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http://purl.uniprot.org/citations/24412565http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24412565http://www.w3.org/2000/01/rdf-schema#comment"Muscle fructose-1,6-bisphosphatase (FBP2), a regulatory enzyme of glyconeogenesis, binds to mitochondria where it interacts with proteins involved in regulation of energy homeostasis. Here, we show that the quaternary structure of FBP2 plays a crucial role in this interaction, and that the AMP-driven transition of the FBP2 subunit arrangement from active to inactive precludes its association with the mitochondria. Moreover, we demonstrate that truncation of the evolutionarily conserved N-terminal residues of FBP2 results in a loss of its mitochondria-protective functions. This strengthens the recently raised hypothesis that FBP2 evolved as a regulator not only for glycogen storage but also for mitochondrial function in contracting muscle."xsd:string
http://purl.uniprot.org/citations/24412565http://purl.org/dc/terms/identifier"doi:10.1016/j.biocel.2013.12.015"xsd:string
http://purl.uniprot.org/citations/24412565http://purl.uniprot.org/core/author"Gizak A."xsd:string
http://purl.uniprot.org/citations/24412565http://purl.uniprot.org/core/author"Rakus D."xsd:string
http://purl.uniprot.org/citations/24412565http://purl.uniprot.org/core/author"Pirog M."xsd:string
http://purl.uniprot.org/citations/24412565http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24412565http://purl.uniprot.org/core/name"Int J Biochem Cell Biol"xsd:string
http://purl.uniprot.org/citations/24412565http://purl.uniprot.org/core/pages"55-59"xsd:string
http://purl.uniprot.org/citations/24412565http://purl.uniprot.org/core/title"Changes in quaternary structure of muscle fructose-1,6-bisphosphatase regulate affinity of the enzyme to mitochondria."xsd:string
http://purl.uniprot.org/citations/24412565http://purl.uniprot.org/core/volume"48"xsd:string
http://purl.uniprot.org/citations/24412565http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24412565
http://purl.uniprot.org/citations/24412565http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24412565
http://purl.uniprot.org/uniprot/#_O00757-mappedCitation-24412565http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24412565
http://purl.uniprot.org/uniprot/#_Q9UJ73-mappedCitation-24412565http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24412565
http://purl.uniprot.org/uniprot/#_Q9UMQ9-mappedCitation-24412565http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24412565
http://purl.uniprot.org/uniprot/#_Q9UMR0-mappedCitation-24412565http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24412565
http://purl.uniprot.org/uniprot/O00757http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/24412565
http://purl.uniprot.org/uniprot/Q9UMQ9http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/24412565
http://purl.uniprot.org/uniprot/Q9UMR0http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/24412565
http://purl.uniprot.org/uniprot/Q9UJ73http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/24412565