pubmed-article:12482429 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12482429 | lifeskim:mentions | umls-concept:C0037903 | lld:lifeskim |
pubmed-article:12482429 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:12482429 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
pubmed-article:12482429 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
pubmed-article:12482429 | lifeskim:mentions | umls-concept:C0243077 | lld:lifeskim |
pubmed-article:12482429 | lifeskim:mentions | umls-concept:C0750502 | lld:lifeskim |
pubmed-article:12482429 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:12482429 | pubmed:dateCreated | 2002-12-16 | lld:pubmed |
pubmed-article:12482429 | pubmed:abstractText | A series of short-chain analogues of N-palmitoylsphingosine-1-phosphate, modified by replacement of the phosphate and the long alkenyl side chain with hydrolytically stable difluoromethylene phosphonate and phenyl, respectively, were prepared to study the structure-activity relationship for inhibition of sphingomyelinase. The study revealed that inhibition is highly dependent upon the stereochemistry of the asymmetric centers of the acylamino moiety, and resulted in identification of a non-competitive inhibitor with the same level of inhibitory activity of schyphostatin, the most potent of the few known small molecular inhibitors of sphingomyelinase. | lld:pubmed |
pubmed-article:12482429 | pubmed:language | eng | lld:pubmed |
pubmed-article:12482429 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12482429 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12482429 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12482429 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12482429 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12482429 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12482429 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12482429 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12482429 | pubmed:month | Jan | lld:pubmed |
pubmed-article:12482429 | pubmed:issn | 0960-894X | lld:pubmed |
pubmed-article:12482429 | pubmed:author | pubmed-author:SoedaShinjiS | lld:pubmed |
pubmed-article:12482429 | pubmed:author | pubmed-author:YokomatsuTsut... | lld:pubmed |
pubmed-article:12482429 | pubmed:author | pubmed-author:MuranoTetsuoT | lld:pubmed |
pubmed-article:12482429 | pubmed:author | pubmed-author:ShibuyaShiros... | lld:pubmed |
pubmed-article:12482429 | pubmed:author | pubmed-author:ShimenoHirosh... | lld:pubmed |
pubmed-article:12482429 | pubmed:author | pubmed-author:TsujiYoshiaki... | lld:pubmed |
pubmed-article:12482429 | pubmed:author | pubmed-author:AkiyamaTakesh... | lld:pubmed |
pubmed-article:12482429 | pubmed:author | pubmed-author:KoizumiJunich... | lld:pubmed |
pubmed-article:12482429 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12482429 | pubmed:day | 20 | lld:pubmed |
pubmed-article:12482429 | pubmed:volume | 13 | lld:pubmed |
pubmed-article:12482429 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12482429 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12482429 | pubmed:pagination | 229-36 | lld:pubmed |
pubmed-article:12482429 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:12482429 | pubmed:meshHeading | pubmed-meshheading:12482429... | lld:pubmed |
pubmed-article:12482429 | pubmed:meshHeading | pubmed-meshheading:12482429... | lld:pubmed |
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pubmed-article:12482429 | pubmed:meshHeading | pubmed-meshheading:12482429... | lld:pubmed |
pubmed-article:12482429 | pubmed:meshHeading | pubmed-meshheading:12482429... | lld:pubmed |
pubmed-article:12482429 | pubmed:meshHeading | pubmed-meshheading:12482429... | lld:pubmed |
pubmed-article:12482429 | pubmed:meshHeading | pubmed-meshheading:12482429... | lld:pubmed |
pubmed-article:12482429 | pubmed:meshHeading | pubmed-meshheading:12482429... | lld:pubmed |
pubmed-article:12482429 | pubmed:meshHeading | pubmed-meshheading:12482429... | lld:pubmed |
pubmed-article:12482429 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:12482429 | pubmed:articleTitle | Synthesis of non-competitive inhibitors of sphingomyelinases with significant activity. | lld:pubmed |
pubmed-article:12482429 | pubmed:affiliation | School of Pharmacy, Tokyo University of Pharmacy & Life Science, 1432-1 Horinouchi, Hachioji, Tokyo 192-0392, Japan. yokomatu@ps.toyaku.ac.jp | lld:pubmed |
pubmed-article:12482429 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12482429 | pubmed:publicationType | In Vitro | lld:pubmed |
http://linkedlifedata.com/r... | http://linkedlifedata.com/r... | pubmed-article:12482429 | lld:chembl |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12482429 | lld:pubmed |