Inhibition of FGF10-ERK signal activation suppresses intraductal papillary neoplasm of the bile duct and its associated carcinomas

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NADPH activation of deoxycytidylate kinase in rat liver extract: involvement of an endogenous disulfide reductase system.

Deoxycytidylate kinase (EC 2.7.4.14) in cell-free extract of rat liver, whose activity was highly dependent on the presence of high concentrations of thiol compound during incubation prior to assay, could be activated by substituting 0.1 to 0.2 mM NADPH for the thiol. Partial purification of the extract resulted in a separation of components indicating that the NADPH-dependent activation system was composed of, other than kinase itself, at least two protein factors: one was heat-stable and the other was indistinguishable from NADPH-dependent disulfide reductase [4]. Similarity of this system to thioredoxin-thioredoxin reductase system [7] is noted.     

OGT Regulates Hematopoietic Stem Cell Maintenance via PINK1-Dependent Mitophagy

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Validity of the agonid fish,Podothecus hamlini,and the first confirmed record from Japanese waters

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Regulation of human tyrosine hydroxylase activity. Effects of cyclic AMP-dependent protein kinase, calmodulin-dependent protein kinase II and polyanion

To determine the regulatory mechanism for human tyrosine hydroxylase, we examined modulations of the activity of the enzyme from human pheochromocytoma by cyclic AMP-dependent protein kinase, calmodulin-dependent protein kinase II and polyanion. The most remarkable activation was observed when the enzyme was assayed at physiological pH (pH 7) after being subjected to phosphorylation by cyclic AMP-dependent protein kinase. Calmodulin-dependent protein kinase II and polyanion also modulated the enzyme activity. The results suggest that tyrosine hydroxylase may be regulated similarly in both human and rat.