| pubmed-article:2282462 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2282462 | lifeskim:mentions | umls-concept:C0999699 | lld:lifeskim |
| pubmed-article:2282462 | lifeskim:mentions | umls-concept:C0006255 | lld:lifeskim |
| pubmed-article:2282462 | lifeskim:mentions | umls-concept:C0079284 | lld:lifeskim |
| pubmed-article:2282462 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:2282462 | lifeskim:mentions | umls-concept:C0059282 | lld:lifeskim |
| pubmed-article:2282462 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:2282462 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:2282462 | pubmed:dateCreated | 1991-3-15 | lld:pubmed |
| pubmed-article:2282462 | pubmed:abstractText | 1. We describe the results of a structure-activity study in which the C-terminal hexapeptide of the endothelins, endothelin (16-21), is compared with shorter fragments; hexapeptides bearing amino-acid substitutions and the corresponding C-terminal fragments of sarafotoxins. The guinea-pig bronchus was used in this study since it is the most sensitive preparation for endothelin (16-21) thus far developed. 2. The biological results obtained with endothelin (16-21) and analogues demonstrate that the contractile activity of the C-terminal hexapeptide of endothelin on the guinea-pig bronchus depends on quite close structural requirements, strongly suggestive of a receptor interaction. The following features appear to be essential for the biological activity: (a) the C-terminal free carboxylic function; (b) the L-configuration of Trp-21; (c) the beta-carboxylic function of Asp-18; (d) the presence of Leu-17 and (e) the imidazole moiety of His-16. 3. The hexapeptide corresponding to the C-terminal portion of sarafotoxin, sarafotoxin (16-21), was devoid of biological activity. This behaviour might be related to the proposed existence of more than one receptor for the endothelin/sarafotoxin family in the guinea-pig bronchus. | lld:pubmed |
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| pubmed-article:2282462 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2282462 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2282462 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2282462 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2282462 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:2282462 | pubmed:issn | 0007-1188 | lld:pubmed |
| pubmed-article:2282462 | pubmed:author | pubmed-author:MaggiC ACA | lld:pubmed |
| pubmed-article:2282462 | pubmed:author | pubmed-author:PatacchiniRR | lld:pubmed |
| pubmed-article:2282462 | pubmed:author | pubmed-author:RoveroPP | lld:pubmed |
| pubmed-article:2282462 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2282462 | pubmed:volume | 101 | lld:pubmed |
| pubmed-article:2282462 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2282462 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2282462 | pubmed:pagination | 232-4 | lld:pubmed |
| pubmed-article:2282462 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2282462 | pubmed:meshHeading | pubmed-meshheading:2282462-... | lld:pubmed |
| pubmed-article:2282462 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2282462 | pubmed:articleTitle | Structure-activity studies on endothelin (16-21), the C-terminal hexapeptide of the endothelins, in the guinea-pig bronchus. | lld:pubmed |
| pubmed-article:2282462 | pubmed:affiliation | Chemistry Department, A. Menarini Pharmaceuticals, Firenze, Italy. | lld:pubmed |
| pubmed-article:2282462 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2282462 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:2282462 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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