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http://purl.uniprot.org/citations/34105236http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/34105236http://www.w3.org/2000/01/rdf-schema#comment"Glucokinase, which phosphorylates glucose to form glucose-6-phosphate, plays a critical role in regulating blood glucose levels. On the basis of data of glucokinase-knockout and transgenic mice and humans with glucokinase mutations, glucokinase was targeted for drug development aiming to augment its activity, and thereby reduce hyperglycaemia in patients with diabetes. In fact, various small molecule compounds have been developed and clinically tested as glucokinase activators. However, some have been discontinued because of efficacy and safety issues. One of these issues is loss of the drug's efficacy over time. This unsustained glycaemic efficacy may be associated with the excess glycolysis by glucokinase activation in pancreatic beta cells, resulting in beta-cell failure. Recently, we have shown that glucokinase haploinsufficiency ameliorated glucose intolerance by increasing beta-cell function and mass in a mouse model of diabetes. Given that a similar phenotype has been observed in glucokinase-activated beta cells and diabetic beta cells, glucokinase inactivation may be a new therapeutic target for type 2 diabetes."xsd:string
http://purl.uniprot.org/citations/34105236http://purl.org/dc/terms/identifier"doi:10.1111/dom.14459"xsd:string
http://purl.uniprot.org/citations/34105236http://purl.uniprot.org/core/author"Nakamura A."xsd:string
http://purl.uniprot.org/citations/34105236http://purl.uniprot.org/core/author"Omori K."xsd:string
http://purl.uniprot.org/citations/34105236http://purl.uniprot.org/core/author"Terauchi Y."xsd:string
http://purl.uniprot.org/citations/34105236http://purl.uniprot.org/core/date"2021"xsd:gYear
http://purl.uniprot.org/citations/34105236http://purl.uniprot.org/core/name"Diabetes Obes Metab"xsd:string
http://purl.uniprot.org/citations/34105236http://purl.uniprot.org/core/pages"2199-2206"xsd:string
http://purl.uniprot.org/citations/34105236http://purl.uniprot.org/core/title"Glucokinase activation or inactivation: Which will lead to the treatment of type 2 diabetes?"xsd:string
http://purl.uniprot.org/citations/34105236http://purl.uniprot.org/core/volume"23"xsd:string
http://purl.uniprot.org/citations/34105236http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/34105236
http://purl.uniprot.org/citations/34105236http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/34105236
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http://purl.uniprot.org/uniprot/#_M4PPI9-mappedCitation-34105236http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34105236
http://purl.uniprot.org/uniprot/#_M4PS72-mappedCitation-34105236http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34105236
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http://purl.uniprot.org/uniprot/#_M4Q000-mappedCitation-34105236http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34105236
http://purl.uniprot.org/uniprot/#_M4Q005-mappedCitation-34105236http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34105236