Publicação:
N-glycosylation in sugarcane

dc.contributor.authorMaia, Ivan de Godoy [UNESP]
dc.contributor.authorLeite, Adilson [UNESP]
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-27T11:20:21Z
dc.date.available2014-05-27T11:20:21Z
dc.date.issued2001-12-01
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.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.format.extent231-234
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.doi10.1590/S1415-47572001000100030
dc.identifier.file2-s2.0-0035739416.pdf
dc.identifier.issn1415-4757
dc.identifier.lattes8649222099176162
dc.identifier.scieloS1415-47572001000100030
dc.identifier.scopus2-s2.0-0035739416
dc.identifier.urihttp://hdl.handle.net/11449/66691
dc.language.isoeng
dc.relation.ispartofGenetics and Molecular Biology
dc.relation.ispartofjcr1.493
dc.relation.ispartofsjr0,638
dc.rights.accessRightsAcesso aberto
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.typeArtigo
dcterms.licensehttp://www.scielo.br/revistas/gmb/iaboutj.htm
dspace.entity.typePublication
unesp.author.lattes8649222099176162
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências, Botucatupt
unesp.departmentGenética - IBBpt

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