pubmed-article:15708846 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15708846 | lifeskim:mentions | umls-concept:C0249860 | lld:lifeskim |
pubmed-article:15708846 | lifeskim:mentions | umls-concept:C1416453 | lld:lifeskim |
pubmed-article:15708846 | lifeskim:mentions | umls-concept:C1424898 | lld:lifeskim |
pubmed-article:15708846 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
pubmed-article:15708846 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:15708846 | pubmed:issue | 15 | lld:pubmed |
pubmed-article:15708846 | pubmed:dateCreated | 2005-4-11 | lld:pubmed |
pubmed-article:15708846 | pubmed:abstractText | The relaxin-like factor (RLF) is thought to be responsible for the intra-abdominal migration of the testis during mammalian development. Our latest studies of RLF and LGR8 have revealed that the N-terminal region of the A chain is not required for receptor binding but is indispensable for cyclic AMP generation. RLF derivatives with six residues deleted from the N terminus of the A chain are active, whereas further truncation, up to the first A chain cysteine (A-10), yields tightly binding ligands devoid of signaling activity. These derivatives are specific competitive inhibitors (RLFi) of RLF. Although receptor binding is dependent upon B chain residues, the N-terminal region of the A chain is a generic trigger of the trans-membrane signaling activity. | lld:pubmed |
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pubmed-article:15708846 | pubmed:language | eng | lld:pubmed |
pubmed-article:15708846 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15708846 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:15708846 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15708846 | pubmed:month | Apr | lld:pubmed |
pubmed-article:15708846 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:15708846 | pubmed:author | pubmed-author:BüllesbachEri... | lld:pubmed |
pubmed-article:15708846 | pubmed:author | pubmed-author:SchwabeChrist... | lld:pubmed |
pubmed-article:15708846 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15708846 | pubmed:day | 15 | lld:pubmed |
pubmed-article:15708846 | pubmed:volume | 280 | lld:pubmed |
pubmed-article:15708846 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15708846 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15708846 | pubmed:pagination | 14586-90 | lld:pubmed |
pubmed-article:15708846 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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pubmed-article:15708846 | pubmed:year | 2005 | lld:pubmed |
pubmed-article:15708846 | pubmed:articleTitle | LGR8 signal activation by the relaxin-like factor. | lld:pubmed |
pubmed-article:15708846 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston South Carolina 29425, USA. bullesee@musc.edu | lld:pubmed |
pubmed-article:15708846 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15708846 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:15708846 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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