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000723988 019__ $$a908089680
000723988 020__ $$a9781493910106$$qelectronic book
000723988 020__ $$a1493910108$$qelectronic book
000723988 020__ $$a1493910094
000723988 020__ $$a9781493910090
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000723988 0247_ $$a10.1007/978-1-4939-1010-6$$2doi
000723988 035__ $$aSP(OCoLC)ocn894508835
000723988 035__ $$aSP(OCoLC)894508835$$z(OCoLC)908089680
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000723988 049__ $$aISEA
000723988 050_4 $$aQP552.P4
000723988 08204 $$a572/.65$$223
000723988 1001_ $$aLi, Yanyan,$$eauthor.
000723988 24510 $$aLasso peptides$$h[electronic resource] :$$bbacterial strategies to make and maintain bioactive entangled scaffolds /$$cYanyan Li, Séverine Zirah, Sylvie Rebuffat.
000723988 264_1 $$aNew York, NY :$$bSpringer,$$c2015.
000723988 300__ $$a1 online resource (xiii, 103 pages) :$$billustrations (some color).
000723988 336__ $$atext$$btxt$$2rdacontent
000723988 337__ $$acomputer$$bc$$2rdamedia
000723988 338__ $$aonline resource$$bcr$$2rdacarrier
000723988 4901_ $$aSpringerBriefs in Microbiology,$$x2191-5385
000723988 504__ $$aIncludes bibliographical references.
000723988 5050_ $$aOverview on Lasso Peptide Research -- From the Producer Microorganisms to the Lasso Scaffold -- Biological Activities of Lasso Peptides and Structure-Activity Relationships -- Biosynthesis, Regulation and Export of Lasso Peptides -- Lasso Peptide Bioengineering and Bioprospecting.
000723988 506__ $$aAccess limited to authorized users.
000723988 520__ $$aLasso peptides form a growing family of fascinating ribosomally-synthesized and post-translationally modified peptides produced by bacteria. They contain 15 to 24 residues and share a unique interlocked topology that involves an N-terminal 7 to 9-residue macrolactam ring where the C-terminal tail is threaded and irreversibly trapped. The ring results from the condensation of the N-terminal amino group with a side-chain carboxylate of a glutamate at position 8 or 9, or an aspartate at position 7, 8 or 9. The trapping of the tail involves bulky amino acids located in the tail below and above the ring and/or disulfide bridges connecting the ring and the tail. Lasso peptides are subdivided into three subtypes depending on the absence (class II) or presence of one (class III) or two (class I) disulfide bridges. The lasso topology results in highly compact structures that give to lasso peptides an extraordinary stability towards both protease degradation and denaturing conditions. Lasso peptides are generally receptor antagonists, enzyme inhibitors and/or antibacterial or antiviral (anti-HIV) agents. The lasso scaffold and the associated biological activities shown by lasso peptides on different key targets make them promising molecules with high therapeutic potential. Their application in drug design has been exemplified by the development of an integrin antagonist based on a lasso peptide scaffold. The biosynthesis machinery of lasso peptides is therefore of high biotechnological interest, especially since such highly compact and stable structures have to date revealed inaccessible by peptide synthesis. Lasso peptides are produced from a linear precursor LasA, which undergoes a maturation process involving several steps, in particular cleavage of the leader peptide and cyclization. The post-translational modifications are ensured by a dedicated enzymatic machinery, which is composed of an ATP-dependent cysteine protease (LasB) and a lactam synthetase (LasC) that form an enzymatic complex called lasso synthetase. Microcin J25, produced by Escherichia coli AY25, is the archetype of lasso peptides and the most extensively studied. To date only around forty lasso peptides have been isolated, but genome mining approaches have revealed that they are widely distributed among Proteobacteria and Actinobacteria, particularly in Streptomyces, making available a rich resource of novel lasso peptides and enzyme machineries towards lasso topologies.
000723988 588__ $$aOnline resource; title from PDF title page (SpringerLink, viewed November 10, 2014).
000723988 650_0 $$aPeptides.
000723988 7001_ $$aZirah, Séverine,$$eauthor.
000723988 7001_ $$aRebuffat, Sylvie,$$eauthor.
000723988 77608 $$iPrint version:$$z9781493910090
000723988 830_0 $$aSpringerBriefs in microbiology.
000723988 852__ $$bebk
000723988 85640 $$3SpringerLink$$uhttps://univsouthin.idm.oclc.org/login?url=http://link.springer.com/10.1007/978-1-4939-1010-6$$zOnline Access$$91397441.1
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000723988 980__ $$aBIB
000723988 982__ $$aEbook
000723988 983__ $$aOnline
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