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http://purl.uniprot.org/citations/24915078http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24915078http://www.w3.org/2000/01/rdf-schema#comment"Cyclophilin D (CypD) is a key mitochondrial target for amyloid-β-induced mitochondrial and synaptic dysfunction and is considered a potential drug target for Alzheimer's disease. The high-resolution crystal structures of primitive orthorhombic (CypD-o) and primitive tetragonal (CypD-t) forms have been determined to 1.45 and 0.85 Å resolution, respectively, and are nearly identical structurally. Although an isomorphous structure of CypD-t has previously been reported, the structure reported here was determined at atomic resolution, while CypD-o represents a new crystal form for this protein. In addition, each crystal form contains a PEG 400 molecule bound to the same region along with a second PEG 400 site in CypD-t which occupies the cyclosporine A inhibitor binding site of CypD. Highly precise structural information for CypD should be extremely useful for discerning the detailed interaction of small molecules, particularly drugs and/or inhibitors, bound to CypD. The 0.85 Å resolution structure of CypD-t is the highest to date for any CypD structure."xsd:string
http://purl.uniprot.org/citations/24915078http://purl.org/dc/terms/identifier"doi:10.1107/s2053230x14009480"xsd:string
http://purl.uniprot.org/citations/24915078http://purl.uniprot.org/core/author"Wang C."xsd:string
http://purl.uniprot.org/citations/24915078http://purl.uniprot.org/core/author"Battaile K.P."xsd:string
http://purl.uniprot.org/citations/24915078http://purl.uniprot.org/core/author"Lovell S."xsd:string
http://purl.uniprot.org/citations/24915078http://purl.uniprot.org/core/author"Carlson E.A."xsd:string
http://purl.uniprot.org/citations/24915078http://purl.uniprot.org/core/author"Valasani K.R."xsd:string
http://purl.uniprot.org/citations/24915078http://purl.uniprot.org/core/author"Bisson A."xsd:string
http://purl.uniprot.org/citations/24915078http://purl.uniprot.org/core/author"ShiDu Yan S."xsd:string
http://purl.uniprot.org/citations/24915078http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24915078http://purl.uniprot.org/core/name"Acta Crystallogr F Struct Biol Commun"xsd:string
http://purl.uniprot.org/citations/24915078http://purl.uniprot.org/core/pages"717-722"xsd:string
http://purl.uniprot.org/citations/24915078http://purl.uniprot.org/core/title"High-resolution crystal structures of two crystal forms of human cyclophilin D in complex with PEG 400 molecules."xsd:string
http://purl.uniprot.org/citations/24915078http://purl.uniprot.org/core/volume"70"xsd:string
http://purl.uniprot.org/citations/24915078http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24915078
http://purl.uniprot.org/citations/24915078http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24915078
http://purl.uniprot.org/uniprot/#_P30405-mappedCitation-24915078http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24915078
http://purl.uniprot.org/uniprot/P30405http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/24915078