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10.1016/j.cell.2020.09.018

http://scihub22266oqcxt.onion/10.1016/j.cell.2020.09.018
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32979942!7474903!32979942
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suck abstract from ncbi

pmid32979942      Cell 2020 ; 183 (3): 730-738.e13
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  • Molecular Architecture of the SARS-CoV-2 Virus #MMPMID32979942
  • Yao H; Song Y; Chen Y; Wu N; Xu J; Sun C; Zhang J; Weng T; Zhang Z; Wu Z; Cheng L; Shi D; Lu X; Lei J; Crispin M; Shi Y; Li L; Li S
  • Cell 2020[Oct]; 183 (3): 730-738.e13 PMID32979942show ga
  • SARS-CoV-2 is an enveloped virus responsible for the COVID-19 pandemic. Despite recent advances in the structural elucidation of SARS-CoV-2 proteins, the detailed architecture of the intact virus remains to be unveiled. Here we report the molecular assembly of the authentic SARS-CoV-2 virus using cryoelectron tomography (cryo-ET) and subtomogram averaging (STA). Native structures of the S proteins in pre- and postfusion conformations were determined to average resolutions of 8.7-11 A. Compositions of the N-linked glycans from the native spikes were analyzed by mass spectrometry, which revealed overall processing states of the native glycans highly similar to that of the recombinant glycoprotein glycans. The native conformation of the ribonucleoproteins (RNPs) and their higher-order assemblies were revealed. Overall, these characterizations revealed the architecture of the SARS-CoV-2 virus in exceptional detail and shed light on how the virus packs its approximately 30-kb-long single-segmented RNA in the approximately 80-nm-diameter lumen.
  • |*Virus Assembly[MESH]
  • |Animals[MESH]
  • |Betacoronavirus/*physiology/*ultrastructure[MESH]
  • |Chlorocebus aethiops[MESH]
  • |Cryoelectron Microscopy[MESH]
  • |Humans[MESH]
  • |Mass Spectrometry[MESH]
  • |Models, Molecular[MESH]
  • |Protein Conformation[MESH]
  • |SARS-CoV-2[MESH]
  • |Vero Cells[MESH]
  • |Viral Proteins/chemistry/ultrastructure[MESH]


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  • suck abstract from ncbi

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