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Ishida, Tsuyoshi; Nakashima, Shinichi; Kondo, Shinji; Hayashibara, Kenichi; Yamada, Shigeki*; Okamoto, Ryo*; Nakamura, Hironobu
Dai-44-Kai Nihon Kaku Busshitsu Kanri Gakkai Nenji Taikai Kaigi Rombunshu (Internet), 4 Pages, 2023/11
no abstracts in English
evaluation of F(
-
I)KCCYSL for targeting HER2Sasaki, Ichiro; Watanabe, Shigeki; Ohshima, Yasuhiro; Sugo, Yumi; Yamada, Keiichi*; Hanaoka, Hirofumi*; Ishioka, Noriko
Peptide Science 2015, p.243 - 246, 2016/03
Li + 
Pb reactionNishinaka, Ichiro; Yokoyama, Akihiko*; Washiyama, Koshin*; Maeda, Eita*; Watanabe, Shigeki; Hashimoto, Kazuyuki; Ishioka, Noriko; Makii, Hiroyuki; Toyoshima, Atsushi; Yamada, Norihiro*; et al.
Journal of Radioanalytical and Nuclear Chemistry, 304(3), p.1077 - 1083, 2015/06
Times Cited Count：9 Percentile：60.64(Chemistry, Analytical)Production cross sections of astatine isotopes 
At in the 29-57 MeV Li induced reaction with Pb target have been measured by 
- and 
-ray spectrometry. Excitation functions of production cross sections have been compared with a statistical model calculation to study the reaction mechanism of Li + Pb. Considerably small experimental cross sections of 
At and 
At compared with the calculation were clearly observed at incident energies higher than 44 MeV, indicating that the effects of breakup reaction play a role. A chemical separation of astatine from an irradiated lead target has been studied with a dry-distillation method. A complementary way to produce astatine isotopes has been developed.
-lactamase from the moderate halophile 
sp.560 and the discovery of a Cs
-selective binding siteArai, Shigeki; Yonezawa, Yasushi*; Okazaki, Nobuo*; Matsumoto, Fumiko*; Shibazaki, Chie; Shimizu, Rumi; Yamada, Mitsugu*; Adachi, Motoyasu; Tamada, Taro; Kawamoto, Masahide*; et al.
Acta Crystallographica Section D, 71(3), p.541 - 554, 2015/03
Times Cited Count：7 Percentile：50.76(Biochemical Research Methods)The crystal structure of halophilic -lactamase from sp.560 (HaBLA) was determined using X-ray crystallography. Moreover, the locations of bound Sr
and Cs ions were identified by anomalous X-ray diffraction. The location of one Cs specific binding site was identified on HaBLA even in the presence of 9-fold molar excess of Na (90 mM Na /10 mM Cs). This Cs binding site is formed by two main-chain O atoms and an aromatic ring of a side chain of Trp. An aromatic ring of Trp interacts with Cs by the cation-
interaction. The observation of a selective and high-affinity Cs binding site provides important information that is useful for designing artificial Cs binding sites useful in bioremediation of radioactive isotopes.
Sasaki, Ichiro; Hanaoka, Hirofumi*; Yamada, Keiichi*; Watanabe, Shigeki; Sugo, Yumi; Ohshima, Yasuhiro; Suzuki, Hiroyuki; Ishioka, Noriko
Peptide Science 2014, p.257 - 260, 2015/03
Sasaki, Ichiro; Yamada, Keiichi*; Watanabe, Shigeki; Hanaoka, Hirofumi*; Sugo, Yumi; Oku, Hiroyuki*; Ishioka, Noriko
JAEA-Review 2013-059, JAEA Takasaki Annual Report 2012, P. 96, 2014/03
Sasaki, Ichiro; Yamada, Keiichi*; Watanabe, Shigeki; Hanaoka, Hirofumi*; Sugo, Yumi; Oku, Hiroyuki*; Ishioka, Noriko
Peptide Science 2013, p.157 - 160, 2013/03
I]-sansalvamide A derivativeWatanabe, Shigeki; Yamada, Keiichi*; Tsukui, Narutaka*; Hanaoka, Hirofumi*; Ohshima, Yasuhiro; Yamaguchi, Aiko*; Oku, Hiroyuki*; Ishioka, Noriko
JAEA-Review 2012-046, JAEA Takasaki Annual Report 2011, P. 88, 2013/01
Br-labeled amino acid derivative for PET imaging of tumorHanaoka, Hirofumi*; Watanabe, Shigeki; Tominaga, Hideyuki*; Ohshima, Yasuhiro; Watanabe, Satoshi; Yamada, Keiichi*; Iida, Yasuhiko*; Ishioka, Noriko; Endo, Keigo*
JAEA-Review 2012-046, JAEA Takasaki Annual Report 2011, P. 89, 2013/01
