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http://purl.uniprot.org/citations/23236605http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23236605http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23236605http://www.w3.org/2000/01/rdf-schema#comment"The mouse macrophage-derived apoptosis inhibitor of macrophage (AIM), which is incorporated into adipocytes and induces lipolysis by suppressing fatty acid synthase (FAS) activity, possesses three potential N-glycosylation sites. Inactivation of N-glycosylation sites revealed that mouse AIM contains two N-glycans in the first and second scavenger receptor cysteine-rich domains, and that depletion of N-glycans decreased AIM secretion from producing cells. Interestingly, the lack of N-glycans increased AIM lipolytic activity through enhancing AIM incorporation into adipocytes. Although human AIM contains no N-glycan, attachment of N-glycans increased AIM secretion. Thus, the N-glycosylation plays important roles in the secretion and lipolytic function of AIM."xsd:string
http://purl.uniprot.org/citations/23236605http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2012.08.017"xsd:string
http://purl.uniprot.org/citations/23236605http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2012.08.017"xsd:string
http://purl.uniprot.org/citations/23236605http://purl.uniprot.org/core/author"Arai S."xsd:string
http://purl.uniprot.org/citations/23236605http://purl.uniprot.org/core/author"Arai S."xsd:string
http://purl.uniprot.org/citations/23236605http://purl.uniprot.org/core/author"Mori M."xsd:string
http://purl.uniprot.org/citations/23236605http://purl.uniprot.org/core/author"Mori M."xsd:string
http://purl.uniprot.org/citations/23236605http://purl.uniprot.org/core/author"Miyazaki T."xsd:string
http://purl.uniprot.org/citations/23236605http://purl.uniprot.org/core/author"Miyazaki T."xsd:string
http://purl.uniprot.org/citations/23236605http://purl.uniprot.org/core/author"Kimura H."xsd:string
http://purl.uniprot.org/citations/23236605http://purl.uniprot.org/core/author"Kimura H."xsd:string
http://purl.uniprot.org/citations/23236605http://purl.uniprot.org/core/author"Iwamura Y."xsd:string
http://purl.uniprot.org/citations/23236605http://purl.uniprot.org/core/author"Iwamura Y."xsd:string
http://purl.uniprot.org/citations/23236605http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23236605http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23236605http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/23236605http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/23236605http://purl.uniprot.org/core/pages"3569-3574"xsd:string
http://purl.uniprot.org/citations/23236605http://purl.uniprot.org/core/pages"3569-3574"xsd:string
http://purl.uniprot.org/citations/23236605http://purl.uniprot.org/core/title"Modification of N-glycosylation modulates the secretion and lipolytic function of apoptosis inhibitor of macrophage (AIM)."xsd:string
http://purl.uniprot.org/citations/23236605http://purl.uniprot.org/core/title"Modification of N-glycosylation modulates the secretion and lipolytic function of apoptosis inhibitor of macrophage (AIM)."xsd:string
http://purl.uniprot.org/citations/23236605http://purl.uniprot.org/core/volume"586"xsd:string
http://purl.uniprot.org/citations/23236605http://purl.uniprot.org/core/volume"586"xsd:string