pubmed-article:1534125 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1534125 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
pubmed-article:1534125 | lifeskim:mentions | umls-concept:C0079883 | lld:lifeskim |
pubmed-article:1534125 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
pubmed-article:1534125 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
pubmed-article:1534125 | lifeskim:mentions | umls-concept:C1148574 | lld:lifeskim |
pubmed-article:1534125 | lifeskim:mentions | umls-concept:C0243076 | lld:lifeskim |
pubmed-article:1534125 | pubmed:issue | 10 | lld:pubmed |
pubmed-article:1534125 | pubmed:dateCreated | 1992-6-23 | lld:pubmed |
pubmed-article:1534125 | pubmed:abstractText | A series of substituted 3-(2-carboxyindol-3-yl)propionic acids was synthesized and tested as antagonists for the strychnine-insensitive glycine binding site of the NMDA receptor. Chlorine, and other small electron-withdrawing substituents in the 4- and 6-positions of the indole ring, greatly enhanced binding and selectivity for the glycine site over the glutamate site of the NMDA receptor; one of the most potent compounds is 3-(4,6-dichloro-2-carboxyindol-3-yl)propionic acid (IC50 = 170 nM; greater than 2100-fold selective for glycine). The importance of a heteroatom NH and the enhancing effect of the propionic acid side chain were demonstrated and are consistent with previous results which suggest the presence of a pocket on the receptor which can accept an acidic side chain. Substitution of a sulfur at C3 led to the most potent compound 3-[(carboxymethyl)thio]-2-carboxy-4,6-dichloroindole (IC50 = 100 nM). | lld:pubmed |
pubmed-article:1534125 | pubmed:language | eng | lld:pubmed |
pubmed-article:1534125 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1534125 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1534125 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1534125 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1534125 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1534125 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1534125 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1534125 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1534125 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1534125 | pubmed:month | May | lld:pubmed |
pubmed-article:1534125 | pubmed:issn | 0022-2623 | lld:pubmed |
pubmed-article:1534125 | pubmed:author | pubmed-author:KehneJ HJH | lld:pubmed |
pubmed-article:1534125 | pubmed:author | pubmed-author:WhiteH SHS | lld:pubmed |
pubmed-article:1534125 | pubmed:author | pubmed-author:McDonaldI AIA | lld:pubmed |
pubmed-article:1534125 | pubmed:author | pubmed-author:StewartK TKT | lld:pubmed |
pubmed-article:1534125 | pubmed:author | pubmed-author:HarrisonB LBL | lld:pubmed |
pubmed-article:1534125 | pubmed:author | pubmed-author:BaronB MBM | lld:pubmed |
pubmed-article:1534125 | pubmed:author | pubmed-author:SalituroF GFG | lld:pubmed |
pubmed-article:1534125 | pubmed:author | pubmed-author:MeekC LCL | lld:pubmed |
pubmed-article:1534125 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1534125 | pubmed:day | 15 | lld:pubmed |
pubmed-article:1534125 | pubmed:volume | 35 | lld:pubmed |
pubmed-article:1534125 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1534125 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1534125 | pubmed:pagination | 1791-9 | lld:pubmed |
pubmed-article:1534125 | pubmed:dateRevised | 2003-11-14 | lld:pubmed |
pubmed-article:1534125 | pubmed:meshHeading | pubmed-meshheading:1534125-... | lld:pubmed |
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pubmed-article:1534125 | pubmed:meshHeading | pubmed-meshheading:1534125-... | lld:pubmed |
pubmed-article:1534125 | pubmed:year | 1992 | lld:pubmed |
pubmed-article:1534125 | pubmed:articleTitle | 3-(2-Carboxyindol-3-yl)propionic acid-based antagonists of the N-methyl-D-aspartic acid receptor associated glycine binding site. | lld:pubmed |
pubmed-article:1534125 | pubmed:affiliation | Marion Merrell Dow Research Institute, Cincinnati, Ohio 45215. | lld:pubmed |
pubmed-article:1534125 | pubmed:publicationType | Journal Article | lld:pubmed |
http://linkedlifedata.com/r... | http://linkedlifedata.com/r... | pubmed-article:1534125 | lld:chembl |