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10.1021/acs.jpcb.1c04871 http://scihub22266oqcxt.onion/10.1021/acs.jpcb.1c04871 34370466!8369982!34370466     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Phys+Chem+B 2021 ; 125 (32): 9155-9167 Nephropedia Template TP {{tp|p=34370466|t=2021. Presence of a SARS-CoV-2 Protein Enhances Amyloid Formation of Serum Amyloid A |pdf=|usr=}}{{34370466}} gab.com Text Presence of a SARS-CoV-2 Protein Enhances Amyloid Formation of Serum Amyloid A JO: J Phys Chem B http://www.kidney.de/pget.php?&tw=1&pmid=34370466 #FOAvip A marker for the severeness and disease progress of COVID-19 is overexpression of serum amyloid A (SAA) to levels that in other diseases are associated with a risk for SAA amyloidosis. To understand whether SAA amyloidosis could also be a long-term risk of SARS-CoV-2 infections, we have used long all-atom molecular dynamic simulations to study the effect of a SARS-CoV-2 protein segment on SAA amyloid formation. Sampling over 40 mus, we find that the presence of the nine-residue segment SK9, located at the C-terminus of the envelope protein, increases the propensity for SAA fibril formation by three mechanisms: it reduces the stability of the lipid-transporting hexamer shifting the equilibrium toward monomers, it increases the frequency of aggregation-prone configurations in the resulting chains, and it raises the stability of SAA fibrils. Our results therefore suggest that SAA amyloidosis and related pathologies may be a long-term risk of SARS-CoV-2 infections. Twit Text FOAVip Presence of a SARS-CoV-2 Protein Enhances Amyloid Formation of Serum Amyloid A ????J Phys Chem B http://www.kidney.de/pget.php?&tw=1&pmid=34370466 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34370466 #FOAvip English Wikipedia <ref>{{Cite pmid|34370466}}</ref> Presence of a SARS-CoV-2 Protein Enhances Amyloid Formation of Serum Amyloid A #MMPMID34370466 Jana AK; Greenwood AB; Hansmann UHE J Phys Chem B 2021[Aug]; 125 (32): 9155-9167 PMID34370466show ga A marker for the severeness and disease progress of COVID-19 is overexpression of serum amyloid A (SAA) to levels that in other diseases are associated with a risk for SAA amyloidosis. To understand whether SAA amyloidosis could also be a long-term risk of SARS-CoV-2 infections, we have used long all-atom molecular dynamic simulations to study the effect of a SARS-CoV-2 protein segment on SAA amyloid formation. Sampling over 40 mus, we find that the presence of the nine-residue segment SK9, located at the C-terminus of the envelope protein, increases the propensity for SAA fibril formation by three mechanisms: it reduces the stability of the lipid-transporting hexamer shifting the equilibrium toward monomers, it increases the frequency of aggregation-prone configurations in the resulting chains, and it raises the stability of SAA fibrils. Our results therefore suggest that SAA amyloidosis and related pathologies may be a long-term risk of SARS-CoV-2 infections. |*Amyloidosis[MESH] |*COVID-19[MESH] |Amyloid[MESH] |Humans[MESH] |SARS-CoV-2[MESH]Presence of a SARS-CoV-2 Protein Enhances Amyloid Formation of Serum A(epmc).pdf DeepDyve Pubget Overpricing