thioredoxin-2 mediated denitrosylation of mitochondria-associated caspase-3, a process required for caspase-3 activation, and promoted apoptosis. Inhibition of thioredoxin-thioredoxin reductases enabled identification of additional substrates subject to endogenous S-nitrosylation. Thus, specific enzymatic mechanisms may regulate basal and stimulus-induced denitrosylation in mammalian cells. | lld:pubmed |
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pubmed-article:18497292 | pubmed:language | eng | lld:pubmed |
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pubmed-article:18497292 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:18497292 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18497292 | pubmed:month | May | lld:pubmed |
pubmed-article:18497292 | pubmed:issn | 1095-9203 | lld:pubmed |
pubmed-article:18497292 | pubmed:author | pubmed-author:StamlerJonath... | lld:pubmed |
pubmed-article:18497292 | pubmed:author | pubmed-author:HessDouglas... | lld:pubmed |
pubmed-article:18497292 | pubmed:author | pubmed-author:BenharMoranM | lld:pubmed |
pubmed-article:18497292 | pubmed:author | pubmed-author:ForresterMich... | lld:pubmed |
pubmed-article:18497292 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:18497292 | pubmed:day | 23 | lld:pubmed |
pubmed-article:18497292 | pubmed:volume | 320 | lld:pubmed |
pubmed-article:18497292 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18497292 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18497292 | pubmed:pagination | 1050-4 | lld:pubmed |
pubmed-article:18497292 | pubmed:dateRevised | 2011-6-7 | lld:pubmed |
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pubmed-article:18497292 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18497292 | pubmed:articleTitle | Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins. | lld:pubmed |
pubmed-article:18497292 | pubmed:affiliation | Department of Medicine, Duke University Medical Center, Durham, NC 27710, USA. | lld:pubmed |
pubmed-article:18497292 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18497292 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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