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http://purl.uniprot.org/citations/11101510http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11101510http://www.w3.org/2000/01/rdf-schema#comment"Efficient cellular energy homeostasis is a critical determinant of muscle performance, providing evolutionary advantages responsible for species survival. Phosphotransfer reactions, which couple ATP production and utilization, are thought to play a central role in this process. Here, we provide evidence that genetic disruption of AK1-catalyzed ss-phosphoryl transfer in mice decreases the potential of myofibers to sustain nucleotide ratios despite up-regulation of high-energy phosphoryl flux through glycolytic, guanylate and creatine kinase phosphotransfer pathways. A maintained contractile performance of AK1-deficient muscles was associated with higher ATP turnover rate and larger amounts of ATP consumed per contraction. Metabolic stress further aggravated the energetic cost in AK1(-/-) muscles. Thus, AK1-catalyzed phosphotransfer is essential in the maintenance of cellular energetic economy, enabling skeletal muscle to perform at the lowest metabolic cost."xsd:string
http://purl.uniprot.org/citations/11101510http://purl.org/dc/terms/identifier"doi:10.1093/emboj/19.23.6371"xsd:string
http://purl.uniprot.org/citations/11101510http://purl.uniprot.org/core/author"de Haan A."xsd:string
http://purl.uniprot.org/citations/11101510http://purl.uniprot.org/core/author"Terzic A."xsd:string
http://purl.uniprot.org/citations/11101510http://purl.uniprot.org/core/author"Wieringa B."xsd:string
http://purl.uniprot.org/citations/11101510http://purl.uniprot.org/core/author"Janssen E."xsd:string
http://purl.uniprot.org/citations/11101510http://purl.uniprot.org/core/author"Dzeja P.P."xsd:string
http://purl.uniprot.org/citations/11101510http://purl.uniprot.org/core/author"Oerlemans F."xsd:string
http://purl.uniprot.org/citations/11101510http://purl.uniprot.org/core/author"Heerschap A."xsd:string
http://purl.uniprot.org/citations/11101510http://purl.uniprot.org/core/author"Rush P.S."xsd:string
http://purl.uniprot.org/citations/11101510http://purl.uniprot.org/core/author"Simonetti A.W."xsd:string
http://purl.uniprot.org/citations/11101510http://purl.uniprot.org/core/author"Terjung R.R."xsd:string
http://purl.uniprot.org/citations/11101510http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11101510http://purl.uniprot.org/core/name"EMBO J"xsd:string
http://purl.uniprot.org/citations/11101510http://purl.uniprot.org/core/pages"6371-6381"xsd:string
http://purl.uniprot.org/citations/11101510http://purl.uniprot.org/core/title"Adenylate kinase 1 gene deletion disrupts muscle energetic economy despite metabolic rearrangement."xsd:string
http://purl.uniprot.org/citations/11101510http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/11101510http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11101510
http://purl.uniprot.org/citations/11101510http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11101510
http://purl.uniprot.org/uniprot/#_A0A0A6YXW8-mappedCitation-11101510http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11101510
http://purl.uniprot.org/uniprot/#_Q9R0Y5-mappedCitation-11101510http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11101510
http://purl.uniprot.org/uniprot/#_Z4YN97-mappedCitation-11101510http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11101510
http://purl.uniprot.org/uniprot/Q9R0Y5http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11101510
http://purl.uniprot.org/uniprot/Z4YN97http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11101510