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pubmed-article:20043911pubmed:abstractTextThe glucagon receptor antagonist BI-32169, recently isolated from Streptomyces sp., was described as a bicyclic peptide, although its primary structure comprises conserved elements of class I and class II lasso peptides. Tandem mass spectrometric and nuclear magnetic resonance spectroscopic studies revealed that BI-32169 is a lasso-structured peptide constituting the new class III of lasso peptides. The determined lasso fold opens new avenues to improve the promising biological activity of BI-32169.lld:pubmed
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pubmed-article:20043911pubmed:authorpubmed-author:MarahielMoham...lld:pubmed
pubmed-article:20043911pubmed:authorpubmed-author:LinneUweUlld:pubmed
pubmed-article:20043911pubmed:authorpubmed-author:XieXiulanXlld:pubmed
pubmed-article:20043911pubmed:authorpubmed-author:KnappeThomas...lld:pubmed
pubmed-article:20043911pubmed:copyrightInfoCopyright 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.lld:pubmed
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pubmed-article:20043911pubmed:articleTitleThe glucagon receptor antagonist BI-32169 constitutes a new class of lasso peptides.lld:pubmed
pubmed-article:20043911pubmed:affiliationDepartment of Chemistry/Biochemistry, Philipps-University Marburg, Marburg, Germany.lld:pubmed
pubmed-article:20043911pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:20043911pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed