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10.1016/j.bbrc.2022.01.038

http://scihub22266oqcxt.onion/10.1016/j.bbrc.2022.01.038
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35063769!8759804!35063769
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suck abstract from ncbi

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  • How tetraspanin-mediated cell entry of SARS-CoV-2 can dysregulate the shedding of the ACE2 receptor by ADAM17 #MMPMID35063769
  • Healy EF
  • Biochem Biophys Res Commun 2022[Feb]; 593 (ä): 52-56 PMID35063769show ga
  • COVID-19, the respiratory infection caused by the novel coronavirus SARS-CoV-2, presents a clinical picture consistent with the dysregulation of many of the pathways mediated by the metalloprotease ADAM17. ADAM17 is a sheddase that plays a key role in the modulation of ACE2, the receptor which also functions as the point of attachment leading to cell entry by the virus. This work investigates the possibility that ADAM17 dysregulation and attachment of the SARS-CoV-2 virion to the ACE2 receptor are linked events, with the latter causing the former. Tetraspanins, the transmembrane proteins that function as scaffolds for the construction of viral entry platforms, are mooted as key components in this connection.
  • |*Virus Internalization[MESH]
  • |ADAM17 Protein/chemistry/*metabolism[MESH]
  • |Angiotensin-Converting Enzyme 2/chemistry/*metabolism[MESH]
  • |Binding Sites[MESH]
  • |COVID-19/epidemiology/transmission/virology[MESH]
  • |Humans[MESH]
  • |Models, Biological[MESH]
  • |Molecular Docking Simulation[MESH]
  • |Multiprotein Complexes/chemistry/metabolism[MESH]
  • |Pandemics[MESH]
  • |Protein Binding[MESH]
  • |Protein Domains[MESH]
  • |Receptors, Virus/chemistry/*metabolism[MESH]
  • |SARS-CoV-2/*metabolism/physiology[MESH]
  • |Tetraspanin 29/chemistry/*metabolism[MESH]


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  • suck abstract from ncbi

    52 ä.593 2022