pubmed-article:17395470 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17395470 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
pubmed-article:17395470 | lifeskim:mentions | umls-concept:C0031453 | lld:lifeskim |
pubmed-article:17395470 | lifeskim:mentions | umls-concept:C1521970 | lld:lifeskim |
pubmed-article:17395470 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
pubmed-article:17395470 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
pubmed-article:17395470 | lifeskim:mentions | umls-concept:C0443199 | lld:lifeskim |
pubmed-article:17395470 | lifeskim:mentions | umls-concept:C0597358 | lld:lifeskim |
pubmed-article:17395470 | lifeskim:mentions | umls-concept:C1707491 | lld:lifeskim |
pubmed-article:17395470 | lifeskim:mentions | umls-concept:C0537638 | lld:lifeskim |
pubmed-article:17395470 | pubmed:issue | 11 | lld:pubmed |
pubmed-article:17395470 | pubmed:dateCreated | 2007-4-30 | lld:pubmed |
pubmed-article:17395470 | pubmed:abstractText | Endogenous opioid peptides consist of a conserved amino acid residue of Phe(3) and Phe(4), although their binding modes for opioid receptors have not been elucidated in detail. Endomorphin-2, which is highly selective and specific for the mu opioid receptor, possesses two Phe residues at the consecutive positions 3 and 4. In order to clarify the role of Phe(3) and Phe(4) in binding to the mu receptor, we synthesized a series of analogs in which Phe(3) and Phe(4) were replaced by various amino acids. It was found that the aromaticity of the Phe-beta-phenyl groups of Phe(3) and Phe(4) is a principal determinant of how strongly it binds to the receptor, although better molecular hydrophobicity reinforces the activity. The receptor binding subsites of Phe(3) and Phe(4) of endomorphin-2 were found to exhibit different structural requirements. The results suggest that [Trp(3)]endomorphin-2 (native endomorphin-1) and endomorphin-2 bind to different receptor subclasses. | lld:pubmed |
pubmed-article:17395470 | pubmed:language | eng | lld:pubmed |
pubmed-article:17395470 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17395470 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17395470 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17395470 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17395470 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17395470 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17395470 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17395470 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17395470 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17395470 | pubmed:month | Jun | lld:pubmed |
pubmed-article:17395470 | pubmed:issn | 0968-0896 | lld:pubmed |
pubmed-article:17395470 | pubmed:author | pubmed-author:HondaTakeshiT | lld:pubmed |
pubmed-article:17395470 | pubmed:author | pubmed-author:ShimohigashiY... | lld:pubmed |
pubmed-article:17395470 | pubmed:author | pubmed-author:ChumanYoshiro... | lld:pubmed |
pubmed-article:17395470 | pubmed:author | pubmed-author:NoseTakeruT | lld:pubmed |
pubmed-article:17395470 | pubmed:author | pubmed-author:ShirasuNaotoN | lld:pubmed |
pubmed-article:17395470 | pubmed:author | pubmed-author:FujitaTsugumi... | lld:pubmed |
pubmed-article:17395470 | pubmed:author | pubmed-author:IsozakiKaname... | lld:pubmed |
pubmed-article:17395470 | pubmed:author | pubmed-author:KawanoMichiak... | lld:pubmed |
pubmed-article:17395470 | pubmed:author | pubmed-author:ShigehiroDaik... | lld:pubmed |
pubmed-article:17395470 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17395470 | pubmed:day | 1 | lld:pubmed |
pubmed-article:17395470 | pubmed:volume | 15 | lld:pubmed |
pubmed-article:17395470 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17395470 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17395470 | pubmed:pagination | 3883-8 | lld:pubmed |
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pubmed-article:17395470 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17395470 | pubmed:articleTitle | Differential receptor binding characteristics of consecutive phenylalanines in micro-opioid specific peptide ligand endomorphin-2. | lld:pubmed |
pubmed-article:17395470 | pubmed:affiliation | Laboratory of Structure-Function Biochemistry, Department of Chemistry, Faculty and Graduate School of Sciences, Kyushu University, Fukuoka 812-8581, Japan. | lld:pubmed |
pubmed-article:17395470 | pubmed:publicationType | Journal Article | lld:pubmed |
http://linkedlifedata.com/r... | http://linkedlifedata.com/r... | pubmed-article:17395470 | lld:chembl |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17395470 | lld:pubmed |