Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1002/ardp.202100160 http://scihub22266oqcxt.onion/10.1002/ardp.202100160 34427335!8646807!34427335     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       Arch+Pharm+(Weinheim) 2021 ; 354 (11): e2100160 Nephropedia Template TP {{tp|p=34427335|t=2021. Binding of boswellic acids to functional proteins of the SARS-CoV-2 virus: Bioinformatic studies |pdf=|usr=}}{{34427335}} gab.com Text Binding of boswellic acids to functional proteins of the SARS-CoV-2 virus: Bioinformatic studies JO: Arch Pharm (Weinheim) http://www.kidney.de/pget.php?&tw=1&pmid=34427335 #FOAvip Boswellic acids (BAs) have been shown to possess antiviral activity. Using bioinformatic methods, it was tested whether or not acetyl-11-keto-beta-boswellic acid (AKBA), 11-keto-beta-boswellic acid (KBA), beta-boswellic acid (BBA), and the phosphorylated active metabolite of Remdesivir(R) (RGS-P3) bind to functional proteins of SARS-CoV-2, that is, the replicase polyprotein P0DTD1, the spike glycoprotein P0DTC2, and the nucleoprotein P0DTC9. Using P0DTD1, AKBA and KBA showed micromolar binding affinity to the RNA-dependent RNA polymerase (RdRp) and to the main proteinase complex M(pro) . Phosphorylated BAs even bond in the nanomolar range. Due to their positive and negative charges, BAs and RGS-P3 bond to corresponding negative and positive areas of the protein. BAs and RGS-P3 docked in the tunnel-like cavity of RdRp. BAs also docked into the elongated surface rim of viral M(pro) . In both cases, binding occurred with active site amino acids in the lower micromolecular to upper nanomolar range. KBA, BBA, and RGS-P3 also bond to P0DTC2 and P0DTC9. The binding energies for BAs were in the range of -5.8 to -6.3 kcal/mol. RGS-P3 and BAs occluded the centrally located pore of the donut-like protein structure of P0DTC9 and, in the case of P0DTC2, RGS-P3 and BAs impacted the double-wing-like protein structure. The data of this bioinformatics study clearly show that BAs bind to three functional proteins of the SARS-CoV-2 virus responsible for adhesion and replication, as does RGS-P3, a drug on the market to treat this disease. The binding effectiveness of BAs can be increased through phosphate esterification. Whether or not BAs are druggable against the SARS-CoV-2 disease remains to be established. Twit Text FOAVip Binding of boswellic acids to functional proteins of the SARS-CoV-2 virus: Bioinformatic studies ????Arch Pharm (Weinheim) http://www.kidney.de/pget.php?&tw=1&pmid=34427335 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34427335 #FOAvip English Wikipedia <ref>{{Cite pmid|34427335}}</ref> Binding of boswellic acids to functional proteins of the SARS-CoV-2 virus: Bioinformatic studies #MMPMID34427335 Caliebe RH; Scior T; Ammon HPT Arch Pharm (Weinheim) 2021[Nov]; 354 (11): e2100160 PMID34427335show ga Boswellic acids (BAs) have been shown to possess antiviral activity. Using bioinformatic methods, it was tested whether or not acetyl-11-keto-beta-boswellic acid (AKBA), 11-keto-beta-boswellic acid (KBA), beta-boswellic acid (BBA), and the phosphorylated active metabolite of Remdesivir(R) (RGS-P3) bind to functional proteins of SARS-CoV-2, that is, the replicase polyprotein P0DTD1, the spike glycoprotein P0DTC2, and the nucleoprotein P0DTC9. Using P0DTD1, AKBA and KBA showed micromolar binding affinity to the RNA-dependent RNA polymerase (RdRp) and to the main proteinase complex M(pro) . Phosphorylated BAs even bond in the nanomolar range. Due to their positive and negative charges, BAs and RGS-P3 bond to corresponding negative and positive areas of the protein. BAs and RGS-P3 docked in the tunnel-like cavity of RdRp. BAs also docked into the elongated surface rim of viral M(pro) . In both cases, binding occurred with active site amino acids in the lower micromolecular to upper nanomolar range. KBA, BBA, and RGS-P3 also bond to P0DTC2 and P0DTC9. The binding energies for BAs were in the range of -5.8 to -6.3 kcal/mol. RGS-P3 and BAs occluded the centrally located pore of the donut-like protein structure of P0DTC9 and, in the case of P0DTC2, RGS-P3 and BAs impacted the double-wing-like protein structure. The data of this bioinformatics study clearly show that BAs bind to three functional proteins of the SARS-CoV-2 virus responsible for adhesion and replication, as does RGS-P3, a drug on the market to treat this disease. The binding effectiveness of BAs can be increased through phosphate esterification. Whether or not BAs are druggable against the SARS-CoV-2 disease remains to be established. |*COVID-19 Drug Treatment[MESH] |*COVID-19/virology[MESH] |*SARS-CoV-2/drug effects/physiology[MESH] |Adenosine Monophosphate/*analogs & derivatives/pharmacology[MESH] |Alanine/*analogs & derivatives/pharmacology[MESH] |Anti-Inflammatory Agents, Non-Steroidal/pharmacology[MESH] |Antiviral Agents/pharmacology[MESH] |Binding Sites/physiology[MESH] |Boswellia[MESH] |Computational Biology/methods[MESH] |Humans[MESH] |Molecular Docking Simulation[MESH] |Nucleoproteins/metabolism[MESH] |Polyproteins/metabolism[MESH] |Prodrugs/pharmacology[MESH] |Protein Binding/physiology[MESH] |Spike Glycoprotein, Coronavirus/*physiology[MESH] |Structure-Activity Relationship[MESH] |Triterpenes/*pharmacology[MESH]Binding of boswellic acids to functional proteins of the SARS-CoV-2 vi(epmc).pdf DeepDyve Pubget Overpricing