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Asymmetric arginine dimethylation determines life span in C. elegans by regulating forkhead transcription factor DAF-16.
Arginine methylation is a widespread posttranslational modification of proteins catalyzed by a family of protein arginine methyltransferases (PRMTs). It is well established that PRMTs are implicatedExpand
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The C. elegans PRMT-3 possesses a type III protein arginine methyltransferase activity
Protein arginine methylation is a common post-translational modification in eukaryotes that is catalyzed by a family of the protein arginine methyltransferases (PRMTs). PRMTs are classified intoExpand
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Synthesis and anti-barnacle activities of novel 3-isocyanotheonellin analogues
An antifouling active natural compound, 3-isocyanotheonellin, and its analogues were synthesized and evaluated for antifouling activity against the larvae of the barnacle Balanus amphirite in orderExpand
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EFFECT OF HIGH PRESSURE TREATMENT ON CYTOPLASMIC 5′‐NUCLEOTIDASE FROM RABBIT SKELETAL MUSCLE
We investigated the effect of high-pressure treatment on the properties of cytoplasmic 5′-nucleotidase (NT), which converts inosine monophosphate (IMP) into inosine. After pressure treatment at 400Expand
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Long-term reproduction in mouse populations of different origin.
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The GATA transcription factor ELT-2 modulates both the expression and methyltransferase activity of PRMT-1 in Caenorhabditis elegans
Protein arginine methyltransferase 1 (PRMT1) catalyzes asymmetric arginine dimethylation of cellular proteins and thus modulates various biological processes, including gene regulation, RNAExpand
Dietary Protein Sources Modify the Cholesterol-Lowering Effect of Saponins in Chicks.
Effects of casein (CAS) and casein hydrolysate (CHY) as the dietary protein sources on serum and liver cholesterol concentrations in chicks were compared in the first experiment. Next, effects ofExpand
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[Recent progress in alternatives to toxicity tests. 2. Tissue culture using mammalian fetuses].