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10.3389/fnut.2020.00143 http://scihub22266oqcxt.onion/10.3389/fnut.2020.00143 32984400!7492384!32984400     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Front+Nutr 2020 ; 7 (ä): 143 Nephropedia Template TP {{tp|p=32984400|t=2020. Understanding Selenium and Glutathione as Antiviral Factors in COVID-19: Does the Viral M(pro) Protease Target Host Selenoproteins and Glutathione Synthesis?|pdf=|usr=}}{{32984400}} gab.com Text Understanding Selenium and Glutathione as Antiviral Factors in COVID-19: Does the Viral M(pro) Protease Target Host Selenoproteins and Glutathione Synthesis JO: Front Nutr http://www.kidney.de/pget.php?&tw=1&pmid=32984400 #FOAvip Glutathione peroxidases (GPX), a family of antioxidant selenoenzymes, functionally link selenium and glutathione, which both show correlations with clinical outcomes in COVID-19. Thus, it is highly significant that cytosolic GPX1 has been shown to interact with an inactive C145A mutant of M(pro), the main cysteine protease of SARS-CoV-2, but not with catalytically active wild-type M(pro). This seemingly anomalous result is what might be expected if GPX1 is a substrate for the active protease, leading to its fragmentation. We show that the GPX1 active site sequence is substantially similar to a known M(pro) cleavage site, and is identified as a potential cysteine protease site by the Procleave algorithm. Proteolytic knockdown of GPX1 is highly consistent with previously documented effects of recombinant SARS-CoV M(pro) in transfected cells, including increased reactive oxygen species and NF-kappaB activation. Because NF-kappaB in turn activates many pro-inflammatory cytokines, this mechanism could contribute to increased inflammation and cytokine storms observed in COVID-19. Using web-based protease cleavage site prediction tools, we show that M(pro) may be targeting not only GPX1, but several other selenoproteins including SELENOF and thioredoxin reductase 1, as well as glutamate-cysteine ligase, the rate-limiting enzyme for glutathione synthesis. This hypothesized proteolytic knockdown of components of both the thioredoxin and glutaredoxin systems is consistent with a viral strategy to inhibit DNA synthesis, to increase the pool of ribonucleotides for RNA synthesis, thereby enhancing virion production. The resulting "collateral damage" of increased oxidative stress and inflammation would be exacerbated by dietary deficiencies of selenium and glutathione precursors. Twit Text FOAVip Understanding Selenium and Glutathione as Antiviral Factors in COVID-19: Does the Viral M(pro) Protease Target Host Selenoproteins and Glutathione Synthesis ????Front Nutr http://www.kidney.de/pget.php?&tw=1&pmid=32984400 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32984400 #FOAvip English Wikipedia <ref>{{Cite pmid|32984400}}</ref> Understanding Selenium and Glutathione as Antiviral Factors in COVID-19: Does the Viral M(pro) Protease Target Host Selenoproteins and Glutathione Synthesis? #MMPMID32984400 Taylor EW; Radding W Front Nutr 2020[]; 7 (ä): 143 PMID32984400show ga Glutathione peroxidases (GPX), a family of antioxidant selenoenzymes, functionally link selenium and glutathione, which both show correlations with clinical outcomes in COVID-19. Thus, it is highly significant that cytosolic GPX1 has been shown to interact with an inactive C145A mutant of M(pro), the main cysteine protease of SARS-CoV-2, but not with catalytically active wild-type M(pro). This seemingly anomalous result is what might be expected if GPX1 is a substrate for the active protease, leading to its fragmentation. We show that the GPX1 active site sequence is substantially similar to a known M(pro) cleavage site, and is identified as a potential cysteine protease site by the Procleave algorithm. Proteolytic knockdown of GPX1 is highly consistent with previously documented effects of recombinant SARS-CoV M(pro) in transfected cells, including increased reactive oxygen species and NF-kappaB activation. Because NF-kappaB in turn activates many pro-inflammatory cytokines, this mechanism could contribute to increased inflammation and cytokine storms observed in COVID-19. Using web-based protease cleavage site prediction tools, we show that M(pro) may be targeting not only GPX1, but several other selenoproteins including SELENOF and thioredoxin reductase 1, as well as glutamate-cysteine ligase, the rate-limiting enzyme for glutathione synthesis. This hypothesized proteolytic knockdown of components of both the thioredoxin and glutaredoxin systems is consistent with a viral strategy to inhibit DNA synthesis, to increase the pool of ribonucleotides for RNA synthesis, thereby enhancing virion production. The resulting "collateral damage" of increased oxidative stress and inflammation would be exacerbated by dietary deficiencies of selenium and glutathione precursors. äUnderstanding Selenium and Glutathione as Antiviral Factors in COVID-1(epmc).pdf DeepDyve Pubget Overpricing