pubmed-article:10428468 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10428468 | lifeskim:mentions | umls-concept:C0031670 | lld:lifeskim |
pubmed-article:10428468 | lifeskim:mentions | umls-concept:C0085732 | lld:lifeskim |
pubmed-article:10428468 | pubmed:issue | 1-2 | lld:pubmed |
pubmed-article:10428468 | pubmed:dateCreated | 1999-8-16 | lld:pubmed |
pubmed-article:10428468 | pubmed:abstractText | The N-acylphosphatidylethanolamine-hydrolysing phospholipase D (NAPE-PLD) generates N-acylethanolamines, including N-arachidonoyl-ethanolamine (anandamide), that may be neuroprotective and analgesic. The properties of NAPE-PLD from rat heart and brain microsomes are investigated and compared to those of other PLDs. NAPE-PLD is inhibited by the fatty acid aminohydrolase inhibitor MAFP in high concentrations (> or = 100 microM) while PMSF in high concentrations (10 mM) tends to stabilise NAPE-PLD activity. Oleate inhibits NAPE-PLD but the enzyme is not affected by PIP2, alpha-synuclein or mastoparan. Furthermore, it is for the first time reported that NAPE-PLD is not capable of catalysing a transphosphatidylation reaction like most other known PLDs. | lld:pubmed |
pubmed-article:10428468 | pubmed:language | eng | lld:pubmed |
pubmed-article:10428468 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10428468 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10428468 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10428468 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10428468 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10428468 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10428468 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10428468 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10428468 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10428468 | pubmed:month | Jul | lld:pubmed |
pubmed-article:10428468 | pubmed:issn | 0014-5793 | lld:pubmed |
pubmed-article:10428468 | pubmed:author | pubmed-author:HansenH SHS | lld:pubmed |
pubmed-article:10428468 | pubmed:author | pubmed-author:PetersenGG | lld:pubmed |
pubmed-article:10428468 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10428468 | pubmed:day | 16 | lld:pubmed |
pubmed-article:10428468 | pubmed:volume | 455 | lld:pubmed |
pubmed-article:10428468 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10428468 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10428468 | pubmed:pagination | 41-4 | lld:pubmed |
pubmed-article:10428468 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:10428468 | pubmed:meshHeading | pubmed-meshheading:10428468... | lld:pubmed |
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pubmed-article:10428468 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10428468 | pubmed:articleTitle | N-acylphosphatidylethanolamine-hydrolysing phospholipase D lacks the ability to transphosphatidylate. | lld:pubmed |
pubmed-article:10428468 | pubmed:affiliation | Department of Pharmacology, The Royal Danish School of Pharmacy, Copenhagen. | lld:pubmed |
pubmed-article:10428468 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10428468 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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