Novel pi-electron systems with trifluoromethylphenyl groups and/or a thiazolothiazole unit were developed as n-type semiconductors for OFETs. They showed excellent n-type performances with high electron mobilities. The trifluoromethylphenyl group was found to be very effective in inducing n-type behavior. The thiazolothiazole unit was favorable for forming stacking structures leading to efficient intermolecular pi-pi interactions.
Novel thiazole oligomers and thiazole/thiophene co-oligomers with trifluoromethylphenyl groups were developed as n-type semiconductors for OFETs. They showed excellent n-type performances with high electron mobilities. A 5,5'-bithiazole with trifluoromethylphenyl groups forms a closely packed two-dimensional columnar structure leading to a high performance n-type FET. The electron mobility was enhanced to 1.83 cm2/Vs on the OTS-treated substrate.
We examined the intracellular distribution of 8-oxo-dGTPase (8-oxo-7,8-dihydrodeoxyguanosine triphosphatase) encoded by the MTH1 gene, a human mutator homologue. The activity of 8-oxo-dGTPase mainly located in cytosolic and mitochondrial soluble fractions of Jurkat cells, a human T-cell leukemia line. Electron microscopic immunocytochemistry, using a specific antibody against MTH1 protein, showed localization of MTH1 protein in the mitochondrial matrix. Activity in the mitochondria accounted for about 4% of the total activity. The specific activity in the mitochondrial soluble fraction (8093 units/mg protein) was as high as that in the cytosolic fraction (8111 unit/mg protein). The 8-oxo-dGTPase activities in cytosolic and mitochondrial soluble fractions co-eluted with MTH1 protein by anion-exchange chromatography, and the molecular mass of the mitochondrial MTH1 protein was much the same as that of the cytosolic MTH1 protein (about 18 kDa). HeLa cells expressing MTH1 cDNA showed an increased cytoplasmic signal together with a weak signal in the nucleus in in situ immunostaining of MTH1 protein, and the overexpressed MTH1 protein was recovered from both cytosolic and mitochondrial fractions. Thus, the 8-oxo-dGTPase encoded by MTH1 gene is localized in mitochondrial and cytosol.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.