| pubmed-article:8982281 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8982281 | lifeskim:mentions | umls-concept:C0036534 | lld:lifeskim |
| pubmed-article:8982281 | lifeskim:mentions | umls-concept:C0042395 | lld:lifeskim |
| pubmed-article:8982281 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:8982281 | lifeskim:mentions | umls-concept:C0071163 | lld:lifeskim |
| pubmed-article:8982281 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:8982281 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
| pubmed-article:8982281 | lifeskim:mentions | umls-concept:C1510827 | lld:lifeskim |
| pubmed-article:8982281 | lifeskim:mentions | umls-concept:C0971125 | lld:lifeskim |
| pubmed-article:8982281 | lifeskim:mentions | umls-concept:C1875307 | lld:lifeskim |
| pubmed-article:8982281 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:8982281 | pubmed:dateCreated | 1997-1-23 | lld:pubmed |
| pubmed-article:8982281 | pubmed:abstractText | Rabbit secretin, which differs from all other mammalian secretins in having a Leu residue in position 6 (instead of Phe) and a basic residue (Arg) in position 16, had a lower affinity than porcine secretion on recombinant rat secretin receptors but had a greater affinity than porcine secretin on recombinant rat VIP1 and PACAP I receptors. Synthetic [L6] porcine secretin had a reduced potency on secretin and VIP1 receptors whereas [R16] porcine secretin had a similar binding profile as rabbit secretin. Thus, an arginine residue in position 16 reduced 3-fold the affinity of secretin for secretin receptors but increased 30-fold its affinity for the VIP1 and PACAP I receptors. The introduction of an arginine residue in position 16, instead of glutamine, in VIP and PACAP had a similar effect: [R16] VIP and [R16] PACAP had 3- to 10-fold higher affinities than VIP and PACAP for VIP1 and PACAP I receptors, and 3-fold lower affinities for the secretin receptors. The three [R16] peptides also had a reduced potency on the chimeric receptor consisting of the N-terminal part of the secretin receptor grafted on the VIP1 receptor, and an enhanced potency on the chimeric receptor consisting of the N-terminal part of VIP1 receptor grafted on the secretin receptor, indicating that position 16 of each ligand interacted with the N-terminal extracellular domain of the receptors. | lld:pubmed |
| pubmed-article:8982281 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8982281 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8982281 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8982281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8982281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8982281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8982281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8982281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8982281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8982281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8982281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8982281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8982281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8982281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8982281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8982281 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8982281 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8982281 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:8982281 | pubmed:author | pubmed-author:RobberechtPP | lld:pubmed |
| pubmed-article:8982281 | pubmed:author | pubmed-author:De NeefPP | lld:pubmed |
| pubmed-article:8982281 | pubmed:author | pubmed-author:VandermeersAA | lld:pubmed |
| pubmed-article:8982281 | pubmed:author | pubmed-author:Vandermeers-P... | lld:pubmed |
| pubmed-article:8982281 | pubmed:author | pubmed-author:WaelbroeckMM | lld:pubmed |
| pubmed-article:8982281 | pubmed:author | pubmed-author:GourletPP | lld:pubmed |
| pubmed-article:8982281 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8982281 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:8982281 | pubmed:volume | 1314 | lld:pubmed |
| pubmed-article:8982281 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8982281 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8982281 | pubmed:pagination | 267-73 | lld:pubmed |
| pubmed-article:8982281 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:8982281 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8982281 | pubmed:articleTitle | Effect of introduction of an arginine16 in VIP, PACAP and secretin on ligand affinity for the receptors. | lld:pubmed |
| pubmed-article:8982281 | pubmed:affiliation | Department of Biochemistry and Nutrition, Faculty of Medicine, Université Libre de Bruxelles, Belgium. | lld:pubmed |
| pubmed-article:8982281 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8982281 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8982281 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8982281 | lld:pubmed |
