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您的检索式：作者名="Qiangzhen Yang"
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| 1 | Structural Comparison and Drug Screening of Spike Proteins of Ten SARS-CoV-2 Variants显示文摘SARS-CoV-2(severe acute respiratory syndrome coronavirus 2)has evolved many variants with stronger infectivity and immune evasion than the original strain,including Alpha,Beta,Gamma,Delta,Epsilon,Kappa,lota,Lambda,and 21H strains.Amino acid mutations are enriched in the spike protein of SARS CoV-2.which plays a crucial role in cell infetion.However,the impact of these mutations on protein structure and function is unclear.Understanding the pathophysiology and pandemic feaures of these SARS-CoV-2 variants requires knowledge of the spike protein structures.Here,we obtained the spike protein structures of 10 main globally endemic SARS CoV-2 strains using AlphaFold2.The clustering analysis based on structural similarity revealed the unique features of the mainly pandemic SARS CoV-2 Delta variants.indicating that structural clusters can reflect the current characteristics of the epidemic more accurately than those based on the protein sequence.The analysis of the binding afinities of ACE2-RBD,antibody-NTD,and antibody-RBD complexes in the different variants revealed that the recognition of antibodies against SI NTD and RBD was decreased in the variants,especally the Delta variant compared with the original strain,which may induce the immune evasion of SARS-CoV-2 variants.Furthermore,by virtual screening the ZINC database against a high-accuracy predicted structure of Delta spike protein and experimental validation,we identified multiple compounds that target S1 NTD and RBD,which might contribute towards the development of clinical anti-SARS-CoV-2 medicines.Our findings provided a basic foundation for future in vitro and in vivo investigations that might speed up the development of potential therapies for the SARS-CoV-2 va riants. | Qiangzhen Yang Xuemin Jian Ali Alamdar Shah Syed Aamir Fahira Chenxiang Zheng zijia Zhu Ke Wang Jinmai Zhang Yangin Wen Zhiqiang Li Dun Pan Tingting Lu Zhuo Wang Yongyong Shi | 2022 | Research2022，，2： | 2 |
| 2 | Structural Analysis of the SARS-CoV-2 Omicron Variant Proteins显示文摘The spread of the latest SARS-CoV-2 variant Omicron is particularly concerning because of the large number of mutations present in its genome and lack of knowledge about how these mutations would affect the current SARS-CoV-2 vaccines and treatments.Here,by performing phylogenetic analysis using the Omicron spike(S)protein sequence,we found that the Omicron S protein presented the longest evolutionary distance in relation to the other SARS-CoV-2 variants.We predicted the structures of S,M,and N proteins of the Omicron variant using AlphaFold2 and investigated how the mutations have affected the S protein and its parts,S1 NTD and RBD,in detail.We found many amino acids on RBD were mutated,which may influence the interactions between the RBD and ACE2,while also showing the S309 antibody could still be capable of neutralizing Omicron RBD.The Omicron S1 NTD structures display significant differences from the original strain,which could lead to reduced recognition by antibodies resulting in potential immune escape and decreased effectiveness of the existing vaccines.However,this study of the Omicron variant was mainly limited to structural predictions,and these findings should be explored and verified by subsequent experiments.This study provided basic data of the Omicron protein structures that lay the groundwork for future studies related to the SARS-CoV-2 Omicron variant. | Qiangzhen Yang Ali Alamdar Shah Syed Aamir Fahira Yongyong Shi | 2021 | Research2021，，1： | 1 |
| 3 | Structural Analysis of the SARS-CoV-2 Omicron Variant Proteins显示文摘The spread of the latest SARS-CoV-2 variant Omicron is particularly concerning because of the large number of mutations present in its genome and lack of knowledge about how these mutations would affect the current SARS-CoV-2 vaccines and treatments.Here,by performing phylogenetic analysis using the Omicron spike(S)protein sequence,we found that the Omicron Sprotein presented thelongest evolutionary distance in relation totheother SARS-CoV-2variants.We predicted the structures of S,M,and N proteins of the Omicron variant using AlphaFold2 and investigated how the mutations have affected the S protein and its parts,SI NTD and RBD,in detail.We found many amino acids on RBD were mutated,which may infuence the interactions between the RBD and ACE2,while also showing the S309 antibody could stllbe capable of neutralizing Omicron RBD.The Omicron SI NTD structures display significant differences from the original strain,which could lead toreduced recognition by antibodies resulting in potential immune escape and decreased efectiveness ofthe existing vaccines.However,this study of the Omicron variant was mainly limited to structural predictions,and these findings should be explored and verifed by subsequent experiments.This study provided basic data of the Omicron protein structures that lay the groundwork for future studies related to the SARS-CoV-2 Omicron variant. | Qiangzhen Yang AliAlamdar Shah Syed amir Fahira Yongyong Shi | 2022 | Research2022，，2： | 0 |
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