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10.3390/ijms21155346 http://scihub22266oqcxt.onion/10.3390/ijms21155346 32731361!7432786!32731361     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Int+J+Mol+Sci 2020 ; 21 (15): ä Nephropedia Template TP {{tp|p=32731361|t=2020. Computational Studies of SARS-CoV-2 3CLpro: Insights from MD Simulations |pdf=|usr=}}{{32731361}} gab.com Text Computational Studies of SARS-CoV-2 3CLpro: Insights from MD Simulations JO: Int J Mol Sci http://www.kidney.de/pget.php?&tw=1&pmid=32731361 #FOAvip Given the enormous social and health impact of the pandemic triggered by severe acute respiratory syndrome 2 (SARS-CoV-2), the scientific community made a huge effort to provide an immediate response to the challenges posed by Coronavirus disease 2019 (COVID-19). One of the most important proteins of the virus is an enzyme, called 3CLpro or main protease, already identified as an important pharmacological target also in SARS and Middle East respiratory syndrome virus (MERS) viruses. This protein triggers the production of a whole series of enzymes necessary for the virus to carry out its replicating and infectious activities. Therefore, it is crucial to gain a deeper understanding of 3CLpro structure and function in order to effectively target this enzyme. All-atoms molecular dynamics (MD) simulations were performed to examine the different conformational behaviors of the monomeric and dimeric form of SARS-CoV-2 3CLpro apo structure, as revealed by microsecond time scale MD simulations. Our results also shed light on the conformational dynamics of the loop regions at the entry of the catalytic site. Studying, at atomic level, the characteristics of the active site and obtaining information on how the protein can interact with its substrates will allow the design of molecules able to block the enzymatic function crucial for the virus. Twit Text FOAVip Computational Studies of SARS-CoV-2 3CLpro: Insights from MD Simulations ????Int J Mol Sci http://www.kidney.de/pget.php?&tw=1&pmid=32731361 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32731361 #FOAvip English Wikipedia <ref>{{Cite pmid|32731361}}</ref> Computational Studies of SARS-CoV-2 3CLpro: Insights from MD Simulations #MMPMID32731361 Grottesi A; Besker N; Emerson A; Manelfi C; Beccari AR; Frigerio F; Lindahl E; Cerchia C; Talarico C Int J Mol Sci 2020[Jul]; 21 (15): ä PMID32731361show ga Given the enormous social and health impact of the pandemic triggered by severe acute respiratory syndrome 2 (SARS-CoV-2), the scientific community made a huge effort to provide an immediate response to the challenges posed by Coronavirus disease 2019 (COVID-19). One of the most important proteins of the virus is an enzyme, called 3CLpro or main protease, already identified as an important pharmacological target also in SARS and Middle East respiratory syndrome virus (MERS) viruses. This protein triggers the production of a whole series of enzymes necessary for the virus to carry out its replicating and infectious activities. Therefore, it is crucial to gain a deeper understanding of 3CLpro structure and function in order to effectively target this enzyme. All-atoms molecular dynamics (MD) simulations were performed to examine the different conformational behaviors of the monomeric and dimeric form of SARS-CoV-2 3CLpro apo structure, as revealed by microsecond time scale MD simulations. Our results also shed light on the conformational dynamics of the loop regions at the entry of the catalytic site. Studying, at atomic level, the characteristics of the active site and obtaining information on how the protein can interact with its substrates will allow the design of molecules able to block the enzymatic function crucial for the virus. |Betacoronavirus/chemistry/*metabolism[MESH] |Catalytic Domain[MESH] |Coronavirus 3C Proteases[MESH] |Cysteine Endopeptidases/*chemistry/*metabolism[MESH] |Humans[MESH] |Models, Molecular[MESH] |Molecular Dynamics Simulation[MESH] |Protein Binding[MESH] |Protein Conformation[MESH] |Protein Multimerization[MESH] |SARS-CoV-2[MESH]Computational Studies of SARS-CoV-2 3CLpro: Insights from MD Simulatio(epmc).pdf DeepDyve Pubget Overpricing