dc.creatorTegge W.
dc.creatorBonafe C.F.S.
dc.creatorTeichmann A.
dc.creatorErck C.
dc.date2010
dc.date2015-06-26T12:38:17Z
dc.date2015-11-26T15:27:52Z
dc.date2015-06-26T12:38:17Z
dc.date2015-11-26T15:27:52Z
dc.date.accessioned2018-03-28T22:36:32Z
dc.date.available2018-03-28T22:36:32Z
dc.identifier
dc.identifierInternational Journal Of Peptides. , v. 2010, n. , p. - , 2010.
dc.identifier16879767
dc.identifier10.1155/2010/189396
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-84879192609&partnerID=40&md5=64cfeb2b0d40c3dbfe569cd0fbba15a8
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/91320
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/91320
dc.identifier2-s2.0-84879192609
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1261451
dc.descriptionSide-chain oligo- and polyglutamylation represents an important posttranslational modification in tubulin physiology. The particular number of glutamate units is related to specific regulatory functions. In this work, we present a method for the synthesis of building blocks for the Fmoc synthesis of peptides containing main chain glutamic acid residues that carry side-chain branching with oligo-glutamic acid. The two model peptide sequences CYEEVGVDSVEGEG-E(E x)-EEGEEY and CQDATADEQG-E(E x)-FEEEEGEDEA from the C-termini of mammalian α1- and β1-tubulin, respectively, containing oligo-glutamic acid side-chain branching with lengths of 1 to 5 amino acids were assembled in good yield and purity. The products may lead to the generation of specific antibodies which should be important tools for a more detailed investigation of polyglutamylation processes. © 2010 Werner Tegge et al.
dc.description2010
dc.description
dc.description
dc.description
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dc.languageen
dc.publisher
dc.relationInternational Journal of Peptides
dc.rightsaberto
dc.sourceScopus
dc.titleSynthesis Of Peptides From α- And β-tubulin Containing Glutamic Acid Side-chain Linked Oligo-glu With Defined Length
dc.typeArtículos de revistas


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