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10.15252/embj.2020105938 http://scihub22266oqcxt.onion/10.15252/embj.2020105938 32914439!7560215!32914439     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       EMBO+J 2020 ; 39 (20): e105938 Nephropedia Template TP {{tp|p=32914439|t=2020. Structures of the SARS-CoV-2 nucleocapsid and their perspectives for drug design |pdf=|usr=}}{{32914439}} gab.com Text Structures of the SARS-CoV-2 nucleocapsid and their perspectives for drug design JO: EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=32914439 #FOAvip COVID-19, caused by SARS-CoV-2, has resulted in severe and unprecedented economic and social disruptions in the world. Nucleocapsid (N) protein, which is the major structural component of the virion and is involved in viral replication, assembly and immune regulation, plays key roles in the viral life cycle. Here, we solved the crystal structures of the N- and C-terminal domains (N-NTD and N-CTD) of SARS-CoV-2 N protein, at 1.8 and 1.5 A resolution, respectively. Both structures show conserved features from other CoV N proteins. The binding sites targeted by small molecules against HCoV-OC43 and MERS-CoV, which inhibit viral infection by blocking the RNA-binding activity or normal oligomerization of N protein, are relatively conserved in our structure, indicating N protein is a promising drug target. In addition, certain areas of N-NTD and N-CTD display distinct charge distribution patterns in SARS-CoV-2, which may alter the RNA-binding modes. The specific antigenic characteristics are critical for developing specific immune-based rapid diagnostic tests. Our structural information can aid in the discovery and development of antiviral inhibitors against SARS-CoV-2 in the future. Twit Text FOAVip Structures of the SARS-CoV-2 nucleocapsid and their perspectives for drug design ????EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=32914439 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32914439 #FOAvip English Wikipedia <ref>{{Cite pmid|32914439}}</ref> Structures of the SARS-CoV-2 nucleocapsid and their perspectives for drug design #MMPMID32914439 Peng Y; Du N; Lei Y; Dorje S; Qi J; Luo T; Gao GF; Song H EMBO J 2020[Oct]; 39 (20): e105938 PMID32914439show ga COVID-19, caused by SARS-CoV-2, has resulted in severe and unprecedented economic and social disruptions in the world. Nucleocapsid (N) protein, which is the major structural component of the virion and is involved in viral replication, assembly and immune regulation, plays key roles in the viral life cycle. Here, we solved the crystal structures of the N- and C-terminal domains (N-NTD and N-CTD) of SARS-CoV-2 N protein, at 1.8 and 1.5 A resolution, respectively. Both structures show conserved features from other CoV N proteins. The binding sites targeted by small molecules against HCoV-OC43 and MERS-CoV, which inhibit viral infection by blocking the RNA-binding activity or normal oligomerization of N protein, are relatively conserved in our structure, indicating N protein is a promising drug target. In addition, certain areas of N-NTD and N-CTD display distinct charge distribution patterns in SARS-CoV-2, which may alter the RNA-binding modes. The specific antigenic characteristics are critical for developing specific immune-based rapid diagnostic tests. Our structural information can aid in the discovery and development of antiviral inhibitors against SARS-CoV-2 in the future. |*Drug Design[MESH] |Antiviral Agents/*pharmacology[MESH] |Betacoronavirus/*chemistry/drug effects[MESH] |Coronavirus Nucleocapsid Proteins[MESH] |Crystallography, X-Ray[MESH] |Drug Delivery Systems[MESH] |Humans[MESH] |Models, Molecular[MESH] |Nucleocapsid Proteins/*chemistry/drug effects[MESH] |Phosphoproteins[MESH] |Protein Conformation[MESH] |Protein Domains[MESH] |Recombinant Proteins/chemistry[MESH]Structures of the SARS-CoV-2 nucleocapsid and their perspectives for d(epmc).pdf DeepDyve Pubget Overpricing