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http://purl.uniprot.org/citations/18622667http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18622667http://www.w3.org/2000/01/rdf-schema#comment"In plants the post-translational modification of proteins by polyamines catalysed by transglutaminases has been studied since 1987; it was identified by the production of glutamyl-polyamine derivatives, biochemical features, recognition by animal antibodies and modification of typical animal substrates. Transglutaminases are widespread in all plant organs and cell compartments studied until now, chloroplast being the most studied. Substrates are: photosynthetic complexes and Rubisco in chloroplasts, cytoskeleton and cell wall proteins. Roles either specific of plants or in common with animals are related to photosynthesis, fertilisation, stresses, senescence and programmed cell death, showing that the catalytic function is conserved across the kingdoms. AtPng1p, the first plant transglutaminase sequenced shows undetectable sequence homology to the animal enzymes, except for the catalytic triad. It is, however, endowed with a calcium-dependent activity that allowed us to build a three-dimensional model adopting as a template the animal transglutaminase 2."xsd:string
http://purl.uniprot.org/citations/18622667http://purl.org/dc/terms/identifier"doi:10.1007/s00726-008-0131-9"xsd:string
http://purl.uniprot.org/citations/18622667http://purl.uniprot.org/core/author"Casadio R."xsd:string
http://purl.uniprot.org/citations/18622667http://purl.uniprot.org/core/author"Del Duca S."xsd:string
http://purl.uniprot.org/citations/18622667http://purl.uniprot.org/core/author"Tasco G."xsd:string
http://purl.uniprot.org/citations/18622667http://purl.uniprot.org/core/author"Serafini-Fracassini D."xsd:string
http://purl.uniprot.org/citations/18622667http://purl.uniprot.org/core/author"Della Mea M."xsd:string
http://purl.uniprot.org/citations/18622667http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/18622667http://purl.uniprot.org/core/name"Amino Acids"xsd:string
http://purl.uniprot.org/citations/18622667http://purl.uniprot.org/core/pages"643-657"xsd:string
http://purl.uniprot.org/citations/18622667http://purl.uniprot.org/core/title"Plant and animal transglutaminases: do similar functions imply similar structures?"xsd:string
http://purl.uniprot.org/citations/18622667http://purl.uniprot.org/core/volume"36"xsd:string
http://purl.uniprot.org/citations/18622667http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18622667
http://purl.uniprot.org/citations/18622667http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18622667
http://purl.uniprot.org/uniprot/#_A5PHD1-mappedCitation-18622667http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18622667
http://purl.uniprot.org/uniprot/#_Q9FGY9-mappedCitation-18622667http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18622667
http://purl.uniprot.org/uniprot/A5PHD1http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18622667
http://purl.uniprot.org/uniprot/Q9FGY9http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18622667