Tokyo University of Science

About: Tokyo University of Science is a education organization based out in Tokyo, Japan. It is known for research contribution in the topics: Catalysis & Thin film. The organization has 15800 authors who have published 24147 publications receiving 438081 citations. The organization is also known as: Tōkyō Rika Daigaku & Science University of Tokyo.

A layer-structured Na2CoP2O7 pyrophosphate cathode for sodium-ion batteries

Abstract: We introduce Na2CoP2O7 pyrophosphate as a new potential cathode for sodium-ion batteries Based on a layered structure, it offers a two-dimensional Na-diffusion pathway delivering a reversible capacity close to 80 mA h g−1 involving Co3+/Co2+ redox activity with an average potential of 3 V

β -Decay Half-Lives of Co76,77 , Ni79,80 , and Cu81 : Experimental Indication of a Doubly Magic Ni78

Abstract: The half-lives of 20 neutron-rich nuclei with $Z=27--30$ have been measured at the RIBF, including five new half-lives of $^{76}\mathrm{Co}(21.{7}_{\ensuremath{-}4.9}^{+6.5}\text{ }\text{ }\mathrm{ms})$, $^{77}\mathrm{Co}(13.{0}_{\ensuremath{-}4.3}^{+7.2}\text{ }\text{ }\mathrm{ms})$, $^{79}\mathrm{Ni}({43.0}_{\ensuremath{-}7.5}^{+8.6}\text{ }\text{ }\mathrm{ms})$, $^{80}\mathrm{Ni}(23.{9}_{\ensuremath{-}17.2}^{+26.0}\text{ }\text{ }\mathrm{ms})$, and $^{81}\mathrm{Cu}(73.2\ifmmode\pm\else\textpm\fi{}6.8\text{ }\text{ }\mathrm{ms})$. In addition, the half-lives of $^{73--75}\mathrm{Co}$, $^{74--78}\mathrm{Ni}$, $^{78--80}\mathrm{Cu}$, and $^{80--82}\mathrm{Zn}$ were determined with higher precision than previous works. Based on these new results, a systematic study of the $\ensuremath{\beta}$-decay half-lives has been carried out, which suggests a sizable magicity for both the proton number $Z=28$ and the neutron number $N=50$ in $^{78}\mathrm{Ni}$.

Involvement of uric acid transporter in increased renal clearance of the xanthine oxidase inhibitor oxypurinol induced by a uricosuric agent, benzbromarone.

Abstract: Benzbromarone has been reported to increase the renal clearance of oxypurinol, an active metabolite of allopurinol. We examined the renal transport of oxypurinol to determine whether such a change in renal clearance could be explained by altered transporter-mediated reabsorption. Since the first step of reabsorption takes place at the renal epithelial apical membrane, we focused on membrane transporters. Benzbromarone is an inhibitor of reabsorption of uric acid mediated by the uric acid transporter (URAT) URAT1 (SLC22A12), which is expressed at the apical membrane of proximal tubular cells in humans. Uptake of oxypurinol by Xenopus oocytes injected with complementary RNA of URAT1 was significantly higher than that by water-injected oocytes, and the uptake was saturable, with a Km of about 800 μM. Moreover, benzbromarone inhibited the oxypurinol uptake by URAT1 at concentrations as low as 0.01 μM. The uptake of oxypurinol by another organic anion transporter (OAT), OAT4 (SLC22A11), which is also expressed at the apical membrane of proximal tubular epithelial cells, was negligible, whereas the uptake of [3H]estrone-3-sulfate by OAT4 was significantly inhibited by oxypurinol. Furthermore, neither the transport activity of organic cation/carnitine transporter (OCTN) 1 nor OCTN2 was affected by oxypurinol or benzbromarone. These results indicate that URAT1 is involved in renal reabsorption of oxypurinol, and the increment of renal clearance of oxypurinol upon concomitant administration of benzbromarone could be due to drug interaction at URAT1.

Substitutions in the N-glycan core as regulators of biorecognition: the case of core-fucose and bisecting GlcNAc moieties.

Abstract: Core fucosylation and the bisecting N-acetylglucosamine residue are prominent natural substitutions of the N-glycan core. To address the issue of whether these two substituents can modulate ligand properties of complex-type biantennary N-glycans, we performed chemoenzymatic synthesis of the respective galactosylated and α2,3/6-sialylated N-glycans. Neoglycoproteins were then produced to determine these glycans' reactivities with sugar receptors in solid-phase assays and with tumor cells in vitro as well as their in vivo biodistribution profiles in mice. Slight protein-type-dependent changes were noted in lectin binding, including adhesion/growth-regulatory galectins as study objects, when the data were related to properties of N-glycans without or with only one core substituent. Monitoring binding in vitro revealed cell-type-dependent changes. They delimited the ligand activity of this glycan type from that of chains with un- and monosubstituted cores. A markedly prolonged serum half-life was conferred to...