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        Modelling Resonance Dependent Angular Distribution via DBRC in Monte Carlo Codes

        R. Dagan,B. Becker,Y. Danon,M. Rapp,G. Lohnert 한국물리학회 2011 THE JOURNAL OF THE KOREAN PHYSICAL SOCIETY Vol.59 No.23

        The development of a new energy dependent double differential resonance scattering kernel by Rothenstein & Dagan, Annals of Nuclear Energy (1998) was shown to have a significant impact on core calculations as far as their criticality, Doppler Effect and the nuclide inventory is concerned. Thereafter, it was of great interest to experimentally validate this scattering kernel in addition to analytically proving its consistency with the integral Doppler broadened cross section, which was achieved by integrating the new kernel over all angles and all scattered energies. This study deals with the unique experiment suggested by Y. Danon at the Gaerttner Linear Accelerator Laboratory at Rensselaer Polytechnic Institute (RPI). The main advantage of this facility is the ability to move the neutron production source off axis relative to the detector beam line. It was, therefore, possible to position the sample, from which the neutron were scattered, on the same axis as the detector. In this way it was possible to directly measure the angular distribution of scattered neutron from heavy nuclides with pronounced resonances. In this study the previous results obtained for ^(238)U were extended to ^(232)Th. Improvements were made to the new resonance scattering kernel by development of a stochastic formalism known as DBRC (Doppler Broadened Rejection Correction) which was implemented by Becker et al. in several Monte Carlo codes. Based on the good agreement between this DBRC model and the measurements presented in this paper, it was shown that the standard asymptotic back angle scattering used previously in Monte Carlo codes differs by almost 80% for highly scattering resonances. Moreover, the scattering angle measurements and the ability to simulate it accurately by means of stochastic methods emphasized the deficiencies of the current methods which use only transmission and capture measurements.

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        Structural Switch of Lysyl-tRNA Synthetase between Translation and Transcription

        Ofir-Birin, Y.,Fang, P.,Bennett, Steven P.,Zhang, H.M.,Wang, J.,Rachmin, I.,Shapiro, R.,Song, J.,Dagan, A.,Pozo, J.,Kim, S.,Marshall, Alan G.,Schimmel, P.,Yang, X.L.,Nechushtan, H.,Razin, E.,Guo, M. Cell Press 2013 Molecular Cell Vol.49 No.1

        Lysyl-tRNA synthetase (LysRS), a component of the translation apparatus, is released from the cytoplasmic multi-tRNA synthetase complex (MSC) to activate the transcription factor MITF in stimulated mast cells through undefined mechanisms. Here we show that Ser207 phosphorylation provokes a new conformer of LysRS that inactivates its translational function but activates its transcriptional function. The crystal structure of an MSC subcomplex established that LysRS is held in the MSC by binding to the N terminus of the scaffold protein p38/AIMP2. Phosphorylation-created steric clashes at the LysRS domain interface disrupt its binding grooves for p38/AIMP2, releasing LysRS and provoking its nuclear translocation. This alteration also exposes the C-terminal domain of LysRS to bind to MITF and triggers LysRS-directed production of the second messenger Ap<SUB>4</SUB>A that activates MITF. Thus our results establish that a single conformational change triggered by phosphorylation leads to multiple effects driving an exclusive switch of LysRS function from translation to transcription.

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