rdf:type |
|
lifeskim:mentions |
umls-concept:C0002520,
umls-concept:C0026377,
umls-concept:C0030956,
umls-concept:C0185125,
umls-concept:C0443288,
umls-concept:C0597357,
umls-concept:C0936012,
umls-concept:C1167622,
umls-concept:C1257890,
umls-concept:C1435361,
umls-concept:C1708111,
umls-concept:C1709743
|
pubmed:issue |
2
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pubmed:dateCreated |
2004-1-8
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pubmed:abstractText |
Compounds (2S,4S)- and (2S,4R)-4-(2'-guanidinoethyl)proline have been synthesized as a conformationally restricted arginine. Their backbones fit the i + 1 position in a turn, and the side chains are restricted compared to that of arginine. These analogues were incorporated into mini atrial natriuretic polypeptide, which has an important turnlike conformation at Gly(6)-Arg(7)()-Met(8)-Asp(9). Structural analysis revealed that the size of the conformational space of Arg(7) on binding to the receptor was approximately one-third of the entire conformational space.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Atrial Natriuretic Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Guanidines,
http://linkedlifedata.com/resource/pubmed/chemical/Guanylate Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides, Cyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Proline,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Atrial Natriuretic Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Solutions,
http://linkedlifedata.com/resource/pubmed/chemical/atrial natriuretic factor receptor A
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0022-2623
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
15
|
pubmed:volume |
47
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
489-92
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:14711318-Animals,
pubmed-meshheading:14711318-Arginine,
pubmed-meshheading:14711318-Atrial Natriuretic Factor,
pubmed-meshheading:14711318-CHO Cells,
pubmed-meshheading:14711318-Cricetinae,
pubmed-meshheading:14711318-Cyclic AMP,
pubmed-meshheading:14711318-Guanidines,
pubmed-meshheading:14711318-Guanylate Cyclase,
pubmed-meshheading:14711318-Magnetic Resonance Spectroscopy,
pubmed-meshheading:14711318-Models, Molecular,
pubmed-meshheading:14711318-Peptide Fragments,
pubmed-meshheading:14711318-Peptides, Cyclic,
pubmed-meshheading:14711318-Proline,
pubmed-meshheading:14711318-Protein Structure, Secondary,
pubmed-meshheading:14711318-Receptors, Atrial Natriuretic Factor,
pubmed-meshheading:14711318-Solutions,
pubmed-meshheading:14711318-Structure-Activity Relationship
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pubmed:year |
2004
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pubmed:articleTitle |
Restriction of a peptide turn conformation and conformational analysis of guanidino group using arginine-proline fused amino acids: application to mini atrial natriuretic peptide on binding to the receptor.
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pubmed:affiliation |
Suntory Institute for Bioorganic Research and Daiichi Suntory Biomedical Research Co., Ltd, Shimamoto, Mishima 618-8503, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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