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http://purl.uniprot.org/citations/1982555http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1982555http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1982555http://www.w3.org/2000/01/rdf-schema#comment"The expression site for the variant surface glycoprotein (VSG) gene of Trypanosoma brucei contains several genes of unknown function (ESAGs, for expression site-associated genes). Among these, ESAG 4 shows homology to eukaryotic adenylate/guanylate cyclase genes, in the region encoding the presumptive enzyme catalytic domain. This gene belongs to a family of related sequences, and hybridizes to the genomic DNA of other trypanosomatids, such as Trypanosoma congolense, Trypanosoma vivax and Trypanosoma mega. While ESAG 4 is transcribed only in bloodstream forms by a RNA polymerase resistant to alpha-amanitin, at least three other members of this family are transcribed in both bloodstream and procyclic forms, by a RNA polymerase sensitive to the drug. These genes encode different putative transmembrane proteins showing high sequence conservation in the region corresponding to the adenylate/guanylate cyclase catalytic domain."xsd:string
http://purl.uniprot.org/citations/1982555http://purl.org/dc/terms/identifier"doi:10.1016/0166-6851(90)90152-c"xsd:string
http://purl.uniprot.org/citations/1982555http://purl.org/dc/terms/identifier"doi:10.1016/0166-6851(90)90152-c"xsd:string
http://purl.uniprot.org/citations/1982555http://purl.uniprot.org/core/author"Steinert M."xsd:string
http://purl.uniprot.org/citations/1982555http://purl.uniprot.org/core/author"Steinert M."xsd:string
http://purl.uniprot.org/citations/1982555http://purl.uniprot.org/core/author"Alexandre S."xsd:string
http://purl.uniprot.org/citations/1982555http://purl.uniprot.org/core/author"Alexandre S."xsd:string
http://purl.uniprot.org/citations/1982555http://purl.uniprot.org/core/author"Halleux S."xsd:string
http://purl.uniprot.org/citations/1982555http://purl.uniprot.org/core/author"Halleux S."xsd:string
http://purl.uniprot.org/citations/1982555http://purl.uniprot.org/core/author"Paindavione P."xsd:string
http://purl.uniprot.org/citations/1982555http://purl.uniprot.org/core/author"Paindavione P."xsd:string
http://purl.uniprot.org/citations/1982555http://purl.uniprot.org/core/author"Pays A."xsd:string
http://purl.uniprot.org/citations/1982555http://purl.uniprot.org/core/author"Pays A."xsd:string
http://purl.uniprot.org/citations/1982555http://purl.uniprot.org/core/author"Pays E."xsd:string
http://purl.uniprot.org/citations/1982555http://purl.uniprot.org/core/author"Pays E."xsd:string
http://purl.uniprot.org/citations/1982555http://purl.uniprot.org/core/author"Tebabi P."xsd:string
http://purl.uniprot.org/citations/1982555http://purl.uniprot.org/core/author"Tebabi P."xsd:string
http://purl.uniprot.org/citations/1982555http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/1982555http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/1982555http://purl.uniprot.org/core/name"Mol. Biochem. Parasitol."xsd:string
http://purl.uniprot.org/citations/1982555http://purl.uniprot.org/core/name"Mol. Biochem. Parasitol."xsd:string
http://purl.uniprot.org/citations/1982555http://purl.uniprot.org/core/pages"279-288"xsd:string
http://purl.uniprot.org/citations/1982555http://purl.uniprot.org/core/pages"279-288"xsd:string