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| 1 | Increased migratory properties of aortal smooth muscle cells exposed to calcitriol in culture显示文摘 | Cecylia Tukaj Piotr Trzonkowski Micha? Piku?a Anna Hallmann Stefan Tukaj | 2010 | Journal of Steroid Biochemistry and Molecular Biology2010，，1： | 1 |
| 2 | Cerebral vessels express interleukin 1 β after focal cerebral ischemia显示文摘 | Zhenggang Zhang Michael Chopp Anton Goussev Cecylia Powers | 1998 | Brain Research1998，，1： | 1 |
| 3 | Neurodamage and plasticity identified by MAP2, GAP43, CyclinDI imm unoreactivity after fo - cal cerebral ischemia in rats显示文摘 | Yi Li Ning Jiang Cecylia Powers | 1998 | Stroke1998，29，： | 1 |
| 4 | The temporal profiles of ICAM-1 protein and mRNA expression after transient MCA occlusion in the rat显示文摘 | Rui-Lan Zhang Michael Chopp Cecylia Zaloga Zheng G. Zhang Ning Jiang Subhash C. Gautam Wen Xue Tang Wayne Tsang Donald C. Anderson Anthony M. Manning | 1995 | Brain Research1995，，1： | 1 |
| 5 | A computational study of the chemokine receptor CXCR1 bound with interleukin-8显示文摘CXCR1 is a G-protein coupled receptor, transducing signals from chemokines, in particular the interleukin-8(IL8)molecules. This study combines homology modeling and molecular dynamics simulation methods to study the structure of CXCR1-IL8 complex. By using CXCR4-v MIP-II crystallography structure as the homologous template, CXCR1-IL8 complex structure was constructed, and then refined using all-atom molecular dynamics simulations. Through extensive simulations, CXCR1-IL8 binding poses were investigated in detail. Furthermore, the role of the N-terminal of CXCR1 receptor was studied by comparing four complex models differing in the N-terminal sequences. The results indicate that the receptor N-terminal affects the binding of IL8 significantly. With a shorter N-terminal domain, the binding of IL8 to CXCR1 becomes unstable. The homology modeling and simulations also reveal the key receptor-ligand residues involved in the electrostatic interactions known to be vital for complex formation. | 王洋 Cecylia Severin Lupala 王亭 李选选 Ji-Hye Yun Jae-hyun Park 金泽宇 Weontae Lee 汤雷翰 刘海广 | 2018 | Chinese Physics B2018，27，3： | 1 |
| 6 | Neuronal damage and plasticity identified by microtubule- associated protein 2,growth-associated protein 43,and cyclin D1 immunoreactivity after focal cerebral ischemia in rats 显示文摘 | Yi L Ning J Cecylia P | 1998 | Stroke1998，29，： | 1 |
| 7 | Computational simulations reveal the binding dynamics between human ACE2 and the receptor binding domain of SARS-CoV-2 spike protein显示文摘Background:A novel coronavirus(the SARS-CoV-2)has been identified in January 2020 as the causal pathogen for COVID-19,a pandemic started near the end of 2019.The Angiotensin converting enzyme 2 protein(ACE2)utilized by the SARS-CoV as a receptor was found to facilitate the infection of SARS-CoV-2,initiated by the binding of the spike protein to human ACE2.Methods:Using homology modeling and molecular dynamics(MD)simulation methods,we report here the detailed structure and dynamics of the ACE2 in complex with the receptor binding domain(RBD)of the SARS-CoV-2 spike protein.Results:The predicted model is highly consistent with the experimentally determined structures,validating the homology modeling results.Besides the binding interface reported in the crystal structures,novel binding poses are revealed from all-atom MD simulations.The simulation data are used to identify critical residues at the complex interface and provide more details about the interactions between the SARS-CoV-2 RBD and human ACE2.Conclusion:Simulations reveal that RBD binds to both open and closed state of ACE2.Two human ACE2 mutants and rat ACE2 are modeled to study the mutation effects on RBD binding to ACE2.The simulations show that the N-terminal helix and the K353 are very important for the tight binding of the complex,the mutants are found to alter the binding modes of the CoV2-RBD to ACE2. | Cecylia SLupala Xuanxuan Li Jian Lei Hong Chen Jianxun Qi Haiguang Liu Xiao-Dong Su | 2021 | Quantitative Biology2021，9，1： | 0 |
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