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The methylglutaconyl-CoA hydratase, mitochondrial protein binds to the AU-rich element (ARE), a common element found in the 3' UTR of rapidly decaying mRNA such as c-fos, c-myc and granulocyte/ macrophage colony stimulating factor. De plus, nous expédions AU RNA Binding Protein/enoyl-CoA Hydratase Protéines (8) et AU RNA Binding Protein/enoyl-CoA Hydratase Kits (4) et beaucoup plus de produits pour cette protéine.
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Human Polyclonal AUH Primary Antibody pour WB - ABIN610746
Anderson, Teutsch, Dong, Wortis: An essential role for Bruton's [corrected] tyrosine kinase in the regulation of B-cell apoptosis. dans Proceedings of the National Academy of Sciences of the United States of America 1996
Show all 2 Pubmed References
AUH localizes to the inner mitochondrial membrane and matrix where it associates with mitochondrial ribosomes and regulates protein synthesis.
Phenotypic heterogeneity in two siblings with 3-methylglutaconic aciduria type I caused by a novel deletion of exons 1-3 within the AUH gene.
3-Methylglutaconic aciduria type I is caused by mutations in AUH
Human 3-methylglutaconyl-CoA hydratase is identical with RNA-binding protein (AUH); molecular analyses of MGA1 patients show homozygosity or compound heterozygosity for mutations in AUH.
Mutation analysis in the AUH gene revealed homozygosity for a novel splice site mutation IVS9-2A>G. We conclude that MGA1 may be associated with fever-associated seizures even in children without delayed psychomotor development.
Mutations in the AUH gene are linked to metabolic disease 3-methylglutaconic aciduria type I (MGA1).
The AUH trimer dimerizes upon binding to one molecule of a long RNA containing 24 repeats of the AUUU motif, (AUUU)(24)A.
The methylglutaconyl-CoA hydratase, mitochondrial protein binds to the AU-rich element (ARE), a common element found in the 3' UTR of rapidly decaying mRNA such as c-fos, c-myc and granulocyte/ macrophage colony stimulating factor. ARE elements are involved in directing RNA to rapid degradation and deadenylation. AUH is also homologous to enol-CoA hydratase, an enzyme involved in fatty acid degradation, and has been shown to have intrinsic hydratase enzymatic activity. AUH is thus a bifunctional chimera between RNA binding and metabolic enzyme activity. A possible subcellular localization in the mitochondria has been demonstrated for the mouse homolog of this protein which shares 92% identity with the human protein. It has been suggested that AUH may have a novel role as a mitochondrial located AU-binding protein. Human AUH is expressed as a single mRNA species of 1.8 kb, and translated as a 40-kDa precursor protein which is subsequently processed to a 32-kDa mature form.
, AU RNA binding protein/enoyl-Coenzyme A hydratase
, AU RNA-binding protein/enoyl-Coenzyme A hydratase
, AU-binding protein/Enoyl-CoA hydratase
, AU-specific RNA-binding enoyl-CoA hydratase
, methylglutaconyl-CoA hydratase, mitochondrial
, AU-binding enoyl-CoA hydratase
, AU RNA binding protein/enoyl-coenzyme A hydratase