| pubmed-article:164658 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:164658 | lifeskim:mentions | umls-concept:C0037949 | lld:lifeskim |
| pubmed-article:164658 | lifeskim:mentions | umls-concept:C0030095 | lld:lifeskim |
| pubmed-article:164658 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:164658 | lifeskim:mentions | umls-concept:C0441472 | lld:lifeskim |
| pubmed-article:164658 | lifeskim:mentions | umls-concept:C0243071 | lld:lifeskim |
| pubmed-article:164658 | lifeskim:mentions | umls-concept:C1880177 | lld:lifeskim |
| pubmed-article:164658 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:164658 | pubmed:dateCreated | 1975-6-25 | lld:pubmed |
| pubmed-article:164658 | pubmed:abstractText | This investigation was undertaken to evaluate the functional contribution of the peptide backbone of oxytocin in its interaction with receptor. Corey-Pauling-Koltun models of (Gly-7) deaminooxytocin, deaminotocinamide, and their respective retro-D-analogs built in any specific conformation (e.g., the Walter-Urry model for oxytocin) have a quai-equivalent topochemical arrangement of amino-acid side chains; however, the CO and NH elements of the peptide backbone of the retro-D-analog are reversed. The retro-D-analogs of deaminotocinamide and (Gly-7) deaminooxytocin (prepared using D-alle for L-Ile) and their respective N-formyl derivatives were assayed for uterotonic activity relative to related L-peptides. All retro-D-analogs (tested at concentrations ranging from 10-10 to 10-5 M) were devoid of angonistic (or antagonistic) activity in the isolated rat uterus, except for the retro-D-(D-alle-3, Gly-7) deaminooxytocinamine, which retains a terminal NH-2 group on the tail; the latter is a partial agonist with very low affinity. The results obtained with retro-D-analogs indicate that one or more of the elements of the peptide backbone of the tocinamide ring are essential for "occupation" and "activation" of uterine receptors. Oxytocin action may be the resultant of multiple hydrogen-bonding interactions between CO, NH, NH-2, and OH groups of the hormone with complementary groups on receptor, made possible by appropriate hydrophobic bonding. | lld:pubmed |
| pubmed-article:164658 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:164658 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:164658 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:164658 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:164658 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:164658 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:164658 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:164658 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:164658 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:164658 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:164658 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:164658 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:164658 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:164658 | pubmed:language | eng | lld:pubmed |
| pubmed-article:164658 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:164658 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:164658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:164658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:164658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:164658 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:164658 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:164658 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:164658 | pubmed:author | pubmed-author:KatoTT | lld:pubmed |
| pubmed-article:164658 | pubmed:author | pubmed-author:YanoNN | lld:pubmed |
| pubmed-article:164658 | pubmed:author | pubmed-author:HechterOO | lld:pubmed |
| pubmed-article:164658 | pubmed:author | pubmed-author:FlouretGG | lld:pubmed |
| pubmed-article:164658 | pubmed:author | pubmed-author:NakagawaS HSH | lld:pubmed |
| pubmed-article:164658 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:164658 | pubmed:volume | 72 | lld:pubmed |
| pubmed-article:164658 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:164658 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:164658 | pubmed:pagination | 563-6 | lld:pubmed |
| pubmed-article:164658 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:164658 | pubmed:meshHeading | pubmed-meshheading:164658-P... | lld:pubmed |
| pubmed-article:164658 | pubmed:meshHeading | pubmed-meshheading:164658-O... | lld:pubmed |
| pubmed-article:164658 | pubmed:meshHeading | pubmed-meshheading:164658-P... | lld:pubmed |
| pubmed-article:164658 | pubmed:meshHeading | pubmed-meshheading:164658-A... | lld:pubmed |
| pubmed-article:164658 | pubmed:meshHeading | pubmed-meshheading:164658-S... | lld:pubmed |
| pubmed-article:164658 | pubmed:meshHeading | pubmed-meshheading:164658-R... | lld:pubmed |
| pubmed-article:164658 | pubmed:year | 1975 | lld:pubmed |
| pubmed-article:164658 | pubmed:articleTitle | Contribution of the peptide backbone to the action of oxytocin analogs. | lld:pubmed |
| pubmed-article:164658 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:164658 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:164658 | lld:pubmed |
