pubmed-article:17055291 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17055291 | lifeskim:mentions | umls-concept:C0439849 | lld:lifeskim |
pubmed-article:17055291 | lifeskim:mentions | umls-concept:C1514468 | lld:lifeskim |
pubmed-article:17055291 | lifeskim:mentions | umls-concept:C1442080 | lld:lifeskim |
pubmed-article:17055291 | lifeskim:mentions | umls-concept:C1881708 | lld:lifeskim |
pubmed-article:17055291 | lifeskim:mentions | umls-concept:C0445223 | lld:lifeskim |
pubmed-article:17055291 | lifeskim:mentions | umls-concept:C0205251 | lld:lifeskim |
pubmed-article:17055291 | lifeskim:mentions | umls-concept:C0332472 | lld:lifeskim |
pubmed-article:17055291 | lifeskim:mentions | umls-concept:C0599748 | lld:lifeskim |
pubmed-article:17055291 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
pubmed-article:17055291 | lifeskim:mentions | umls-concept:C2827424 | lld:lifeskim |
pubmed-article:17055291 | lifeskim:mentions | umls-concept:C1552599 | lld:lifeskim |
pubmed-article:17055291 | lifeskim:mentions | umls-concept:C1704787 | lld:lifeskim |
pubmed-article:17055291 | lifeskim:mentions | umls-concept:C1705938 | lld:lifeskim |
pubmed-article:17055291 | lifeskim:mentions | umls-concept:C1547179 | lld:lifeskim |
pubmed-article:17055291 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
pubmed-article:17055291 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
pubmed-article:17055291 | lifeskim:mentions | umls-concept:C1453711 | lld:lifeskim |
pubmed-article:17055291 | lifeskim:mentions | umls-concept:C1869313 | lld:lifeskim |
pubmed-article:17055291 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:17055291 | pubmed:dateCreated | 2007-1-8 | lld:pubmed |
pubmed-article:17055291 | pubmed:abstractText | Resolvin D1 (RvD1) and protectin D1 (Neuroprotectin D1, PD1/NPD1) are newly identified anti-inflammatory lipid mediators biosynthesized from docosahexaenoic acid (DHA). In this report, the spectra-structure correlations and fragmentation mechanisms were studied using electrospray low-energy collision-induced dissociation tandem mass spectrometry (MS/MS) for biogenic RvD1 and PD1, as well as mono-hydroxy-DHA and related hydroperoxy-DHA. The loss of H2O and CO2 in the spectra indicates the number of functional group(s). Chain-cut ions are the signature of the positions and numbers of functional groups and double bonds. The observed chain-cut ion is equivalent to a hypothetical homolytic-segment (cc, cm, mc, or mm) with addition or extraction of up to 2 protons (H). The alpha-cleavage ions are equivalent to: [cc + H], with H from the hydroxyl through a beta-ene or gamma-ene rearrangement; [cm - 2H], with 2H from hydroxyls of PD1 through a gamma-ene rearrangement, or 1H from the hydroxyl and the other H from the alpha-carbon of mono-HDHA through an alpha-H-beta-ene rearrangement; [mc - H], with H from hydroxyl through a beta-ene or gamma-ene rearrangement, or from the alpha-carbon through an alpha-H-beta-ene rearrangement; or [mm] through charge-direct fragmentations. The beta-ene or gamma-ene facilitates the H shift to gamma position and alpha-cleavage. Deuterium labeling confirmed the assignment of MS/MS ions and the fragmentation mechanisms. Based on the MS/MS spectra and fragmentation mechanisms, we identified RvD1, PD1, and mono-hydroxy-DHA products in human neutrophils and blood, trout head-kidney, and stroke-injury murine brain-tissue. | lld:pubmed |
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pubmed-article:17055291 | pubmed:language | eng | lld:pubmed |
pubmed-article:17055291 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17055291 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:17055291 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17055291 | pubmed:month | Jan | lld:pubmed |
pubmed-article:17055291 | pubmed:issn | 1044-0305 | lld:pubmed |
pubmed-article:17055291 | pubmed:author | pubmed-author:WinSS | lld:pubmed |
pubmed-article:17055291 | pubmed:author | pubmed-author:SerhanCharles... | lld:pubmed |
pubmed-article:17055291 | pubmed:author | pubmed-author:YangRongR | lld:pubmed |
pubmed-article:17055291 | pubmed:author | pubmed-author:SongHongH | lld:pubmed |
pubmed-article:17055291 | pubmed:author | pubmed-author:PetasisNicos... | lld:pubmed |
pubmed-article:17055291 | pubmed:author | pubmed-author:GotlingerKath... | lld:pubmed |
pubmed-article:17055291 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17055291 | pubmed:volume | 18 | lld:pubmed |
pubmed-article:17055291 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17055291 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17055291 | pubmed:pagination | 128-44 | lld:pubmed |
pubmed-article:17055291 | pubmed:dateRevised | 2011-4-8 | lld:pubmed |
pubmed-article:17055291 | pubmed:meshHeading | pubmed-meshheading:17055291... | lld:pubmed |
pubmed-article:17055291 | pubmed:meshHeading | pubmed-meshheading:17055291... | lld:pubmed |
pubmed-article:17055291 | pubmed:meshHeading | pubmed-meshheading:17055291... | lld:pubmed |
pubmed-article:17055291 | pubmed:meshHeading | pubmed-meshheading:17055291... | lld:pubmed |
pubmed-article:17055291 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17055291 | pubmed:articleTitle | Resolvin D1, protectin D1, and related docosahexaenoic acid-derived products: Analysis via electrospray/low energy tandem mass spectrometry based on spectra and fragmentation mechanisms. | lld:pubmed |
pubmed-article:17055291 | pubmed:affiliation | Analytical Core, Center for Experimental Therapeutics and Reperfusion Injury, Department of Anesthesiology, Perioperative and Pain Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA. | lld:pubmed |
pubmed-article:17055291 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17055291 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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