Venom-Sweet-Venom: N-Linked Glycosylation in Snake Venom Toxins

dc.creatorSOARES, Sandro G.
dc.creatorOLIVEIRA, Leandro L.
dc.date.accessioned2012-10-19T23:34:13Z
dc.date.accessioned2018-07-04T15:19:39Z
dc.date.available2012-10-19T23:34:13Z
dc.date.available2018-07-04T15:19:39Z
dc.date.created2012-10-19T23:34:13Z
dc.date.issued2009
dc.identifierPROTEIN AND PEPTIDE LETTERS, v.16, n.8, p.913-919, 2009
dc.identifier0929-8665
dc.identifierhttp://producao.usp.br/handle/BDPI/24908
dc.identifierhttp://apps.isiknowledge.com/InboundService.do?Func=Frame&product=WOS&action=retrieve&SrcApp=EndNote&UT=000268890600009&Init=Yes&SrcAuth=ResearchSoft&mode=FullRecord
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1621634
dc.description.abstractProtein glycosylation represents one of the most important post-translational events, and is a mean of diversifying a protein without recourse to the genome. The venoms produced by snakes contain an abundance of glycoproteins with N-linked carbohydrates. N-linked glycosylation can ensure the correct folding of important functional domains. Characterization of carbohydrates structures aids in development of human therapeutics by snake venom toxins.
dc.languageeng
dc.publisherBENTHAM SCIENCE PUBL LTD
dc.relationProtein and Peptide Letters
dc.rightsCopyright BENTHAM SCIENCE PUBL LTD
dc.rightsclosedAccess
dc.subjectN-linked oligosaccharides
dc.subjectsnake venom
dc.subjectenzyme activity
dc.subjectserine protease
dc.titleVenom-Sweet-Venom: N-Linked Glycosylation in Snake Venom Toxins
dc.typeArtículos de revistas


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