| pubmed-article:18952440 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18952440 | lifeskim:mentions | umls-concept:C0061355 | lld:lifeskim |
| pubmed-article:18952440 | lifeskim:mentions | umls-concept:C0026377 | lld:lifeskim |
| pubmed-article:18952440 | lifeskim:mentions | umls-concept:C1552603 | lld:lifeskim |
| pubmed-article:18952440 | lifeskim:mentions | umls-concept:C1706202 | lld:lifeskim |
| pubmed-article:18952440 | pubmed:issue | 23 | lld:pubmed |
| pubmed-article:18952440 | pubmed:dateCreated | 2008-11-17 | lld:pubmed |
| pubmed-article:18952440 | pubmed:abstractText | To elucidate the receptor-bound conformation of glucagon-like peptide-1 (GLP-1), a series of conformationally constrained GLP-1 analogues were synthesized by introducing lactam bridges between Lys(i) and Glu(i)(+4) to form alpha-helices at various positions. The activity and affinity of these analogues to GLP-1 receptors suggested that the receptor-bound conformation comprises two alpha-helical segments between residues 11-21 and 23-34. It is notable that the N-terminal alpha-helix is extended to Thr(11), and that Gly(22) plays a pivotal role in arranging the two alpha-helices. Based on these findings, a highly potent bicyclic GLP-1 analogue was synthesized which is the most conformationally constrained GLP-1 analogue reported to date. | lld:pubmed |
| pubmed-article:18952440 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18952440 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18952440 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18952440 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18952440 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18952440 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18952440 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18952440 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18952440 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:18952440 | pubmed:issn | 1464-3391 | lld:pubmed |
| pubmed-article:18952440 | pubmed:author | pubmed-author:AhnJung-MoJM | lld:pubmed |
| pubmed-article:18952440 | pubmed:author | pubmed-author:BeinbornMarti... | lld:pubmed |
| pubmed-article:18952440 | pubmed:author | pubmed-author:MurageEunice... | lld:pubmed |
| pubmed-article:18952440 | pubmed:author | pubmed-author:SchroederJona... | lld:pubmed |
| pubmed-article:18952440 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18952440 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:18952440 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:18952440 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18952440 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18952440 | pubmed:pagination | 10106-12 | lld:pubmed |
| pubmed-article:18952440 | pubmed:meshHeading | pubmed-meshheading:18952440... | lld:pubmed |
| pubmed-article:18952440 | pubmed:meshHeading | pubmed-meshheading:18952440... | lld:pubmed |
| pubmed-article:18952440 | pubmed:meshHeading | pubmed-meshheading:18952440... | lld:pubmed |
| pubmed-article:18952440 | pubmed:meshHeading | pubmed-meshheading:18952440... | lld:pubmed |
| pubmed-article:18952440 | pubmed:meshHeading | pubmed-meshheading:18952440... | lld:pubmed |
| pubmed-article:18952440 | pubmed:meshHeading | pubmed-meshheading:18952440... | lld:pubmed |
| pubmed-article:18952440 | pubmed:meshHeading | pubmed-meshheading:18952440... | lld:pubmed |
| pubmed-article:18952440 | pubmed:meshHeading | pubmed-meshheading:18952440... | lld:pubmed |
| pubmed-article:18952440 | pubmed:meshHeading | pubmed-meshheading:18952440... | lld:pubmed |
| pubmed-article:18952440 | pubmed:meshHeading | pubmed-meshheading:18952440... | lld:pubmed |
| pubmed-article:18952440 | pubmed:meshHeading | pubmed-meshheading:18952440... | lld:pubmed |
| pubmed-article:18952440 | pubmed:meshHeading | pubmed-meshheading:18952440... | lld:pubmed |
| pubmed-article:18952440 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18952440 | pubmed:articleTitle | Search for alpha-helical propensity in the receptor-bound conformation of glucagon-like peptide-1. | lld:pubmed |
| pubmed-article:18952440 | pubmed:affiliation | Department of Chemistry, University of Texas at Dallas, Richardson, TX 75080, USA. | lld:pubmed |
| pubmed-article:18952440 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18952440 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | http://linkedlifedata.com/r... | pubmed-article:18952440 | lld:chembl |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18952440 | lld:pubmed |
