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http://purl.uniprot.org/SHA-384/7788E7A1976ECD6C82AAC1EDE4592B905289A1FB01F3EB87ACAEF15317A574E4AFBFAEAC808E3499F4D8C3CC5D377DA1http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/7788E7A1976ECD6C82AAC1EDE4592B905289A1FB01F3EB87ACAEF15317A574E4AFBFAEAC808E3499F4D8C3CC5D377DA1http://www.w3.org/2000/01/rdf-schema#comment"crystal structures of free TRIAP1 and TRIAP1-SLMO1 complex reveal how the PRELI domain is chaperoned during import into the intermembrane mitochondrial space; structural resemblance of PRELI-like domain of SLMO1 with that of mammalian phoshatidylinositol transfer proteins suggest they share similar lipid transfer mechanisms"xsd:string
http://purl.uniprot.org/uniprot/#_9C0F602AFAFC471B889CBB12AC923930CEACB7041D6ED87E058E5F69D3436C9D9E7ED48930FEFF8D270285B764185CF0http://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/7788E7A1976ECD6C82AAC1EDE4592B905289A1FB01F3EB87ACAEF15317A574E4AFBFAEAC808E3499F4D8C3CC5D377DA1
http://purl.uniprot.org/uniprot/Q7KZQ1http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/7788E7A1976ECD6C82AAC1EDE4592B905289A1FB01F3EB87ACAEF15317A574E4AFBFAEAC808E3499F4D8C3CC5D377DA1
http://purl.uniprot.org/uniprot/#_Q7KZQ1-mappedCitation-26071602http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/7788E7A1976ECD6C82AAC1EDE4592B905289A1FB01F3EB87ACAEF15317A574E4AFBFAEAC808E3499F4D8C3CC5D377DA1