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  • The atomic portrait of SARS-CoV-2 as captured by cryo-electron microscopy #MMPMID34904376
  • Fertig TE; Chitoiu L; Terinte-Balcan G; Peteu VE; Marta D; Gherghiceanu M
  • J Cell Mol Med 2022[Jan]; 26 (1): 25-34 PMID34904376show ga
  • Transmission electron microscopy has historically been indispensable for virology research, as it offers unique insight into virus function. In the past decade, as cryo-electron microscopy (cryo-EM) has matured and become more accessible, we have been able to peer into the structure of viruses at the atomic level and understand how they interact with the host cell, with drugs or with antibodies. Perhaps, there was no time in recent history where cryo-EM was more needed, as SARS-CoV-2 has spread around the globe, causing millions of deaths and almost unquantifiable economic devastation. In this concise review, we aim to mark the most important contributions of cryo-EM to understanding the structure and function of SARS-CoV-2 proteins, from surface spikes to the virus core and from virus-receptor interactions to antibody binding.
  • |Angiotensin-Converting Enzyme 2/*chemistry/immunology/metabolism[MESH]
  • |Antibodies, Viral/biosynthesis/*chemistry[MESH]
  • |COVID-19 Vaccines/administration & dosage/biosynthesis/*chemistry[MESH]
  • |COVID-19/immunology/*prevention & control/virology[MESH]
  • |Cryoelectron Microscopy[MESH]
  • |Epitopes/chemistry/immunology/metabolism[MESH]
  • |Humans[MESH]
  • |Models, Molecular[MESH]
  • |Protein Binding[MESH]
  • |Protein Interaction Domains and Motifs[MESH]
  • |Protein Structure, Secondary[MESH]
  • |Receptors, Virus/*chemistry/immunology/metabolism[MESH]
  • |SARS-CoV-2/drug effects/pathogenicity/ultrastructure[MESH]
  • |Serine Endopeptidases/chemistry/immunology/metabolism[MESH]
  • |Spike Glycoprotein, Coronavirus/*chemistry/immunology/metabolism[MESH]
  • |Virion/drug effects/pathogenicity/ultrastructure[MESH]

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  • suck abstract from ncbi

    25 1.26 2022