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10.1371/journal.pone.0251426

http://scihub22266oqcxt.onion/10.1371/journal.pone.0251426
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34038453!8153447!34038453
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suck abstract from ncbi


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pmid34038453      PLoS+One 2021 ; 16 (5): e0251426
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  • Increased elastase sensitivity and decreased intramolecular interactions in the more transmissible 501Y V1 and 501Y V2 SARS-CoV-2 variants spike protein-an in silico analysis #MMPMID34038453
  • Pokhrel S; Kraemer BR; Lee L; Samardzic K; Mochly-Rosen D
  • PLoS One 2021[]; 16 (5): e0251426 PMID34038453show ga
  • Two SARS-CoV-2 variants of concern showing increased transmissibility relative to the Wuhan virus have recently been identified. Although neither variant appears to cause more severe illness nor increased risk of death, the faster spread of the virus is a major threat. Using computational tools, we found that the new SARS-CoV-2 variants may acquire an increased transmissibility by increasing the propensity of its spike protein to expose the receptor binding domain via proteolysis, perhaps by neutrophil elastase and/or via reduced intramolecular interactions that contribute to the stability of the closed conformation of spike protein. This information leads to the identification of potential treatments to avert the imminent threat of these more transmittable SARS-CoV-2 variants.
  • |Amino Acid Sequence[MESH]
  • |Angiotensin-Converting Enzyme 2/chemistry/metabolism[MESH]
  • |Antibodies, Neutralizing/immunology[MESH]
  • |COVID-19/pathology/virology[MESH]
  • |Humans[MESH]
  • |Molecular Dynamics Simulation[MESH]
  • |Mutation[MESH]
  • |Neutrophils/cytology/metabolism[MESH]
  • |Pancreatic Elastase/*metabolism[MESH]
  • |Protein Binding[MESH]
  • |Protein Stability[MESH]
  • |Protein Structure, Tertiary[MESH]
  • |SARS-CoV-2/isolation & purification/*metabolism/pathogenicity[MESH]
  • |Sequence Alignment[MESH]


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  • suck abstract from ncbi

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