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Journal Articles

Optimization of ion-beam irradiation for mutagenesis in soybean; Effects on plant growth and production of visibly altered mutants

Arase, Sachiko*; Hase, Yoshihiro; Abe, Jun*; Kasai, Megumi*; Yamada, Tetsuya*; Kitamura, Keisuke*; Narumi, Issei; Tanaka, Atsushi; Kanazawa, Akira*

Plant Biotechnology, 28(3), p.323 - 329, 2011/06

 Times Cited Count:20 Percentile:54.28(Biotechnology & Applied Microbiology)

Journal Articles

Production of visibly altered mutants by ion beam irradiation in soybean

Kanazawa, Akira*; Arase, Sachiko*; Abe, Jun*; Hase, Yoshihiro; Tanaka, Atsushi; Narumi, Issei

JAEA-Review 2009-041, JAEA Takasaki Annual Report 2008, P. 68, 2009/12

Journal Articles

Distinct structural requirements for interleukin-4 (IL-4) and IL-13 binding to the shared IL-13 receptor facilitate cellular tuning of cytokine responsiveness

Ito, Takachika*; Suzuki, Shoichi*; Kanaji, Sachiko*; Shiraishi, Hiroshi*; Ota, Shoichiro*; Arima, Kazuhiko*; Tanaka, Go*; Tamada, Taro; Honjo, Eijiro*; Garcia, K. C.*; et al.

Journal of Biological Chemistry, 284(36), p.24289 - 24296, 2009/09

 Times Cited Count:23 Percentile:45.4(Biochemistry & Molecular Biology)

Both IL-4 and IL-13 can bind to the shared receptor composed of the IL-4 receptor $$alpha$$ chain and the IL-13 receptor $$alpha$$-1 chain (IL-13R$$alpha$$1); however, the assembly mechanisms of these ligands to the receptor is different, enabling the principal functions of these ligands to be different. We have previously shown that the N-terminal Ig-like domain in IL-13R$$alpha$$1, called the D1 domain, is the specific and critical binding unit for IL-13. However, it has still remained obscure which the amino acid has specific binding capacity to IL-13 and why the D1 domain acts as the binding site for IL-13, but not IL-4. To address these questions, in this study, we performed the mutational analyses for the D1 domain, combining the structural data to identify the amino acids critical for binding to IL-13. Mutations of Lys76, Lys77, or Ile78 in c' strand in which the crystal structure showed interact with IL-13 and those of Trp65 and Ala79 adjacent to the interacting site, resulted in significant impairment of IL-13 binding, demonstrating that these amino acids generate the binding site. Furthermore, mutations of Val35, Leu38, or Val42 at N-terminal $$beta$$-strand also resulted in loss of IL-13 binding, probably from decrease structural stability. None of the mutations employed here affected IL-4 binding. These results demonstrate that the hydrophobic patch composed of Lys76, Lys77, and Ile78 is the IL-13 recognition site and solidify our understanding that the differential requirements of the D1 domain in IL-13R$$alpha$$1 allows the shared receptor to respond differentially to IL-4 and IL-13.

Journal Articles

Expression of the extracellular region of the human interleukin-4 receptor $$alpha$$ chain and interleukin-13 receptor $$alpha$$1 chain by a silkworm-baculovirus system

Honjo, Eijiro; Shoyama, Yoshinari; Tamada, Taro; Shigematsu, Hideki*; Hatanaka, Takaaki*; Kanaji, Sachiko*; Arima, Kazuhiko*; Ito, Yuji*; Izuhara, Kenji*; Kuroki, Ryota

Protein Expression and Purification, 60(1), p.25 - 30, 2008/07

 Times Cited Count:13 Percentile:33.69(Biochemical Research Methods)

The receptor binding to Interleukin (IL)-13 is composed of the IL-13 receptor $$alpha$$1 chain (IL-13R $$alpha$$1) and the IL-4 receptor $$alpha$$ chain (IL-4R $$alpha$$). In order to investigate the interaction of IL-13 with IL-13R $$alpha$$1 and IL-4R $$alpha$$, the DNA fragments coding the extracellular regions of human IL-13R $$alpha$$1 and the IL-4R $$alpha$$ were fused with mouse Fc and expressed by a silkworm-baculovirus system. The expressed receptors were successfully purified by affinity chromatography using protein A, and the Fc region was removed by thrombin digestion. Size exclusion chromatography and SPR analysis revealed that mixture of IL-13 and IL-13R$$alpha$$1 showed predominant affinity to IL-4R$$alpha$$, although neither detectable affinity of IL-13 nor IL-13R$$alpha$$1 was observed against IL-4R$$alpha$$. Combining these data with the moderate affinity of IL-13 to IL-13R$$alpha$$1, this indicates that IL-13 first binds to IL-13R$$alpha$$1 and recruits consequently to IL-4R.

Oral presentation

Environmental monitoring from resident's point of view

Eda, Itsumu*; Omine, Mayumi*; Nemoto, Norimasa*; Shimizu, Tomoko*; Tanaka, Sachiko*; Kashima, Takao*; Ito, Yukari*; Taniyama, Hiroshi*; Kamei, Mitsuru*; Yonezawa, Rika; et al.

no journal, , 

no abstracts in English

Oral presentation

Status of lithium target facility development in IFMIF/EVEDA project

Wakai, Eiichi; Kondo, Hiroo; Kanemura, Takuji; Furukawa, Tomohiro; Hirakawa, Yasushi; Nakaniwa, Koichi; Ito, Yuzuru; Tanaka, Hiroshi; Tsuji, Yoshiyuki*; Ito, Takahiro*; et al.

no journal, , 

no abstracts in English

Oral presentation

R&D of lithium target and test facilities for the fusion neutron source

Wakai, Eiichi; Kondo, Hiroo; Kanemura, Takuji; Hirakawa, Yasushi; Furukawa, Tomohiro; Kikuchi, Takayuki; Ito, Yuzuru*; Hoashi, Eiji*; Yoshihashi, Sachiko*; Horiike, Hiroshi*; et al.

no journal, , 

no abstracts in English

Oral presentation

Development and advancement of a real-time neutron monitor for boron neutron capture therapy

Ishikawa, Akihisa; Watanabe, Kenichi*; Yoshihashi, Sachiko*; Uritani, Akira*; Tanaka, Hiroki*; Sakurai, Yoshinori*; Masuda, Akihiko*

no journal, , 

no abstracts in English

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