no abstracts in English
Cu-labeled DOTA-
-Phe
-Tyr
-octreotide (Cu-DOTA-TOC) for imaging somatostatin receptor-expressing tumorsHanaoka, Hirofumi*; Tominaga, Hideyuki*; Yamada, Keiichi*; Paudyal, P.*; Iida, Yasuhiko*; Watanabe, Shigeki; Paudyal, B.*; Higuchi, Tetsuya*; Oriuchi, Noboru*; Endo, Keigo*
Annals of Nuclear Medicine, 23(6), p.559 - 567, 2009/08
Times Cited Count：17 Percentile：46.65(Radiology, Nuclear Medicine & Medical Imaging)Tsukui, Narutaka; Watanabe, Shigeki; Yamada, Keiichi*; Hanaoka, Hirofumi*; Oku, Hiroyuki*; Matsuo, Ichiro*; Endo, Keigo*; Ishioka, Noriko
no journal, ,
no abstracts in English
Tsukui, Narutaka; Watanabe, Shigeki; Hanaoka, Hirofumi*; Yamada, Keiichi*; Oku, Hiroyuki*; Ishioka, Noriko; Endo, Keigo*; Matsuo, Ichiro*
no journal, ,
no abstracts in English
Br-labeled amino acid derivative for PET imaging of tumorHanaoka, Hirofumi*; Watanabe, Shigeki; Tominaga, Hideyuki*; Ohshima, Yasuhiro; Tsukui, Narutaka; Watanabe, Satoshi; Yamada, Keiichi*; Iida, Yasuhiko*; Oriuchi, Noboru*; Higuchi, Tetsuya*; et al.
no journal, ,
no abstracts in English
Tsukui, Narutaka; Yamada, Keiichi*; Watanabe, Shigeki; Hanaoka, Hirofumi*; Oku, Hiroyuki*; Endo, Keigo*; Ishioka, Noriko; Matsuo, Ichiro*
no journal, ,
I-Sansalvamide AWatanabe, Shigeki; Tsukui, Narutaka; Hanaoka, Hirofumi*; Yamada, Keiichi*; Ohshima, Yasuhiro; Iida, Yasuhiko*; Endo, Keigo*; Ishioka, Noriko
no journal, ,
no abstracts in English
-Lactamase derived from sp.560Arai, Shigeki; Tokunaga, Hiroko*; Tamada, Taro; Yonezawa, Yasushi; Adachi, Motoyasu; Yamada, Mitsugu; Ishibashi, Matsujiro*; Tokunaga, Masao*; Kuroki, Ryota
no journal, ,
Halophilic proteins can bind various inorganic ions with its negative charges located over the molecular surface. We are investigating the molecular structure of the halophilic proteins because halophilic proteins might be used as a material capturing for the rare metals and/or the radioactive metal ions. Recently, we succeeded in X-ray crystallographic analysis of the halophilic -Lactamase (HaBLA) derived from sp.560 at 3.0 
resolution. From this structural analysis, we found that the back bone structure and the positively charged active site feature of HaBLA was similar to those of non-halophilic BLA. The molecular surface of HaBLA were, however, occupied by large number of negative charges. This structural information is very useful to improve the specificity of metals such as Cs or Sr.
Yamada, Keiichi*; Watanabe, Shigeki; Ohshima, Yasuhiro; Hanaoka, Hirofumi*; Tsukui, Narutaka*; Takano, Chikako*; Yamaguchi, Aiko*; Oku, Hiroyuki*; Ishioka, Noriko
no journal, ,
I labeled cyclic peptide, Sansalvamide AWatanabe, Shigeki; Yamada, Keiichi*; Hanaoka, Hirofumi*; Ohshima, Yasuhiro; Tsukui, Narutaka*; Takano, Chikako*; Yamaguchi, Aiko*; Oku, Hiroyuki*; Iida, Yasuhiko*; Endo, Keigo*; et al.
no journal, ,
no abstracts in English
Li+Pb reaction and simple chemical separation of astatineNishinaka, Ichiro; Yokoyama, Akihiko*; Washiyama, Koshin*; Amano, Ryohei*; Ri, Keiko*; Yamada, Norihiro*; Ishiguro, Rika*; Maeda, Eita*; Makii, Hiroyuki; Hashimoto, Kazuyuki; et al.
no journal, ,
We have started to study production and utilization of an radioactive nuclide 
At which is a prospective candidate for targeted alpha radiotherapy. We determined production cross sections of astatine radioisotopes in the reaction of 29-48 MeV Li+Pb by -ray and -ray spectrometry at the tandem accelerator of JAEA-Tokai. Besides, we developed a simple dry-chemical method for separation of astatine.
Pb reactionNishinaka, Ichiro; Yokoyama, Akihiko*; Washiyama, Koshin*; Amano, Ryohei*; Maeda, Eita*; Yamada, Norihiro*; Makii, Hiroyuki; Watanabe, Shigeki; Ishioka, Noriko; Hashimoto, Kazuyuki
no journal, ,
