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.

10.1021/acs.biochem.0c00309 http://scihub22266oqcxt.onion/10.1021/acs.biochem.0c00309 32578982!7341687!32578982     free     free     free  :  Publisher Nephropedia Template TP {{tp|p=32578982|t=2020. Molecular Basis for ADP-Ribose Binding to the Mac1 Domain of SARS-CoV-2 nsp3 |pdf=|usr=}} gab.com Text Molecular Basis for ADP-Ribose Binding to the Mac1 Domain of SARS-CoV-2 nsp3 JO: Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=32578982 #FOAvip The virus that causes COVID-19, SARS-CoV-2, has a large RNA genome that encodes numerous proteins that might be targets for antiviral drugs. Some of these proteins, such as the RNA-dependent RNA polymerase, helicase, and main protease, are well conserved between SARS-CoV-2 and the original SARS virus, but several others are not. This study examines one of the proteins encoded by SARS-CoV-2 that is most different, a macrodomain of nonstructural protein 3 (nsp3). Although 26% of the amino acids in this SARS-CoV-2 macrodomain differ from those observed in other coronaviruses, biochemical and structural data reveal that the protein retains the ability to bind ADP-ribose, which is an important characteristic of beta coronaviruses and a potential therapeutic target. Twit Text FOAVip Molecular Basis for ADP-Ribose Binding to the Mac1 Domain of SARS-CoV-2 nsp3 🦆🦆Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=32578982 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32578982 #FOAvip English Wikipedia <ref>{{Cite pmid|32578982}}</ref> Molecular Basis for ADP-Ribose Binding to the Mac1 Domain of SARS-CoV-2 nsp3 #MMPMID32578982 Frick DN; Virdi RS; Vuksanovic N; Dahal N; Silvaggi NR Biochemistry 2020[Jul]; 59 (28): 2608-2615 PMID32578982show ga The virus that causes COVID-19, SARS-CoV-2, has a large RNA genome that encodes numerous proteins that might be targets for antiviral drugs. Some of these proteins, such as the RNA-dependent RNA polymerase, helicase, and main protease, are well conserved between SARS-CoV-2 and the original SARS virus, but several others are not. This study examines one of the proteins encoded by SARS-CoV-2 that is most different, a macrodomain of nonstructural protein 3 (nsp3). Although 26% of the amino acids in this SARS-CoV-2 macrodomain differ from those observed in other coronaviruses, biochemical and structural data reveal that the protein retains the ability to bind ADP-ribose, which is an important characteristic of beta coronaviruses and a potential therapeutic target. |Adenosine Diphosphate Ribose/metabolism[MESH] |Betacoronavirus/*chemistry[MESH] |COVID-19[MESH] |Coronavirus Infections/drug therapy/virology[MESH] |Coronavirus Papain-Like Proteases[MESH] |Coronavirus/chemistry[MESH] |Crystallography, X-Ray[MESH] |Drug Delivery Systems[MESH] |Humans[MESH] |Models, Molecular[MESH] |Pandemics[MESH] |Pneumonia, Viral/drug therapy/virology[MESH] |Protein Domains[MESH] |SARS-CoV-2[MESH] |Thermodynamics[MESH] |Viral Nonstructural Proteins/*chemistry/metabolism[MESH]Molecular Basis for ADP-Ribose Binding to the Mac1 Domain of SARS-CoV-(epmc).pdf DeepDyve Pubget Overpricing