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10.1109/MCSE.2020.3015511 http://scihub22266oqcxt.onion/10.1109/MCSE.2020.3015511 33762895!7983027!33762895     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Comput+Sci+Eng 2020 ; 22 (6): 21-29 Nephropedia Template TP {{tp|p=33762895|t=2020. Revealing the mechanism of SARS-CoV-2 spike protein binding with ACE2 |pdf=|usr=}}{{33762895}} gab.com Text Revealing the mechanism of SARS-CoV-2 spike protein binding with ACE2 JO: Comput Sci Eng http://www.kidney.de/pget.php?&tw=1&pmid=33762895 #FOAvip A large population in the world has been infected by COVID-19. Understanding the mechanisms of Severe Acute Respiratory Syndrome CoronaVirus 2 (SARS-CoV-2) is important for management and treatment of the COVID-19. When it comes to the infection process, one of the most important proteins in SARS-CoV-2 is the spike (S) protein, which is able to bind to human Angiotensin-Converting Enzyme 2 (ACE2) and initializes the entry of the host cell. In this study, we implemented multi-scale computational approaches to study the electrostatic features of the interfaces of the SARS-CoV-2 S protein Receptor Binding Domain (RBD) and ACE2. The simulations and analyses were performed on high-performance computing resources in Texas Advanced Computing Center (TACC). Our study identified key residues on the SARS-CoV-2, which can be used as targets for future drug design. The results shed lights on future drug design and therapeutic targets for COVID-19. Twit Text FOAVip Revealing the mechanism of SARS-CoV-2 spike protein binding with ACE2 ????Comput Sci Eng http://www.kidney.de/pget.php?&tw=1&pmid=33762895 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33762895 #FOAvip English Wikipedia <ref>{{Cite pmid|33762895}}</ref> Revealing the mechanism of SARS-CoV-2 spike protein binding with ACE2 #MMPMID33762895 Xie Y; Du D; Karki CB; Guo W; Lopez-Hernandez AE; Sun S; Juarez BY; Li H; Wang J; Li L Comput Sci Eng 2020[Nov]; 22 (6): 21-29 PMID33762895show ga A large population in the world has been infected by COVID-19. Understanding the mechanisms of Severe Acute Respiratory Syndrome CoronaVirus 2 (SARS-CoV-2) is important for management and treatment of the COVID-19. When it comes to the infection process, one of the most important proteins in SARS-CoV-2 is the spike (S) protein, which is able to bind to human Angiotensin-Converting Enzyme 2 (ACE2) and initializes the entry of the host cell. In this study, we implemented multi-scale computational approaches to study the electrostatic features of the interfaces of the SARS-CoV-2 S protein Receptor Binding Domain (RBD) and ACE2. The simulations and analyses were performed on high-performance computing resources in Texas Advanced Computing Center (TACC). Our study identified key residues on the SARS-CoV-2, which can be used as targets for future drug design. The results shed lights on future drug design and therapeutic targets for COVID-19. äRevealing the mechanism of SARS-CoV-2 spike protein binding with ACE2 (epmc).pdf DeepDyve Pubget Overpricing