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10.1007/s12104-020-10001-8 http://scihub22266oqcxt.onion/10.1007/s12104-020-10001-8 33475934!7819138!33475934     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biomol+NMR+Assign 2021 ; 15 (1): 173-176 Nephropedia Template TP {{tp|p=33475934|t=2021. (1)H, (13)C and (15)N backbone chemical shift assignments of SARS-CoV-2 nsp3a |pdf=|usr=}}{{33475934}} gab.com Text (1)H, (13)C and (15)N backbone chemical shift assignments of SARS-CoV-2 nsp3a JO: Biomol NMR Assign http://www.kidney.de/pget.php?&tw=1&pmid=33475934 #FOAvip The non-structural protein nsp3 from SARS-CoV-2 plays an essential role in the viral replication transcription complex. Nsp3a constitutes the N-terminal domain of nsp3, comprising a ubiquitin-like folded domain and a disordered acidic chain. This region of nsp3a has been linked to interactions with the viral nucleoprotein and the structure of double membrane vesicles. Here, we report the backbone resonance assignment of both domains of nsp3a. The study is carried out in the context of the international covid19-nmr consortium, which aims to characterize SARS-CoV-2 proteins and RNAs, providing for example NMR chemical shift assignments of the different viral components. Our assignment will provide the basis for the identification of inhibitors and further functional and interaction studies of this essential protein. Twit Text FOAVip (1)H, (13)C and (15)N backbone chemical shift assignments of SARS-CoV-2 nsp3a ????Biomol NMR Assign http://www.kidney.de/pget.php?&tw=1&pmid=33475934 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33475934 #FOAvip English Wikipedia <ref>{{Cite pmid|33475934}}</ref> (1)H, (13)C and (15)N backbone chemical shift assignments of SARS-CoV-2 nsp3a #MMPMID33475934 Salvi N; Bessa LM; Guseva S; Camacho-Zarco A; Maurin D; Perez LM; Malki A; Hengesbach M; Korn SM; Schlundt A; Schwalbe H; Blackledge M Biomol NMR Assign 2021[Apr]; 15 (1): 173-176 PMID33475934show ga The non-structural protein nsp3 from SARS-CoV-2 plays an essential role in the viral replication transcription complex. Nsp3a constitutes the N-terminal domain of nsp3, comprising a ubiquitin-like folded domain and a disordered acidic chain. This region of nsp3a has been linked to interactions with the viral nucleoprotein and the structure of double membrane vesicles. Here, we report the backbone resonance assignment of both domains of nsp3a. The study is carried out in the context of the international covid19-nmr consortium, which aims to characterize SARS-CoV-2 proteins and RNAs, providing for example NMR chemical shift assignments of the different viral components. Our assignment will provide the basis for the identification of inhibitors and further functional and interaction studies of this essential protein. |*Magnetic Resonance Spectroscopy[MESH] |Carbon Isotopes[MESH] |Coronavirus Papain-Like Proteases/*chemistry[MESH] |Escherichia coli[MESH] |Hydrogen[MESH] |Hydrogen-Ion Concentration[MESH] |Nitrogen Isotopes[MESH] |Plasmids/metabolism[MESH] |Protein Binding[MESH] |Protein Domains[MESH] |Protein Structure, Secondary[MESH](1)H, (13)C and (15)N backbone chemical shift assignments of SARS-CoV-(epmc).pdf DeepDyve Pubget Overpricing