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10.1016/j.bbrc.2021.03.100

http://scihub22266oqcxt.onion/10.1016/j.bbrc.2021.03.100
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33789211!7988450!33789211
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suck abstract from ncbi


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pmid33789211      Biochem+Biophys+Res+Commun 2021 ; 554 (ä): 94-98
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  • SARS-CoV-2 spike protein interactions with amyloidogenic proteins: Potential clues to neurodegeneration #MMPMID33789211
  • Idrees D; Kumar V
  • Biochem Biophys Res Commun 2021[May]; 554 (ä): 94-98 PMID33789211show ga
  • The post-infection of COVID-19 includes a myriad of neurologic symptoms including neurodegeneration. Protein aggregation in brain can be considered as one of the important reasons behind the neurodegeneration. SARS-CoV-2 Spike S1 protein receptor binding domain (SARS-CoV-2 S1 RBD) binds to heparin and heparin binding proteins. Moreover, heparin binding accelerates the aggregation of the pathological amyloid proteins present in the brain. In this paper, we have shown that the SARS-CoV-2 S1 RBD binds to a number of aggregation-prone, heparin binding proteins including Abeta, alpha-synuclein, tau, prion, and TDP-43 RRM. These interactions suggests that the heparin-binding site on the S1 protein might assist the binding of amyloid proteins to the viral surface and thus could initiate aggregation of these proteins and finally leads to neurodegeneration in brain. The results will help us to prevent future outcomes of neurodegeneration by targeting this binding and aggregation process.
  • |*Protein Aggregation, Pathological[MESH]
  • |Amyloid beta-Peptides/metabolism[MESH]
  • |Amyloid/*metabolism[MESH]
  • |Brain/metabolism/pathology/virology[MESH]
  • |COVID-19/*metabolism/virology[MESH]
  • |DNA-Binding Proteins/chemistry/metabolism[MESH]
  • |Heparin/*metabolism[MESH]
  • |Humans[MESH]
  • |Molecular Docking Simulation[MESH]
  • |Neurodegenerative Diseases/*metabolism/virology[MESH]
  • |Prions/metabolism[MESH]
  • |Protein Binding[MESH]
  • |SARS-CoV-2/chemistry/metabolism/*pathogenicity[MESH]
  • |Spike Glycoprotein, Coronavirus/chemistry/*metabolism[MESH]
  • |alpha-Synuclein/metabolism[MESH]


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