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http://purl.uniprot.org/citations/19665998http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19665998http://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/19665998http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2009.08.023"xsd:string
http://purl.uniprot.org/citations/19665998http://purl.uniprot.org/core/author"Mattjus P."xsd:string
http://purl.uniprot.org/citations/19665998http://purl.uniprot.org/core/author"Tuuf J."xsd:string
http://purl.uniprot.org/citations/19665998http://purl.uniprot.org/core/author"Wistbacka L."xsd:string
http://purl.uniprot.org/citations/19665998http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19665998http://purl.uniprot.org/core/name"Biochem Biophys Res Commun"xsd:string
http://purl.uniprot.org/citations/19665998http://purl.uniprot.org/core/pages"395-399"xsd:string
http://purl.uniprot.org/citations/19665998http://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/19665998http://purl.uniprot.org/core/volume"388"xsd:string
http://purl.uniprot.org/citations/19665998http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19665998
http://purl.uniprot.org/citations/19665998http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19665998
http://purl.uniprot.org/uniprot/#_A8KA83-mappedCitation-19665998http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19665998
http://purl.uniprot.org/uniprot/#_E7CEM8-mappedCitation-19665998http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19665998
http://purl.uniprot.org/uniprot/#_F5GZ49-mappedCitation-19665998http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19665998
http://purl.uniprot.org/uniprot/#_I3P687-mappedCitation-19665998http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19665998
http://purl.uniprot.org/uniprot/#_Q9NZD2-mappedCitation-19665998http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19665998
http://purl.uniprot.org/uniprot/#_Q9P0L0-mappedCitation-19665998http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19665998
http://purl.uniprot.org/uniprot/Q9P0L0http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/19665998
http://purl.uniprot.org/uniprot/I3P687http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/19665998
http://purl.uniprot.org/uniprot/Q9NZD2http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/19665998
http://purl.uniprot.org/uniprot/A8KA83http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/19665998
http://purl.uniprot.org/uniprot/E7CEM8http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/19665998
http://purl.uniprot.org/uniprot/F5GZ49http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/19665998