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Institution

Niigata University of Pharmacy and Applied Life Sciences

EducationNiigata, Japan
About: Niigata University of Pharmacy and Applied Life Sciences is a education organization based out in Niigata, Japan. It is known for research contribution in the topics: Oxidative stress & Gene. The organization has 718 authors who have published 962 publications receiving 19790 citations. The organization is also known as: Niigata Yakka Daigaku.


Papers
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Journal ArticleDOI
TL;DR: Compounds 1, 3, 12, and 14-16 can serve as new leads for further development of anti-AIDS agents as well as other benzylisoquinoline, aporphine, and bisbenzylisoquoline alkaloids, which were previously isolated from the leaves and embryo of Nelumbo nucifera and evaluated for anti-HIV activity.

375 citations

Journal ArticleDOI
TL;DR: The present study provides the evidence in novel mouse model that NASH-based fibrosis is an essential histological process for diabetic populations to accelerate the development of HCC.
Abstract: Hepatocellular carcinoma (HCC) is the third most common cause of cancer-related deaths. In addition to hepatitis viral infections, several cohort studies have shown that diabetes mellitus is a risk factor of HCC, making the incidence alarming high. However, it has not been demonstrated directly how diabetes develops to HCC, because of its difficulty to follow changes of liver histology in diabetic populations. Here, we report that non-alcoholic steatohepatitis (NASH) is pivotal to link diabetes with HCC by establishing a novel, reproducible NASH–HCC model in mice. Neonatal male mice exposed to low-dose streptozotocin (STZ) developed liver steatosis with diabetes 1 week after feeding high-fat diet (HFD). Continuous HFD decreased hepatic fat deposit whilst increased lobular inflammation with foam cell-like macrophages, showing NASH pathology. In parallel with decreased phagocytosis of macrophages, fibroblasts accumulated to form “chicken-wired” fibrosis. All mice developed multiple HCC later. Female mice treated with STZ–HFD and male mice treated with STZ alone showed diabetes but never developed HCC by the absence of NASH-based fibrosis. Thus, the present study provides the evidence in novel mouse model that NASH-based fibrosis is an essential histological process for diabetic populations to accelerate the development of HCC.

247 citations

Journal ArticleDOI
TL;DR: It is suggested that curcumin treatment protect against the development of DN in rats by reducing macrophage infiltration through the inhibition of NF-κB activation in STZ-induced diabetic rats.
Abstract: Background Chronic inflammation plays an important role in the progression of diabetic nephropathy (DN) and that the infiltration of macrophages in glomerulus has been implicated in the development of glomerular injury. We hypothesized that the plant polyphenolic compound curcumin, which is known to exert potent anti-inflammatory effect, would ameliorate macrophage infiltration in streptozotocin (STZ)-induced diabetic rats.

191 citations

Journal ArticleDOI
TL;DR: In this article, the Kankyo Techno Consul Consul, Kojidai 3-18-7, Nishi-ku, Kobe 651-2273, Japan, and e
Abstract: cProfesser Emeritus of Kyoto University, Tenjin, 3‐23‐12 Nagaoka-kyo, Kyoto 617‐0824, Japan, d Kankyo Techno Consul, Kojidai 3‐18‐7, Nishi-ku, Kobe 651‐2273, Japan, and e

184 citations

Journal ArticleDOI
TL;DR: It is shown that human ELAC1, which seems to correspond to the C-terminal half of 3' tRNase from ELAC2, also has 3'-tRNase activity, and eight ELac2 variants that seem to be associated with the occurrence of prostate cancer for 3-t RNase activity are examined.
Abstract: tRNA 3′ processing endoribonuclease (3′ tRNase) is an enzyme responsible for the removal of a 3′ trailer from precursor tRNA (pre-tRNA). We purified ∼85 kDa 3′ tRNase from pig liver and determined its partial sequences. BLAST search of them suggested that the enzyme was the product of a candidate human prostate cancer susceptibility gene, ELAC2, the biological function of which was totally unknown. We cloned a human ELAC2 cDNA and expressed the ELAC2 protein in Escherichia coli. The recombinant ELAC2 was able to cleave human pre-tRNAArg efficiently. The 3′ tRNase activity of the yeast ortholog YKR079C was also observed. The C-terminal half of human ELAC2 was able to remove a 3′ trailer from pre-tRNAArg, while the N‐terminal half failed to do so. In the human genome exists a gene, ELAC1, which seems to correspond to the C-terminal half of 3′ tRNase from ELAC2. We showed that human ELAC1 also has 3′-tRNase activity. Furthermore, we examined eight ELAC2 variants that seem to be associated with the occurrence of prostate cancer for 3′-tRNase activity. Seven ELAC2 variants which contain one to three amino acid substitutions showed efficient 3′-tRNase activities, while one truncated variant, which lacked a C-terminal half region, had no activity.

181 citations


Authors

Showing all 718 results

NameH-indexPapersCitations
Kuo Hsiung Lee8187529359
Gozoh Tsujimoto7132918303
Gerald Rimbach7034721345
Fang Rong Chang5544711652
Mahbubur Rahman5368812057
Akira Hirasawa5328011385
Yoshio Hirabayashi522508297
Hiroyuki Itabe501589919
Yoshihisa Takaishi463129038
Hiroshi Suzuki452487541
Hiroshi Terada453027682
Shigeo Nakajo431087063
Toshio Yamaguchi432586993
Makoto Makishima4226218610
Margery C. Beinfeld411666480
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
20222
202132
202035
201945
201839
201764