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http://purl.uniprot.org/citations/11883939http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11883939http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11883939http://www.w3.org/2000/01/rdf-schema#comment"The apoptosis-linked protein ALG-2 is a Ca(2+)-binding protein that belongs to the penta-EF-hand protein family. ALG-2 forms a homodimer, a heterodimer with another penta-EF-hand protein, peflin, and a complex with its interacting protein, named AIP1 or Alix. By yeast two-hybrid screening using human ALG-2 as bait, we isolated a cDNA of a novel ALG-2-interacting protein, which turned out to be annexin XI. Deletion analysis revealed that ALG-2 interacted with the N-terminal domain of annexin XI (AnxN), which has an amino acid sequence similar to that of the C-terminal region of AIP1/Alix. Using recombinant biotin-tagged ALG-2 and the glutathione S-transferase (GST) fusion protein of AnxN, the direct interaction was analyzed by an ALG-2 overlay assay and by real-time interaction analysis with a surface plasmon resonance (SPR) biosensor. The dissociation constant (K(d)) was estimated to be approximately 70 nM. The Ca(2+)-dependent fluorescence change of ALG-2 in the presence of the hydrophobicity fluorescent probe 2-p-toluidinylnaphthalene-6-sulfonate (TNS) was inhibited by mixing with GST-AnxN, suggesting that the Pro/Gly/Tyr/Ala-rich hydrophobic region in AnxN masked the Ca(2+)-dependently exposed hydrophobic surface of ALG-2."xsd:string
http://purl.uniprot.org/citations/11883939http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.2002.6600"xsd:string
http://purl.uniprot.org/citations/11883939http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.2002.6600"xsd:string
http://purl.uniprot.org/citations/11883939http://purl.uniprot.org/core/author"Nakano Y."xsd:string
http://purl.uniprot.org/citations/11883939http://purl.uniprot.org/core/author"Nakano Y."xsd:string
http://purl.uniprot.org/citations/11883939http://purl.uniprot.org/core/author"Maki M."xsd:string
http://purl.uniprot.org/citations/11883939http://purl.uniprot.org/core/author"Maki M."xsd:string
http://purl.uniprot.org/citations/11883939http://purl.uniprot.org/core/author"Shibata H."xsd:string
http://purl.uniprot.org/citations/11883939http://purl.uniprot.org/core/author"Shibata H."xsd:string
http://purl.uniprot.org/citations/11883939http://purl.uniprot.org/core/author"Satoh H."xsd:string
http://purl.uniprot.org/citations/11883939http://purl.uniprot.org/core/author"Satoh H."xsd:string
http://purl.uniprot.org/citations/11883939http://purl.uniprot.org/core/author"Kitaura Y."xsd:string
http://purl.uniprot.org/citations/11883939http://purl.uniprot.org/core/author"Kitaura Y."xsd:string
http://purl.uniprot.org/citations/11883939http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11883939http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11883939http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/11883939http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/11883939http://purl.uniprot.org/core/pages"1166-1172"xsd:string
http://purl.uniprot.org/citations/11883939http://purl.uniprot.org/core/pages"1166-1172"xsd:string
http://purl.uniprot.org/citations/11883939http://purl.uniprot.org/core/title"ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent manner."xsd:string
http://purl.uniprot.org/citations/11883939http://purl.uniprot.org/core/title"ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent manner."xsd:string
http://purl.uniprot.org/citations/11883939http://purl.uniprot.org/core/volume"291"xsd:string
http://purl.uniprot.org/citations/11883939http://purl.uniprot.org/core/volume"291"xsd:string