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10.1111/eva.12980 http://scihub22266oqcxt.onion/10.1111/eva.12980 C7262083!7262083!32837536     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 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       Evol+Appl 2020 ; 13 (9): 2168-78 Nephropedia Template TP {{tp|p=32837536|t=2020. SARS?CoV?2, an evolutionary perspective of interaction with human ACE2 reveals undiscovered amino acids necessary for complex stability |pdf=|usr=}}{{32837536}} gab.com Text SARS CoV 2, an evolutionary perspective of interaction with human ACE2 reveals undiscovered amino acids necessary for complex stability JO: Evol Appl http://www.kidney.de/pget.php?&tw=1&pmid=32837536 #FOAvip The emergence of SARS?CoV?2 has resulted in nearly 1,280,000 infections and 73,000 deaths globally so far. This novel virus acquired the ability to infect human cells using the SARS?CoV cell receptor hACE2. Because of this, it is essential to improve our understanding of the evolutionary dynamics surrounding the SARS?CoV?2 hACE2 interaction. One way theory predicts selection pressures should shape viral evolution is to enhance binding with host cells. We first assessed evolutionary dynamics in select betacoronavirus spike protein genes to predict whether these genomic regions are under directional or purifying selection between divergent viral lineages, at various scales of relatedness. With this analysis, we determine a region inside the receptor?binding domain with putative sites under positive selection interspersed among highly conserved sites, which are implicated in structural stability of the viral spike protein and its union with human receptor ACE2. Next, to gain further insights into factors associated with recognition of the human host receptor, we performed modeling studies of five different betacoronaviruses and their potential binding to hACE2. Modeling results indicate that interfering with the salt bridges at hot spot 353 could be an effective strategy for inhibiting binding, and hence for the prevention of SARS?CoV?2 infections. We also propose that a glycine residue at the receptor?binding domain of the spike glycoprotein can have a critical role in permitting bat SARS?related coronaviruses to infect human cells. Twit Text FOAVip SARS CoV 2, an evolutionary perspective of interaction with human ACE2 reveals undiscovered amino acids necessary for complex stability ????Evol Appl http://www.kidney.de/pget.php?&tw=1&pmid=32837536 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32837536 #FOAvip English Wikipedia <ref>{{Cite pmid|32837536}}</ref> SARS?CoV?2, an evolutionary perspective of interaction with human ACE2 reveals undiscovered amino acids necessary for complex stability #MMPMID32837536 Armijos?Jaramillo V; Yeager J; Muslin C; Perez?Castillo Y Evol Appl 2020[Oct]; 13 (9): 2168-78 PMID32837536show ga The emergence of SARS?CoV?2 has resulted in nearly 1,280,000 infections and 73,000 deaths globally so far. This novel virus acquired the ability to infect human cells using the SARS?CoV cell receptor hACE2. Because of this, it is essential to improve our understanding of the evolutionary dynamics surrounding the SARS?CoV?2 hACE2 interaction. One way theory predicts selection pressures should shape viral evolution is to enhance binding with host cells. We first assessed evolutionary dynamics in select betacoronavirus spike protein genes to predict whether these genomic regions are under directional or purifying selection between divergent viral lineages, at various scales of relatedness. With this analysis, we determine a region inside the receptor?binding domain with putative sites under positive selection interspersed among highly conserved sites, which are implicated in structural stability of the viral spike protein and its union with human receptor ACE2. Next, to gain further insights into factors associated with recognition of the human host receptor, we performed modeling studies of five different betacoronaviruses and their potential binding to hACE2. Modeling results indicate that interfering with the salt bridges at hot spot 353 could be an effective strategy for inhibiting binding, and hence for the prevention of SARS?CoV?2 infections. We also propose that a glycine residue at the receptor?binding domain of the spike glycoprotein can have a critical role in permitting bat SARS?related coronaviruses to infect human cells. äSARS?CoV?2, an evolutionary perspective of interaction with human ACE2(epmc).pdf DeepDyve Pubget Overpricing