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10.1016/j.jinorgbio.2021.111423

http://scihub22266oqcxt.onion/10.1016/j.jinorgbio.2021.111423
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33813307!7955571!33813307
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suck abstract from ncbi


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pmid33813307      J+Inorg+Biochem 2021 ; 219 (ä): 111423
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  • A SARS-CoV-2 -human metalloproteome interaction map #MMPMID33813307
  • Chasapis CT; Georgiopoulou AK; Perlepes SP; Bjorklund G; Peana M
  • J Inorg Biochem 2021[Jun]; 219 (ä): 111423 PMID33813307show ga
  • The recent pandemic caused by the novel coronavirus resulted in the greatest global health crisis since the Spanish flu pandemic of 1918. There is limited knowledge of whether SARS-CoV-2 is physically associated with human metalloproteins. Recently, high-confidence, experimentally supported protein-protein interactions between SARS-CoV-2 and human proteins were reported. In this work, 58 metalloproteins among these human targets have been identified by a structure-based approach. This study reveals that most human metalloproteins interact with the recently discovered SARS-CoV-2 orf8 protein, whose antibodies are one of the principal markers of SARS-CoV-2 infections. Furthermore, this work provides sufficient evidence to conclude that Zn(2+) plays an important role in the interplay between the novel coronavirus and humans. First, the content of Zn-binding proteins in the involved human metalloproteome is significantly higher than that of the other metal ions. Second, a molecular linkage between the identified human Zn-binding proteome with underlying medical conditions, that might increase the risk of severe illness from the SARS-CoV-2 virus, has been found. Likely perturbations of host cellular metal homeostasis by SARS-CoV-2 infection are highlighted.
  • |COVID-19/metabolism[MESH]
  • |Carrier Proteins/metabolism[MESH]
  • |Host-Pathogen Interactions/*physiology[MESH]
  • |Humans[MESH]
  • |Metalloproteins/genetics/*metabolism[MESH]
  • |Nervous System Diseases/*genetics[MESH]
  • |SARS-CoV-2/metabolism/*pathogenicity[MESH]


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