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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：24 Percentile：45.24(Biochemistry & Molecular Biology)Both IL-4 and IL-13 can bind to the shared receptor composed of the IL-4 receptor 
chain and the IL-13 receptor -1 chain (IL-13R1); 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-13R1, 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 
-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-13R1 allows the shared receptor to respond differentially to IL-4 and IL-13.
Nishimori, Nobuyuki; Bazarov, I.*; Dunham, B.*; Grames, J.*; Hernandez-Garcia, C.*; Jones, L.*; Militsyn, B.*; Poelker, M.*; Surles-Law, K.*; Yamamoto, Masahiro*
Proceedings of 45th Advanced ICFA Beam Dynamics Workshop on Energy Recovery Linacs (ERL '09) (Internet), p.6 - 23, 2009/06
Rao, T.*; Burrill, A.*; Chang, X. Y.*; Smedley, J.*; Nishitani, Tomohiro; Hernandez Garcia, C.*; Poelker, M.*; Seddon, E.*; Hannon, F. E.*; Sinclair, C. K.*; et al.
Nuclear Instruments and Methods in Physics Research A, 557(1), p.124 - 130, 2006/02
Times Cited Count：59 Percentile：96.04(Instruments & Instrumentation)In the past few years, there has been considerable interest in using an energy recovery linac (ERL) for future light sources and high-energy nuclear physics. The electron beam requirements of the ERLs under consideration span a wide range in parameters such as current, current density, frequency, operating temperatures, accelerating gradients etc. The design of the injector, whether it is normal conducting or superconducting, DC or RF, average current, temporal profile of the electron bunch all play key role in the choice of the photocathode. In this paper, we attempt to provide an overview of the available cathode materials, the pros and cons associated with each and the electron beam parameters they can provide.
