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Journal Articles

First observation of $$^{28}$$O

Kondo, Yosuke*; Achouri, N. L.*; Al Falou, H.*; Atar, L.*; Aumann, T.*; Baba, Hidetada*; Boretzky, K.*; Caesar, C.*; Calvet, D.*; Chae, H.*; et al.

Nature, 620(7976), p.965 - 970, 2023/08

https://doi.org/10.1038/s41586-023-06352-6
 Times Cited Count：20 Percentile：95.45(Multidisciplinary Sciences)

no abstracts in English

Journal Articles

Intruder configurations in $$^{29}$$Ne at the transition into the island of inversion; Detailed structure study of $$^{28}$$Ne

Wang, H.*; Yasuda, Masahiro*; Kondo, Yosuke*; Nakamura, Takashi*; Tostevin, J. A.*; Ogata, Kazuyuki*; Otsuka, Takaharu*; Poves, A.*; Shimizu, Noritaka*; Yoshida, Kazuki; et al.

Physics Letters B, 843, p.138038_1 - 138038_9, 2023/08

https://doi.org/10.1016/j.physletb.2023.138038
 Times Cited Count：3 Percentile：71.80(Astronomy & Astrophysics)

Detailed $$gamma$$-ray spectroscopy of the exotic neon isotope $$^{28}$$Ne has been performed using the one-neutron removal reaction from $$^{29}$$Ne. Based on an analysis of parallel momentum distributions, a level scheme with spin-parity assignments has been constructed for $$^{28}$$Ne and the negative-parity states are identified for the first time. The measured partial cross sections and momentum distributions reveal a significant intruder p-wave strength providing evidence of the breakdown of the N = 20 and N = 28 shell gaps. Only a weak, possible f-wave strength was observed to bound final states. Large-scale shell-model calculations with different effective interactions do not reproduce the large p-wave and small f-wave strength observed experimentally, indicating an ongoing challenge for a complete theoretical description of the transition into the island of inversion along the Ne isotopic chain.

Journal Articles

Japanese Evaluated Nuclear Data Library version 5; JENDL-5

Iwamoto, Osamu; Iwamoto, Nobuyuki; Kunieda, Satoshi; Minato, Futoshi; Nakayama, Shinsuke; Abe, Yutaka*; Tsubakihara, Kosuke*; Okumura, Shin*; Ishizuka, Chikako*; Yoshida, Tadashi*; et al.

Journal of Nuclear Science and Technology, 60(1), p.1 - 60, 2023/01

https://doi.org/10.1080/00223131.2022.2141903
 Times Cited Count：144 Percentile：99.98(Nuclear Science & Technology)

Journal Articles

Mesospheric ionization during substorm growth phase

Murase, Kiyoka*; Kataoka, Ryuho*; Nishiyama, Takanori*; Nishimura, Koji*; Hashimoto, Taishi*; Tanaka, Yoshimasa*; Kadokura, Akira*; Tomikawa, Yoshihiro*; Tsutsumi, Masaki*; Ogawa, Yasunobu*; et al.

Journal of Space Weather and Space Climate (Internet), 12, p.18_1 - 18_16, 2022/06

https://doi.org/10.1051/swsc/2022012
 Times Cited Count：3 Percentile：11.91(Astronomy & Astrophysics)

We identified two energetic electron precipitation (EEP) events during the growth phase of moderate substorms and estimated the mesospheric ionization rate for an EEP event for which the most comprehensive dataset from ground-based and space-born instruments was available. The mesospheric ionization signature reached below 70 km altitude and continued for ~15 min until the substorm onset, as observed by the PANSY radar and imaging riometer at Syowa Station in the Antarctic region. We also used energetic electron flux observed by the Arase and POES 15 satellites as the input for the air-shower simulation code PHITS to quantitatively estimate the mesospheric ionization rate. Combining the cutting-edge observations and simulations, we shed new light on the space weather impact of the EEP events during geomagnetically quiet times, which is important to understand the possible link between the space environment and climate.

Journal Articles

How different is the core of $$^{25}$$F from $$^{24}$$O$$_{g.s.}$$ ?

Tang, T. L.*; Uesaka, Tomohiro*; Kawase, Shoichiro; Beaumel, D.*; Dozono, Masanori*; Fujii, Toshihiko*; Fukuda, Naoki*; Fukunaga, Taku*; Galindo-Uribarri, A.*; Hwang, S. H.*; et al.

Physical Review Letters, 124(21), p.212502_1 - 212502_6, 2020/05

https://doi.org/10.1103/PhysRevLett.124.212502
 Times Cited Count：18 Percentile：75.44(Physics, Multidisciplinary)

The structure of a neutron-rich $$^{25}$$F nucleus is investigated by a quasifree ($$p,2p$$) knockout reaction. The sum of spectroscopic factors of $$pi 0d_{5/2}$$ orbital is found to be 1.0 $$pm$$ 0.3. The result shows that the $$^{24}$$O core of $$^{25}$$F nucleus significantly differs from a free $$^{24}$$O nucleus, and the core consists of $$sim$$35% $$^{24}$$O$$_{rm g.s.}$$, and $$sim$$65% excited $$^{24}$$O. The result shows that the $$^{24}$$O core of $$^{25}$$F nucleus significantly differs from a free $$^{24}$$O nucleus. The result may infer that the addition of the $$0d_{5/2}$$ proton considerably changes the neutron structure in $$^{25}$$F from that in $$^{24}$$O, which could be a possible mechanism responsible for the oxygen dripline anomaly.

