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10.1016/j.lfs.2020.118056

http://scihub22266oqcxt.onion/10.1016/j.lfs.2020.118056
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32645344!7336130!32645344
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suck abstract from ncbi


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pmid32645344      Life+Sci 2020 ; 257 (ä): 118056
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  • Structural features of coronavirus SARS-CoV-2 spike protein: Targets for vaccination #MMPMID32645344
  • Sternberg A; Naujokat C
  • Life Sci 2020[Sep]; 257 (ä): 118056 PMID32645344show ga
  • Various human pathogenic viruses employ envelope glycoproteins for host cell receptor recognition and binding, membrane fusion and viral entry. The spike (S) glycoprotein of betacoronavirus SARS-CoV-2 is a homotrimeric class I fusion protein that exists in a metastable conformation for cleavage by host cell proteases furin and TMPRSS2, thereby undergoing substantial structural rearrangement for ACE2 host cell receptor binding and subsequent viral entry by membrane fusion. The S protein is densely decorated with N-linked glycans protruding from the trimer surface that affect S protein folding, processing by host cell proteases and the elicitation of humoral immune response. Deep insight into the sophisticated structure of SARS-CoV-2 S protein may provide a blueprint for vaccination strategies, as reviewed herein.
  • |Angiotensin-Converting Enzyme 2[MESH]
  • |Betacoronavirus/immunology/pathogenicity[MESH]
  • |COVID-19[MESH]
  • |Coronavirus Infections/*drug therapy/*immunology/pathology/prevention & control[MESH]
  • |Humans[MESH]
  • |Pandemics/prevention & control[MESH]
  • |Peptidyl-Dipeptidase A/metabolism[MESH]
  • |Pneumonia, Viral/*drug therapy/*immunology/pathology/prevention & control[MESH]
  • |Protein Binding[MESH]
  • |Receptors, Virus/metabolism[MESH]
  • |SARS-CoV-2[MESH]
  • |Spike Glycoprotein, Coronavirus/chemistry/*immunology/metabolism[MESH]
  • |Vaccination/methods[MESH]


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