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http://purl.uniprot.org/citations/19665998 | http://www.w3.org/2000/01/rdf-schema#comment | "The glycolipid transfer protein (GLTP) is a cytoplasmic protein with an ability to bind glycolipids and catalyze their in vitro transfer. In this study, we have found a FFAT-like motif in GLTP. The FFAT (two phenylalanines in an acidic tract) motif in lipid-binding proteins has previously been shown to interact with the VAPs (vesicle-associated membrane protein-associated proteins) in the endoplasmic reticulum. Here we used glutathione S-transferase pull-down experiments to confirm that GLTP and VAP-A interact. By displacing different amino acids in the motif we clearly show that the interaction is dependent on the FFAT-like motif in GLTP. The potential role of GLTP in the endoplasmic reticulum association is discussed."xsd:string |
http://purl.uniprot.org/citations/19665998 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2009.08.023"xsd:string |
http://purl.uniprot.org/citations/19665998 | http://purl.uniprot.org/core/author | "Mattjus P."xsd:string |
http://purl.uniprot.org/citations/19665998 | http://purl.uniprot.org/core/author | "Tuuf J."xsd:string |
http://purl.uniprot.org/citations/19665998 | http://purl.uniprot.org/core/author | "Wistbacka L."xsd:string |
http://purl.uniprot.org/citations/19665998 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
http://purl.uniprot.org/citations/19665998 | http://purl.uniprot.org/core/name | "Biochem Biophys Res Commun"xsd:string |
http://purl.uniprot.org/citations/19665998 | http://purl.uniprot.org/core/pages | "395-399"xsd:string |
http://purl.uniprot.org/citations/19665998 | http://purl.uniprot.org/core/title | "The glycolipid transfer protein interacts with the vesicle-associated membrane protein-associated protein VAP-A."xsd:string |
http://purl.uniprot.org/citations/19665998 | http://purl.uniprot.org/core/volume | "388"xsd:string |
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