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http://purl.uniprot.org/citations/15787614http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15787614http://www.w3.org/2000/01/rdf-schema#comment"The concept that plants exploit polypeptides as post-translational modifiers is rapidly emerging as an important method to manipulate various cellular processes. The best known is Ub (ubiquitin) that serves as reusable tag for selective protein degradation by the 26 S proteasome and for endosomal trafficking. Genomic analyses indicate that Ub pathway alone comprises over 6% of the Arabidopsis proteome with thousands of proteins being targets. Consequently, this pathway influences much of plant biology. Others tags include RUB-1 (related to Ub-1; also known as NEDD8), SUMO (small Ub-like modifier), ATG-8 (autophagy-8) and ATG-12, UFM-1 (Ub-fold modifier-1) and HUB-1 (homology to Ub-1). Preliminary studies indicate that these tags have much more limited sets of targets and provide more specialized functions, including transcriptional regulation, protein localization, autophagic turnover and antagonizing the effects of Ub. On the basis of their widespread distribution and pervasive functions, peptide tags can now be considered as prime players in plant cell regulation."xsd:string
http://purl.uniprot.org/citations/15787614http://purl.org/dc/terms/identifier"doi:10.1042/bst0330393"xsd:string
http://purl.uniprot.org/citations/15787614http://purl.uniprot.org/core/author"Vierstra R.D."xsd:string
http://purl.uniprot.org/citations/15787614http://purl.uniprot.org/core/author"Downes B."xsd:string
http://purl.uniprot.org/citations/15787614http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15787614http://purl.uniprot.org/core/name"Biochem Soc Trans"xsd:string
http://purl.uniprot.org/citations/15787614http://purl.uniprot.org/core/pages"393-399"xsd:string
http://purl.uniprot.org/citations/15787614http://purl.uniprot.org/core/title"Post-translational regulation in plants employing a diverse set of polypeptide tags."xsd:string
http://purl.uniprot.org/citations/15787614http://purl.uniprot.org/core/volume"33"xsd:string
http://purl.uniprot.org/citations/15787614http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15787614
http://purl.uniprot.org/citations/15787614http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15787614
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