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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
15
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pubmed:dateCreated |
2005-4-11
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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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Leydig insulin-like protein,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RXFP2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, G-Protein-Coupled
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
280
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14586-90
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:15708846-Amino Acid Sequence,
pubmed-meshheading:15708846-Binding, Competitive,
pubmed-meshheading:15708846-Cell Line,
pubmed-meshheading:15708846-Chromatography, High Pressure Liquid,
pubmed-meshheading:15708846-Circular Dichroism,
pubmed-meshheading:15708846-Cyclic AMP,
pubmed-meshheading:15708846-Cysteine,
pubmed-meshheading:15708846-DNA, Complementary,
pubmed-meshheading:15708846-Dose-Response Relationship, Drug,
pubmed-meshheading:15708846-Humans,
pubmed-meshheading:15708846-Insulin,
pubmed-meshheading:15708846-Molecular Sequence Data,
pubmed-meshheading:15708846-Peptides,
pubmed-meshheading:15708846-Protein Binding,
pubmed-meshheading:15708846-Protein Structure, Tertiary,
pubmed-meshheading:15708846-Proteins,
pubmed-meshheading:15708846-Receptors, G-Protein-Coupled,
pubmed-meshheading:15708846-Signal Transduction,
pubmed-meshheading:15708846-Spectrometry, Mass, Matrix-Assisted Laser...
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pubmed:year |
2005
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pubmed:articleTitle |
LGR8 signal activation by the relaxin-like factor.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston South Carolina 29425, USA. bullesee@musc.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, N.I.H., Extramural
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