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http://purl.uniprot.org/citations/22750213http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22750213http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22750213http://www.w3.org/2000/01/rdf-schema#comment"Acetylcholinesterase (AChE) is organized into globular tetramers (G(4)) by a structural protein called proline-rich membrane anchor (PRiMA), anchoring it into the cell membrane of neurons in the brain. The assembly of AChE tetramers with PRiMA requires the presence of a C-terminal "t-peptide" in the AChE catalytic subunit (AChE(T)). The glycosylation of AChE(T) is known to be required for its proper assembly and trafficking; however, the role of PRiMA glycosylation in the oligomer assembly has not been revealed. PRiMA is a glycoprotein containing two putative N-linked glycosylation sites. By using site-directed mutagenesis, the asparagine-43 was identified to be the N-linked glycosylation site of PRiMA. Abolishing glycosylation on mouse PRiMA appeared not to affect its assembly with AChE(T), the enzymatic properties of AChE, and the membrane trafficking of PRiMA-linked AChE tetramers. This result is contrary to the reports that glycosylation is essential for conformation and trafficking of membrane glycoproteins."xsd:string
http://purl.uniprot.org/citations/22750213http://purl.org/dc/terms/identifier"doi:10.1016/j.neulet.2012.06.045"xsd:string
http://purl.uniprot.org/citations/22750213http://purl.org/dc/terms/identifier"doi:10.1016/j.neulet.2012.06.045"xsd:string
http://purl.uniprot.org/citations/22750213http://purl.uniprot.org/core/author"Chan W.K."xsd:string
http://purl.uniprot.org/citations/22750213http://purl.uniprot.org/core/author"Chan W.K."xsd:string
http://purl.uniprot.org/citations/22750213http://purl.uniprot.org/core/author"Tsim K.W."xsd:string
http://purl.uniprot.org/citations/22750213http://purl.uniprot.org/core/author"Tsim K.W."xsd:string
http://purl.uniprot.org/citations/22750213http://purl.uniprot.org/core/author"Choi R.C."xsd:string
http://purl.uniprot.org/citations/22750213http://purl.uniprot.org/core/author"Choi R.C."xsd:string
http://purl.uniprot.org/citations/22750213http://purl.uniprot.org/core/author"Chen V.P."xsd:string
http://purl.uniprot.org/citations/22750213http://purl.uniprot.org/core/author"Chen V.P."xsd:string
http://purl.uniprot.org/citations/22750213http://purl.uniprot.org/core/author"Luk W.K."xsd:string
http://purl.uniprot.org/citations/22750213http://purl.uniprot.org/core/author"Luk W.K."xsd:string
http://purl.uniprot.org/citations/22750213http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22750213http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22750213http://purl.uniprot.org/core/name"Neurosci. Lett."xsd:string
http://purl.uniprot.org/citations/22750213http://purl.uniprot.org/core/name"Neurosci. Lett."xsd:string
http://purl.uniprot.org/citations/22750213http://purl.uniprot.org/core/pages"71-75"xsd:string
http://purl.uniprot.org/citations/22750213http://purl.uniprot.org/core/pages"71-75"xsd:string
http://purl.uniprot.org/citations/22750213http://purl.uniprot.org/core/title"N-linked glycosylation of proline-rich membrane anchor (PRiMA) is not required for assembly and trafficking of globular tetrameric acetylcholinesterase."xsd:string
http://purl.uniprot.org/citations/22750213http://purl.uniprot.org/core/title"N-linked glycosylation of proline-rich membrane anchor (PRiMA) is not required for assembly and trafficking of globular tetrameric acetylcholinesterase."xsd:string
http://purl.uniprot.org/citations/22750213http://purl.uniprot.org/core/volume"523"xsd:string
http://purl.uniprot.org/citations/22750213http://purl.uniprot.org/core/volume"523"xsd:string