The N/Z ratio of free nucleons from collisions of neutron-rich nuclei as a function of their momentum is studied by means of isospin-dependent Quantum Molecular Dynamics. We find that this ratio is not only sensitive ...The N/Z ratio of free nucleons from collisions of neutron-rich nuclei as a function of their momentum is studied by means of isospin-dependent Quantum Molecular Dynamics. We find that this ratio is not only sensitive to the form of the density dependence of the symmetry potential energy but also its strength determined by the symmetry energy coefficient. The uncertainties about the symmetry energy coefficient influence the accuracy of probing the density dependence of the symmetry energy by means of the N/Z ratio of free nucleons of neutron-rich nuclei.展开更多
In the References of the original publication[1]of this paper,the authors of ref.[26]should be'S.A.Bass,et al.(UrQMD Collaboration)',the authors of ref.[27]should be'M.Ble-icher,et al.(UrQMD Collaboration)...In the References of the original publication[1]of this paper,the authors of ref.[26]should be'S.A.Bass,et al.(UrQMD Collaboration)',the authors of ref.[27]should be'M.Ble-icher,et al.(UrQMD Collaboration)'.The authors of ref.[35]should be'W.Reisdorf,et al.(FOPI Collaboration)',展开更多
A eukaryotic cell contains thousands of proteins that regulate its cellular function; delivering functional proteins into cells to rectify cellular functions holds great promise for treatment of various diseases, espe...A eukaryotic cell contains thousands of proteins that regulate its cellular function; delivering functional proteins into cells to rectify cellular functions holds great promise for treatment of various diseases, especially cancers. In this context, ribonuclease （RNase）, an enzyme that breaks down ribonucleic acid （RNA）, has great potential for cancer therapy. However, its therapeutic application is hampered by poor intracellular delivery efficiency and inhibition by ubiquitous intracellular RNase inhibitors. In this work, by designing and synthesizing RNase nano-conjugates by in situ atom transfer radical polymerization （ATRP）, we demonstrate a simple solution to address both challenges. Compared with native RNase, nano-conjugates exhibit significantly enhanced intracellular delivery efficiency, inhibitor resistance, and a near five-fold increase in cytotoxicity. This work provides a novel platform for delivery of therapeutic proteins for cancer therapy and other applications.展开更多
基金The project supported by National Natural Science Foundation of China under Grant Nos.10175093 and 10235030+4 种基金the Science Foundation of Chinese Nuclear Industry and the State Key Basic Research Development Program under Contract No.G20000774the Knowledge Innovation Project of the Chinese Academy of Sciences under Grant No.KJCX2-SW-N02the CASK.C.Wong Post-doctors Research Award Fund
文摘The N/Z ratio of free nucleons from collisions of neutron-rich nuclei as a function of their momentum is studied by means of isospin-dependent Quantum Molecular Dynamics. We find that this ratio is not only sensitive to the form of the density dependence of the symmetry potential energy but also its strength determined by the symmetry energy coefficient. The uncertainties about the symmetry energy coefficient influence the accuracy of probing the density dependence of the symmetry energy by means of the N/Z ratio of free nucleons of neutron-rich nuclei.
文摘In the References of the original publication[1]of this paper,the authors of ref.[26]should be'S.A.Bass,et al.(UrQMD Collaboration)',the authors of ref.[27]should be'M.Ble-icher,et al.(UrQMD Collaboration)'.The authors of ref.[35]should be'W.Reisdorf,et al.(FOPI Collaboration)',
文摘A eukaryotic cell contains thousands of proteins that regulate its cellular function; delivering functional proteins into cells to rectify cellular functions holds great promise for treatment of various diseases, especially cancers. In this context, ribonuclease （RNase）, an enzyme that breaks down ribonucleic acid （RNA）, has great potential for cancer therapy. However, its therapeutic application is hampered by poor intracellular delivery efficiency and inhibition by ubiquitous intracellular RNase inhibitors. In this work, by designing and synthesizing RNase nano-conjugates by in situ atom transfer radical polymerization （ATRP）, we demonstrate a simple solution to address both challenges. Compared with native RNase, nano-conjugates exhibit significantly enhanced intracellular delivery efficiency, inhibitor resistance, and a near five-fold increase in cytotoxicity. This work provides a novel platform for delivery of therapeutic proteins for cancer therapy and other applications.
