| pubmed-article:8069595 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8069595 | lifeskim:mentions | umls-concept:C0014597 | lld:lifeskim |
| pubmed-article:8069595 | lifeskim:mentions | umls-concept:C0162714 | lld:lifeskim |
| pubmed-article:8069595 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:8069595 | lifeskim:mentions | umls-concept:C0031164 | lld:lifeskim |
| pubmed-article:8069595 | lifeskim:mentions | umls-concept:C0205549 | lld:lifeskim |
| pubmed-article:8069595 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8069595 | pubmed:dateCreated | 1994-9-29 | lld:pubmed |
| pubmed-article:8069595 | pubmed:abstractText | The influence of the aminoterminal substituent in a homologous series of tetrapeptide analogs on transport across Caco-2 cell monolayers was studied. In a series of pyridylcarboxamide regioisomers, the 2-pyridyl isomer was significantly more permeable than either the 3- or 4-congeners. The uniqueness of this peptide was further suggested by examining the partitioning behavior between heptane and ethylene glycol, a system which has been developed as a simple estimate of the desolvation energy or hydrogen bonding potential of a peptide. In this model, the 2-isomer has a much larger partition coefficient than either the 3- or 4-analogs, consistent with its being less solvated than expected based on simple structural considerations. Factors possibly contributing to this decreased effective polarity could be steric interactions or intramolecular hydrogen bonding. | lld:pubmed |
| pubmed-article:8069595 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8069595 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8069595 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8069595 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8069595 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8069595 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8069595 | pubmed:issn | 1061-186X | lld:pubmed |
| pubmed-article:8069595 | pubmed:author | pubmed-author:HesterJ BJB | lld:pubmed |
| pubmed-article:8069595 | pubmed:author | pubmed-author:ConradiR ARA | lld:pubmed |
| pubmed-article:8069595 | pubmed:author | pubmed-author:BurtonP SPS | lld:pubmed |
| pubmed-article:8069595 | pubmed:author | pubmed-author:HilgersA RAR | lld:pubmed |
| pubmed-article:8069595 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8069595 | pubmed:volume | 2 | lld:pubmed |
| pubmed-article:8069595 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8069595 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8069595 | pubmed:pagination | 167-71 | lld:pubmed |
| pubmed-article:8069595 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
| pubmed-article:8069595 | pubmed:meshHeading | pubmed-meshheading:8069595-... | lld:pubmed |
| pubmed-article:8069595 | pubmed:meshHeading | pubmed-meshheading:8069595-... | lld:pubmed |
| pubmed-article:8069595 | pubmed:meshHeading | pubmed-meshheading:8069595-... | lld:pubmed |
| pubmed-article:8069595 | pubmed:meshHeading | pubmed-meshheading:8069595-... | lld:pubmed |
| pubmed-article:8069595 | pubmed:meshHeading | pubmed-meshheading:8069595-... | lld:pubmed |
| pubmed-article:8069595 | pubmed:meshHeading | pubmed-meshheading:8069595-... | lld:pubmed |
| pubmed-article:8069595 | pubmed:meshHeading | pubmed-meshheading:8069595-... | lld:pubmed |
| pubmed-article:8069595 | pubmed:meshHeading | pubmed-meshheading:8069595-... | lld:pubmed |
| pubmed-article:8069595 | pubmed:meshHeading | pubmed-meshheading:8069595-... | lld:pubmed |
| pubmed-article:8069595 | pubmed:meshHeading | pubmed-meshheading:8069595-... | lld:pubmed |
| pubmed-article:8069595 | pubmed:meshHeading | pubmed-meshheading:8069595-... | lld:pubmed |
| pubmed-article:8069595 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8069595 | pubmed:articleTitle | Epithelial cell permeability of a series of peptidic HIV protease inhibitors: aminoterminal substituent effects. | lld:pubmed |
| pubmed-article:8069595 | pubmed:affiliation | Drug Delivery Systems Research, Upjohn Laboratories, Upjohn Company, Kalamazoo, MI 49001. | lld:pubmed |
| pubmed-article:8069595 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8069595 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8069595 | lld:pubmed |
