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10.1038/s41594-020-00547-5

http://scihub22266oqcxt.onion/10.1038/s41594-020-00547-5
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33402708!7878407!33402708
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suck abstract from ncbi

pmid33402708      Nat+Struct+Mol+Biol 2021 ; 28 (2): 128-131
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  • Cold sensitivity of the SARS-CoV-2 spike ectodomain #MMPMID33402708
  • Edwards RJ; Mansouri K; Stalls V; Manne K; Watts B; Parks R; Janowska K; Gobeil SMC; Kopp M; Li D; Lu X; Mu Z; Deyton M; Oguin TH 3rd; Sprenz J; Williams W; Saunders KO; Montefiori D; Sempowski GD; Henderson R; Munir Alam S; Haynes BF; Acharya P
  • Nat Struct Mol Biol 2021[Feb]; 28 (2): 128-131 PMID33402708show ga
  • The SARS-CoV-2 spike (S) protein, a primary target for COVID-19 vaccine development, presents its receptor binding domain in two conformations, the receptor-accessible 'up' or receptor-inaccessible 'down' states. Here we report that the commonly used stabilized S ectodomain construct '2P' is sensitive to cold temperatures, and this cold sensitivity is abrogated in a 'down' state-stabilized ectodomain. Our findings will impact structural, functional and vaccine studies that use the SARS-CoV-2 S ectodomain.
  • |Antibodies, Viral/chemistry[MESH]
  • |COVID-19 Vaccines/chemistry[MESH]
  • |Cold Temperature[MESH]
  • |Cryoelectron Microscopy[MESH]
  • |Enzyme-Linked Immunosorbent Assay[MESH]
  • |Humans[MESH]
  • |Protein Denaturation[MESH]
  • |Protein Domains[MESH]
  • |Protein Stability[MESH]
  • |Spike Glycoprotein, Coronavirus/*chemistry/ultrastructure[MESH]


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