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您的检索式：作者名="Xiaohang Tong"
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| 1 | Recent progress on the modification of high nickel contentNCM:Coating,doping,and single crystallization显示文摘High nickel content layered cathodes,represented by NCM(LiNi_(x)Co_(y)Mn_(z)O_(2),x+y+z=1),are now widely employed in the market of electric vehicles,owing to their high energy density.With the gradual increase of nickel content and capacity,the issues on cycling life and safety become more serious.In this review,various strategies for improving the performance of high nickel NCM are summarized on the aspects of surface coating,ionic doping,and singlecrystal NCM.The coating strategy was separately described according to the physical property of coating species,including inert material coating,Li^(+)-conductor coating,electronic conductor coating,and mixed conductor coating.These coating species help to suppress the interfacial oxidation of electrolytes by NCM,improving the cycling life and safety.The elemental doping in the crystal lattice of NCM is then presented in the aspects of cation,anion,and mixed-ion doping,which are beneficial to stabilize the layered structure during charge–discharge and so promote the electrochemical performance.In quite recent years,the strategy of single-crystal NCM was demonstrated to be a promising pathway,owing to the dramatically reduced surface area and grain boundary.Finally,the remaining unsolved challenges and future strategies for further development of NCM cathode materials are outlined. | Junqing Yan Hao Huang Junfan Tong Wei Li Xiaohang Liu Haoxuan Zhang Heqin Huang Weidong Zhou | 2022 | Interdisciplinary Materials2022，1，3： | 2 |
| 2 | Structures of the N- and C-terminal domains of MHV-A59 nucleocapsid protein corroborate a conserved RNA-protein binding mechanism in coronavirus显示文摘Coronaviruses are the causative agent of respiratory and enteric diseases in animals and humans.One example is SARS,which caused a worldwide health threat in 2003.In coronaviruses,the structural protein N(nucleocapsid protein)associates with the viral RNA to form the filamentous nucleocapsid and plays a crucial role in genome replication and transcription.The structure of Nterminal domain of MHV N protein also implicated its specific affinity with transcriptional regulatory sequence(TRS)RNA.Here we report the crystal structures of the two proteolytically resistant N-(NTD)and C-terminal(CTD)domains of the N protein from murine hepatitis virus(MHV).The structure of NTD in two different crystal forms was solved to 1.5Å.The higher resolution provides more detailed structural information than previous reports,showing that the NTD structure from MHV shares a similar overall and topology structure with that of SARS-CoV and IBV,but varies in its potential surface,which indicates a possible difference in RNA-binding module.The structure of CTD was solved to 2.0-Åresolution and revealed a tightly intertwined dimer.This is consistent with analytical ultracentrifugation experiments,suggesting a dimeric assembly of the N protein.The similarity between the structures of these two domains from SARS-CoV,IBV and MHV corroborates a conserved mechanism of nucleocapsid formation for coronaviruses. | Yanlin Ma Xiaohang Tong Xiaoling Xu Xuemei Li Zhiyong Lou Zihe Rao | 2010 | Protein & Cell2010，1，7： | 2 |
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