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10.3390/molecules25112529 http://scihub22266oqcxt.onion/10.3390/molecules25112529 32485894!7321236!32485894     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       Molecules 2020 ; 25 (11): ä Nephropedia Template TP {{tp|p=32485894|t=2020. In Silico Evaluation of the Effectivity of Approved Protease Inhibitors against the Main Protease of the Novel SARS-CoV-2 Virus |pdf=|usr=}}{{32485894}} gab.com Text In Silico Evaluation of the Effectivity of Approved Protease Inhibitors against the Main Protease of the Novel SARS-CoV-2 Virus JO: Molecules http://www.kidney.de/pget.php?&tw=1&pmid=32485894 #FOAvip The coronavirus disease, COVID-19, caused by the novel coronavirus SARS-CoV-2, which first emerged in Wuhan, China and was made known to the World in December 2019 turned into a pandemic causing more than 126,124 deaths worldwide up to April 16th, 2020. It has 79.5% sequence identity with SARS-CoV-1 and the same strategy for host cell invasion through the ACE-2 surface protein. Since the development of novel drugs is a long-lasting process, researchers look for effective substances among drugs already approved or developed for other purposes. The 3D structure of the SARS-CoV-2 main protease was compared with the 3D structures of seven proteases, which are drug targets, and docking analysis to the SARS-CoV-2 protease structure of thirty four approved and on-trial protease inhibitors was performed. Increased 3D structural similarity between the SARS-CoV-2 main protease, the HCV protease and alpha-thrombin was found. According to docking analysis the most promising results were found for HCV protease, DPP-4, alpha-thrombin and coagulation Factor Xa known inhibitors, with several of them exhibiting estimated free binding energy lower than -8.00 kcal/mol and better prediction results than reference compounds. Since some of the compounds are well-tolerated drugs, the promising in silico results may warrant further evaluation for viral anticipation. DPP-4 inhibitors with anti-viral action may be more useful for infected patients with diabetes, while anti-coagulant treatment is proposed in severe SARS-CoV-2 induced pneumonia. Twit Text FOAVip In Silico Evaluation of the Effectivity of Approved Protease Inhibitors against the Main Protease of the Novel SARS-CoV-2 Virus ????Molecules http://www.kidney.de/pget.php?&tw=1&pmid=32485894 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32485894 #FOAvip English Wikipedia <ref>{{Cite pmid|32485894}}</ref> In Silico Evaluation of the Effectivity of Approved Protease Inhibitors against the Main Protease of the Novel SARS-CoV-2 Virus #MMPMID32485894 Eleftheriou P; Amanatidou D; Petrou A; Geronikaki A Molecules 2020[May]; 25 (11): ä PMID32485894show ga The coronavirus disease, COVID-19, caused by the novel coronavirus SARS-CoV-2, which first emerged in Wuhan, China and was made known to the World in December 2019 turned into a pandemic causing more than 126,124 deaths worldwide up to April 16th, 2020. It has 79.5% sequence identity with SARS-CoV-1 and the same strategy for host cell invasion through the ACE-2 surface protein. Since the development of novel drugs is a long-lasting process, researchers look for effective substances among drugs already approved or developed for other purposes. The 3D structure of the SARS-CoV-2 main protease was compared with the 3D structures of seven proteases, which are drug targets, and docking analysis to the SARS-CoV-2 protease structure of thirty four approved and on-trial protease inhibitors was performed. Increased 3D structural similarity between the SARS-CoV-2 main protease, the HCV protease and alpha-thrombin was found. According to docking analysis the most promising results were found for HCV protease, DPP-4, alpha-thrombin and coagulation Factor Xa known inhibitors, with several of them exhibiting estimated free binding energy lower than -8.00 kcal/mol and better prediction results than reference compounds. Since some of the compounds are well-tolerated drugs, the promising in silico results may warrant further evaluation for viral anticipation. DPP-4 inhibitors with anti-viral action may be more useful for infected patients with diabetes, while anti-coagulant treatment is proposed in severe SARS-CoV-2 induced pneumonia. |Amino Acid Sequence[MESH] |Anticoagulants/*chemistry/pharmacology[MESH] |Antiviral Agents/*chemistry/pharmacology[MESH] |Betacoronavirus/chemistry/*drug effects/enzymology/genetics[MESH] |Binding Sites[MESH] |COVID-19[MESH] |Coronavirus 3C Proteases[MESH] |Coronavirus Infections/drug therapy[MESH] |Cysteine Endopeptidases/chemistry/genetics/metabolism[MESH] |Dipeptidyl Peptidase 4/chemistry/genetics/metabolism[MESH] |Dipeptidyl-Peptidase IV Inhibitors/*chemistry/pharmacology[MESH] |Factor Xa/chemistry/genetics/metabolism[MESH] |Hepacivirus/chemistry/enzymology/genetics[MESH] |Humans[MESH] |Molecular Docking Simulation[MESH] |Pandemics[MESH] |Pneumonia, Viral/drug therapy[MESH] |Protease Inhibitors/*chemistry/pharmacology[MESH] |Protein Binding[MESH] |Protein Conformation[MESH] |Protein Interaction Domains and Motifs[MESH] |SARS-CoV-2[MESH] |Sequence Alignment[MESH] |Structural Homology, Protein[MESH] |Substrate Specificity[MESH] |Thermodynamics[MESH] |Thrombin/antagonists & inhibitors/chemistry/genetics/metabolism[MESH]In Silico Evaluation of the Effectivity of Approved Protease Inhibitor(epmc).pdf DeepDyve Pubget Overpricing