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10.1177/24725552211008854 http://scihub22266oqcxt.onion/10.1177/24725552211008854 33870746!8053483!33870746     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 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       SLAS+Discov 2021 ; 26 (6): 766-774 Nephropedia Template TP {{tp|p=33870746|t=2021. Label-Free Screening of SARS-CoV-2 NSP14 Exonuclease Activity Using SAMDI Mass Spectrometry |pdf=|usr=}}{{33870746}} gab.com Text Label-Free Screening of SARS-CoV-2 NSP14 Exonuclease Activity Using SAMDI Mass Spectrometry JO: SLAS Discov http://www.kidney.de/pget.php?&tw=1&pmid=33870746 #FOAvip Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the virus responsible for the global COVID-19 pandemic. Nonstructural protein 14 (NSP14), which features exonuclease (ExoN) and guanine N7 methyltransferase activity, is a critical player in SARS-CoV-2 replication and fidelity and represents an attractive antiviral target. Initiating drug discovery efforts for nucleases such as NSP14 remains a challenge due to a lack of suitable high-throughput assay methodologies. This report describes the combination of self-assembled monolayers and matrix-assisted laser desorption ionization mass spectrometry to enable the first label-free and high-throughput assay for NSP14 ExoN activity. The assay was used to measure NSP14 activity and gain insight into substrate specificity and the reaction mechanism. Next, the assay was optimized for kinetically balanced conditions and miniaturized, while achieving a robust assay (Z factor > 0.8) and a significant assay window (signal-to-background ratio > 200). Screening 10,240 small molecules from a diverse library revealed candidate inhibitors, which were counterscreened for NSP14 selectivity and RNA intercalation. The assay methodology described here will enable, for the first time, a label-free and high-throughput assay for NSP14 ExoN activity to accelerate drug discovery efforts and, due to the assay flexibility, can be more broadly applicable for measuring other enzyme activities from other viruses or implicated in various pathologies. Twit Text FOAVip Label-Free Screening of SARS-CoV-2 NSP14 Exonuclease Activity Using SAMDI Mass Spectrometry ????SLAS Discov http://www.kidney.de/pget.php?&tw=1&pmid=33870746 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33870746 #FOAvip English Wikipedia <ref>{{Cite pmid|33870746}}</ref> Label-Free Screening of SARS-CoV-2 NSP14 Exonuclease Activity Using SAMDI Mass Spectrometry #MMPMID33870746 Scholle MD; Liu C; Deval J; Gurard-Levin ZA SLAS Discov 2021[Jul]; 26 (6): 766-774 PMID33870746show ga Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the virus responsible for the global COVID-19 pandemic. Nonstructural protein 14 (NSP14), which features exonuclease (ExoN) and guanine N7 methyltransferase activity, is a critical player in SARS-CoV-2 replication and fidelity and represents an attractive antiviral target. Initiating drug discovery efforts for nucleases such as NSP14 remains a challenge due to a lack of suitable high-throughput assay methodologies. This report describes the combination of self-assembled monolayers and matrix-assisted laser desorption ionization mass spectrometry to enable the first label-free and high-throughput assay for NSP14 ExoN activity. The assay was used to measure NSP14 activity and gain insight into substrate specificity and the reaction mechanism. Next, the assay was optimized for kinetically balanced conditions and miniaturized, while achieving a robust assay (Z factor > 0.8) and a significant assay window (signal-to-background ratio > 200). Screening 10,240 small molecules from a diverse library revealed candidate inhibitors, which were counterscreened for NSP14 selectivity and RNA intercalation. The assay methodology described here will enable, for the first time, a label-free and high-throughput assay for NSP14 ExoN activity to accelerate drug discovery efforts and, due to the assay flexibility, can be more broadly applicable for measuring other enzyme activities from other viruses or implicated in various pathologies. |*High-Throughput Screening Assays[MESH] |Antiviral Agents/chemistry/*pharmacology[MESH] |COVID-19/virology[MESH] |Cloning, Molecular[MESH] |Enzyme Assays[MESH] |Enzyme Inhibitors/chemistry/*pharmacology[MESH] |Escherichia coli/genetics/metabolism[MESH] |Exonucleases/*antagonists & inhibitors/genetics/metabolism[MESH] |Exoribonucleases/*antagonists & inhibitors/genetics/metabolism[MESH] |Gene Expression[MESH] |Genetic Vectors/chemistry/metabolism[MESH] |Humans[MESH] |Kinetics[MESH] |RNA, Viral/*antagonists & inhibitors/genetics/metabolism[MESH] |Recombinant Proteins/genetics/metabolism[MESH] |SARS-CoV-2/*drug effects/enzymology/genetics[MESH] |Small Molecule Libraries/chemistry/pharmacology[MESH] |Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/methods[MESH] |Substrate Specificity[MESH] |Viral Nonstructural Proteins/*antagonists & inhibitors/genetics/metabolism[MESH]Label-Free Screening of SARS-CoV-2 NSP14 Exonuclease Activity Using SA(epmc).pdf DeepDyve Pubget Overpricing