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Moments of the neutron<sub>g2</sub>structure function at intermediate<sup>Q2</sup>
Solvignon, P.,Liyanage, N.,Chen, J.-P.,Choi, Seonho,Slifer, K.,Aniol, K.,Averett, T.,Boeglin, W.,Camsonne, A.,Cates, G. D.,Chang, C. C.,Chudakov, E.,Craver, B.,Cusanno, F.,Deur, A.,Dutta, D.,Ent, R.,F American Physical Society 2015 PHYSICAL REVIEW C - Vol.92 No.1
Katich, J.,Qian, X.,Zhao, Y. X.,Allada, K.,Aniol, K.,Annand, J. R. M.,Averett, T.,Benmokhtar, F.,Bertozzi, W.,Bradshaw, P. C.,Bosted, P.,Camsonne, A.,Canan, M.,Cates, G. D.,Chen, C.,Chen, J.-P.,Chen, American Physical Society 2014 Physical Review Letters Vol.113 No.2
<P>We report the first measurement of the target-normal single-spin asymmetry in deep-inelastic scattering from the inclusive reaction 3)He()(e,e')X on a polarized (3)He gas target. Assuming time-reversal invariance, this asymmetry is strictly zero in the Born approximation but can be nonzero if two-photon-exchange contributions are included. The experiment, conducted at Jefferson Lab using a 5.89 GeV electron beam, covers a range of 1.7<W<2.9??GeV, 1.0<Q(2)<4.0??GeV(2) and 0.16<x<0.65. Neutron asymmetries were extracted using the effective nucleon polarization and measured proton-to-(3)He cross-section ratios. The measured neutron asymmetries are negative with an average value of (-1.090.38)10(-2) for invariant mass W>2??GeV, which is nonzero at the 2.89σ level. Our measured asymmetry agrees both in sign and magnitude with a two-photon-exchange model prediction that uses input from the Sivers transverse momentum distribution obtained from semi-inclusive deep-inelastic scattering.</P>
<i>In Vitro</i> and <i>In Vivo</i> Assessment of FK506 Analogs as Novel Antifungal Drug Candidates
Lee, Yeonseon,Lee, Kyung-Tae,Lee, Soo Jung,Beom, Ji Yoon,Hwangbo, Areum,Jung, Jin A,Song, Myoung Chong,Yoo, Young Ji,Kang, Sang Hyeon,Averette, Anna F.,Heitman, Joseph,Yoon, Yeo Joon,Cheong, Eunji,Bah American Society for Microbiology 2018 Antimicrobial Agents and Chemotherapy Vol.62 No.11
<P>FK506 (tacrolimus) is an FDA-approved immunosuppressant indicated for the prevention of allograft rejections in patients undergoing organ transplants. In mammals, FK506 inhibits the calcineurin-nuclear factor of activated T cells (NFAT) pathway to prevent T-cell proliferation by forming a ternary complex with its binding protein, FKBP12, and calcineurin. FK506 also exerts antifungal activity by inhibiting calcineurin, which is essential for the virulence of human-pathogenic fungi. Nevertheless, FK506 cannot be used directly as an antifungal drug due to its immunosuppressive action. In this study, we analyzed the cytotoxicity, immunosuppressive activity, and antifungal activity of four FK506 analogs, 31-O-demethyl-FK506, 9-deoxo-FK506, 9-deoxo-31-O-demethyl-FK506, and 9-deoxo-prolyl-FK506, in comparison with that of FK506. The four FK506 analogs generally possessed lower cytotoxicity and immunosuppressive activity than FK506. The FK506 analogs, except for 9-deoxo-prolyl-FK506, had strong antifungal activity against Ctyptococcus neoformans and Candida albicans, which are two major invasive pathogenic yeasts, due to the inhibition of the calcineurin pathway. Furthermore, the FK506 analogs, except for 9-deoxo-prolyl-FK506, had strong antifungal activity against the invasive filamentous fungus Aspergillus fumigatus. Notably, 9-deoxo-31-O-demethyl-FK506 and 31-O-demethyl-FK506 exhibited robust synergistic antifungal activity with fluconazole, similar to FK506. Considering the antifungal efficacy, cytotoxicity, immunosuppressive activity, and synergistic effect with commercial antifungal drugs, we selected 9-deoxo-31-O-demethyl-FK506 for further evaluation of its in vivo antifungal efficacy in a murine model of systemic cryptococcosis. Although 9-deoxo-31-O-demethyl-FK506 alone was not sufficient to treat the cryptococcal infection, when it was used in combination with fluconazole, it significantly extended the survival of C. neoformans-infected mice, confirming the synergistic in vivo antifungal efficacy between these two agents.</P>