- 著者
- Ryota Matsuki Takaaki Arai Masaharu Kogure Yutaka Suzuki Yoshihiro Sakamoto
- 出版者
- International Research and Cooperation Association for Bio & Socio-Sciences Advancement
- 雑誌
- BioScience Trends (ISSN:18817815)
- 巻号頁・発行日
- pp.2021.01103, (Released:2021-03-26)
- 参考文献数
- 12
- 被引用文献数
- 6
Pancreatic cancer is known to have the poorest prognosis among digestive cancers. With the development of new chemotherapeutic agents and introduction of multidisciplinary therapy, however, the treatment outcomes for pancreatic cancer have dramatically improved over the past two decades. The keys to successful treatment will be accurate assessment of resectability [resectable (R), borderline resectable (BR) or unresectable (UR)] at the time of diagnosis and prompt adoption of an appropriate multidisciplinary treatment strategy. Prep-02/JSAP-05 trial which is an RCT of upfront surgery versus neoadjuvant chemotherapy using GEM and S-1 (GS) and subsequent surgery for R-PDAC in Japan indicated neoadjuvant chemotherapy had a longer overall survival (OS) than those undergoing upfront surgery (36.7M vs. 26.6M, p = 0.015). In a retrospective multicenter study in Japan reported that in BR-PDAC, median survival time (MST) in the pretreatment group was significantly better than that in the upfront surgery group (25.7 months vs. 19.0 months, p = 0.015) according to a propensity score matching analysis. Another retrospective multicenter study with UR-LA PDAC in Japan reported that conversion surgery was more beneficial for patients with more than 8 months of preoperative therapy than those with less than 8 months of that therapy. Various clinical trials on pancreatic cancer are ongoing, and the results of trials on chemotherapeutic regimens and multidisciplinary treatments will be of further interest.
- 著者
- Ken T. Murata Hidenobu Watanabe Kazunori Yamamoto Eizen Kimura Masahiro Tanaka Osamu Tatebe Kentaro Ukawa Kazuya Muranaga Yutaka Suzuki Hirotsugu Kojima
- 出版者
- (社)電子情報通信学会
- 雑誌
- IEICE Communications Express (ISSN:21870136)
- 巻号頁・発行日
- vol.3, no.2, pp.74-79, 2014-02-25 (Released:2014-02-25)
- 参考文献数
- 6
- 被引用文献数
- 4 7
A variety of satellite missions are carried out every year. Most of the satellites yield big data, and high-performance data processing technologies are expected. We have been developing a cloud system (the NICT Science Cloud) for big data analyses of Earth and Space observations via spacecraft. In the present study, we propose a new technique to process big data considering the fact that high-speed I/O (data file read and write) is important compared with data processing speed. We adopt a task scheduler, the Pwrake, for easy development and management of parallel data processing. Using a set of long-time scientific satellite observation data (GEOTAIL satellite), we examine the performance of the system on the NICT Science Cloud. We successfully archived high-speed data processing more than 100 times faster than those on traditional data processing environments.
- 著者
- Yutaka SUZUKI Yoichi MIZUTANI Tadao TSUJI Naoto OHTANI Kazufumi TAKANO Mitsuru HARUKI Masaaki MORIKAWA Shigenori KANAYA
- 出版者
- Japan Society for Bioscience, Biotechnology, and Agrochemistry
- 雑誌
- Bioscience, Biotechnology, and Biochemistry (ISSN:09168451)
- 巻号頁・発行日
- vol.69, no.2, pp.364-373, 2005 (Released:2005-02-23)
- 参考文献数
- 39
- 被引用文献数
- 19
The gene encoding alkaline phosphatase from the psychrotrophic bacterium Shewanella sp. SIB1 was cloned, sequenced, and overexpressed in Escherichia coli. The recombinant protein was purified and its enzymatic properties were compared with those of E. coli alkaline phosphatase (APase), which shows an amino acid sequence identity of 37%. The optimum temperature of SIB1 APase was 50 °C, lower than that of E. coli APase by 30 °C. The specific activity of SIB1 APase at 50 °C was 3.1 fold higher than that of E. coli APase at 80 °C. SIB1 APase lost activity with a half-life of 3.9 min at 70 °C, whereas E. coli APase lost activity with a half-life of >6 h even at 80 °C. Thus SIB1 APase is well adapted to low temperatures. Comparison of the amino acid sequences of SIB1 and E. coli APases suggests that decreases in electrostatic interactions and number of disulfide bonds are responsible for the cold-adaptation of SIB1 APase.