Pub. Date : 2007 Oct
PMID : 17682063
9 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | MafA stability in pancreatic beta cells is regulated by glucose and is dependent on its constitutive phosphorylation at multiple sites by glycogen synthase kinase 3. | Glucose | v-maf musculoaponeurotic fibrosarcoma oncogene family, protein A (avian) | Mus musculus |
| 2 | Based on increased C1-binding activity, MafA protein levels appear to be up-regulated in response to glucose, but the underlying molecular mechanism for this is not well understood. | Glucose | v-maf musculoaponeurotic fibrosarcoma oncogene family, protein A (avian) | Mus musculus |
| 3 | Mutational analysis of MafA and pharmacological inhibition of GSK3 in MIN6 beta cells strongly suggest that the rate of MafA protein degradation is regulated by glucose, that MafA is constitutively phosphorylated by GSK3, and that phosphorylation is a prerequisite for rapid degradation of MafA under low-glucose conditions. | Glucose | v-maf musculoaponeurotic fibrosarcoma oncogene family, protein A (avian) | Mus musculus |
| 4 | Mutational analysis of MafA and pharmacological inhibition of GSK3 in MIN6 beta cells strongly suggest that the rate of MafA protein degradation is regulated by glucose, that MafA is constitutively phosphorylated by GSK3, and that phosphorylation is a prerequisite for rapid degradation of MafA under low-glucose conditions. | Glucose | v-maf musculoaponeurotic fibrosarcoma oncogene family, protein A (avian) | Mus musculus |
| 5 | Mutational analysis of MafA and pharmacological inhibition of GSK3 in MIN6 beta cells strongly suggest that the rate of MafA protein degradation is regulated by glucose, that MafA is constitutively phosphorylated by GSK3, and that phosphorylation is a prerequisite for rapid degradation of MafA under low-glucose conditions. | Glucose | v-maf musculoaponeurotic fibrosarcoma oncogene family, protein A (avian) | Mus musculus |
| 6 | Mutational analysis of MafA and pharmacological inhibition of GSK3 in MIN6 beta cells strongly suggest that the rate of MafA protein degradation is regulated by glucose, that MafA is constitutively phosphorylated by GSK3, and that phosphorylation is a prerequisite for rapid degradation of MafA under low-glucose conditions. | Glucose | v-maf musculoaponeurotic fibrosarcoma oncogene family, protein A (avian) | Mus musculus |
| 7 | Mutational analysis of MafA and pharmacological inhibition of GSK3 in MIN6 beta cells strongly suggest that the rate of MafA protein degradation is regulated by glucose, that MafA is constitutively phosphorylated by GSK3, and that phosphorylation is a prerequisite for rapid degradation of MafA under low-glucose conditions. | Glucose | v-maf musculoaponeurotic fibrosarcoma oncogene family, protein A (avian) | Mus musculus |
| 8 | Mutational analysis of MafA and pharmacological inhibition of GSK3 in MIN6 beta cells strongly suggest that the rate of MafA protein degradation is regulated by glucose, that MafA is constitutively phosphorylated by GSK3, and that phosphorylation is a prerequisite for rapid degradation of MafA under low-glucose conditions. | Glucose | v-maf musculoaponeurotic fibrosarcoma oncogene family, protein A (avian) | Mus musculus |
| 9 | Our data suggest a new glucose-sensing signaling pathway in islet beta cells that regulates insulin gene expression through the regulation of MafA protein stability. | Glucose | v-maf musculoaponeurotic fibrosarcoma oncogene family, protein A (avian) | Mus musculus |