Journal Articles

Determination of mole percentages of brush and root of polymer chain grafted onto porous sheet

Uchiyama, Shoichiro*; Ishihara, Ryo*; Umeno, Daisuke*; Saito, Kyoichi*; Yamada, Shinsuke*; Hirota, Hideyuki*; Asai, Shiho

Journal of Chemical Engineering of Japan, 46(6), p.414 - 419, 2013/06

https://doi.org/10.1252/jcej.12we274
 Times Cited Count：7 Percentile：25.12(Engineering, Chemical)

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

https://doi.org/10.1074/jbc.M109.007286
 Times Cited Count：24 Percentile：46.00(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.

Oral presentation

Expression and characterization of interleukin-13 receptor $$alpha$$2 chain (IL-13R$$alpha$$2)

Matsumoto, Fumiko; Tamada, Taro; Honjo, Eijiro*; Ota, Shoichiro*; Izuhara, Kenji*; Kuroki, Ryota

no journal, , 

The allergic disease has dramatically increased in recent years. Interleukin-13 (IL-13) is a key cytokine critical to the development of T-cell-mediated humoral immune responses which are associated with allergy and asthma. IL-13 possesses two types of receptor: the heterodimer, composed of IL-13R$$alpha$$1 and IL-4R$$alpha$$, transducing the IL-13 signals; and the IL-13R$$alpha$$2, acting as a nonsignaling "decoy" receptor. Although the extracellular region of IL-13R$$alpha$$1 and IL-13R$$alpha$$2 are composed of a common structure of the class 1 cytokine receptor superfamily and they have similar amino acid sequence, the affinity of IL-13R$$alpha$$2 with IL-13 is more than ten-fold higher than that of IL-13R$$alpha$$1. In order to investigate the reason for this higher ligand affinity to IL-13R$$alpha$$2, extra cellular region of IL-13R$$alpha$$2 was expressed by silkworm-baculovirus expression system after fusing the DNA cording the extracellular region of human IL-13R$$alpha$$2 with the Fc derived from mouse IgG2a. The expressed fusion protein IL-13R$$alpha$$2-Fc was purified by a protein G column, and the affinity to IL-13 was confirmed by gel filtration followed by light scattering analysis. After Fc region was removed by thrombin digestion, the resulting extra cellular region of IL-13R$$alpha$$2 receptor was confirmed to retain strong affinity to IL-13 with 1:1 ratio.

Oral presentation

Inhibition mechanism of Interleukin-13 (IL-13) signal by extracellular region of IL-13 receptor$$alpha$$2 chain

Matsumoto, Fumiko; Hatanaka, Takaaki*; Tamada, Taro; Honjo, Eijiro*; Ota, Shoichiro*; Ito, Yuji*; Izuhara, Kenji*; Kuroki, Ryota

no journal, , 

Interleukin-13 (IL-13) is a key cytokine critical to the development of T-cell-mediated humoral immune responses which are associated with allergy and asthma. IL-13 possesses two types of receptor: the heterodimer, composed of IL-13R$$alpha$$1 and IL-4R$$alpha$$, transducing the IL-13 signals; and the IL-13R$$alpha$$2, it has high affinity rather than IL-13R$$alpha$$1 against IL-13, acting as a nonsignaling "decoy" receptor. In order to investigate the inhibition mechanism of IL-13 signal by IL-13R$$alpha$$2, extra cellular region of IL-13R$$alpha$$2 was expressed by silkworm-baculovirus expression system after fusing the DNA cording the extracellular region of human IL-13R$$alpha$$2 with the Fc derived from mouse IgG2a. The expressed fusion protein (IL-13R$$alpha$$2)2-Fc was purified by a protein A column followed by an ion exchange column. The affinities of the ligand complexes, IL-13/IL-13R$$alpha$$1 and IL-13/IL-13R$$alpha$$2 to (IL-4R$$alpha$$)2-Fc were investigated to explore the inactivation mechanism of the IL-13R$$alpha$$1 signal with IL-13R$$alpha$$2 by surface plasmon resonance analysis. IL-13/IL-13R$$alpha$$1 complex has an affinity (KD=1.20$$times$$10$$^{-7}$$ M) with (IL-4Ra)2-Fc, whereas the IL-13/IL-13R$$alpha$$2 complex had no affinity with (IL-4R$$alpha$$)2-Fc. This observation suggests that IL-13R$$alpha$$2 does not inactivate the IL-13R$$alpha$$1 through formation of a ternary complex with IL-13 and IL-4R$$alpha$$, but removes the IL-13 with its higher affinity to IL-13 without forming a ternary complex.

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