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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/66691
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dc.contributor.authorMaia, Ivan de Godoy-
dc.contributor.authorLeite, Adilson-
dc.date.accessioned2014-05-27T11:20:21Z-
dc.date.accessioned2016-10-25T18:17:22Z-
dc.date.available2014-05-27T11:20:21Z-
dc.date.available2016-10-25T18:17:22Z-
dc.date.issued2001-12-01-
dc.identifierhttp://dx.doi.org/10.1590/S1415-47572001000100030-
dc.identifier.citationGenetics and Molecular Biology, v. 24, n. 1-4, p. 231-234, 2001.-
dc.identifier.issn1415-4757-
dc.identifier.urihttp://hdl.handle.net/11449/66691-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/66691-
dc.description.abstractThe N-linked glycosylation of secretory and membrane proteins is the most complex posttranslational modification known to occur in eukaryotic cells. It has been shown to play critical roles in modulating protein function. Although this important biological process has been extensively studied in mammals, much less is known about this biosynthetic pathway in plants. The enzymes involved in plant N-glycan biosynthesis and processing are still not well defined and the mechanism of their genetic regulation is almost completely unknown. In this paper we describe our first attempt to understand the N-linked glycosylation mechanism in a plant species by using the data generated by the Sugarcane Expressed Sequence Tag (SUCEST) project. The SUCEST database was mined for sugarcane gene products potentially involved in the N-glycosylation pathway. This approach has led to the identification and functional assignment of 90 expressed sequence tag (EST) clusters sharing significant sequence similarity with the enzymes involved in N-glycan biosynthesis and processing. The ESTs identified were also analyzed to establish their relative abundance.en
dc.format.extent231-234-
dc.language.isoeng-
dc.sourceScopus-
dc.subjectgene product-
dc.subjectglycan-
dc.subjectmembrane protein-
dc.subjectsecretory protein-
dc.subjectbiosynthesis-
dc.subjectcontrolled study-
dc.subjectdata base-
dc.subjectdevice-
dc.subjecteukaryotic cell-
dc.subjectexpressed sequence tag-
dc.subjectgenetic regulation-
dc.subjectglycosylation-
dc.subjectmammal-
dc.subjectnonhuman-
dc.subjectplant-
dc.subjectprotein function-
dc.subjectprotein processing-
dc.subjectsequence database-
dc.subjectsequence homology-
dc.subjectsugarcane-
dc.subjectEukaryota-
dc.subjectMammalia-
dc.subjectSaccharum hybrid cultivar-
dc.titleN-glycosylation in sugarcaneen
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.description.affiliationCentro de Biologia Molecular E Engenharia Genética Universidade Estadual de Campinas, C.P. 6010, 13083-970 Campinas, SP-
dc.description.affiliationInstituto de Biociências Departamento de Genética UNESP - Campus de Botucatu, 18618-000 Botucatu, SP-
dc.description.affiliationUnespInstituto de Biociências Departamento de Genética UNESP - Campus de Botucatu, 18618-000 Botucatu, SP-
dc.identifier.doi10.1590/S1415-47572001000100030-
dc.identifier.scieloS1415-47572001000100030-
dc.rights.accessRightsAcesso aberto-
dc.identifier.file2-s2.0-0035739416.pdf-
dc.relation.ispartofGenetics and Molecular Biology-
dc.identifier.scopus2-s2.0-0035739416-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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