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10.1007/s00203-020-01998-6 http://scihub22266oqcxt.onion/10.1007/s00203-020-01998-6 32749662!7401470!32749662     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       Arch+Microbiol 2021 ; 203 (1): 59-66 Nephropedia Template TP {{tp|p=32749662|t=2021. SARS-CoV-2 nucleocapsid and Nsp3 binding: an in silico study |pdf=|usr=}}{{32749662}} gab.com Text SARS-CoV-2 nucleocapsid and Nsp3 binding: an in silico study JO: Arch Microbiol http://www.kidney.de/pget.php?&tw=1&pmid=32749662 #FOAvip Severe acute respiratory syndrome virus 2 (SARS-CoV-2) belongs to the single-stranded positive-sense RNA family. The virus contains a large genome that encodes four structural proteins, small envelope (E), matrix (M), nucleocapsid phosphoprotein (N), spike (S), and 16 nonstructural proteins (nsp1-16) that together, ensure replication of the virus in the host cell. Among these proteins, the interactions of N and Nsp3 are essential that links the viral genome for processing. The N proteins reside at CoV RNA synthesis sites known as the replication-transcription complexes (RTCs). The N-terminal of N has RNA-binding domain (N-NTD), capturing the RNA genome while the C-terminal domain (N-CTD) anchors the viral Nsp3, a component of RTCs. Although the structural information has been recently released, the residues involved in contacts between N-CTD with Nsp3 are still unknown. To find the residues involved in interactions between two proteins, three-dimensional structures of both proteins were retrieved and docked using HADDOCK. Residues at N-CTD were detected in interaction with L499, R500, K501, V502, P503, T504, D505, N506, Y507, I508, T509, K529, K530K532, S533 of Nsp3 and N-NTD to synthesize SARS-CoV-2 RNA. The interaction between Nsp3 and CTD of N protein may be a potential drug target. The current study provides information for better understanding the interaction between N protein and Nsp3 that could be a possible target for future inhibitors. Twit Text FOAVip SARS-CoV-2 nucleocapsid and Nsp3 binding: an in silico study ????Arch Microbiol http://www.kidney.de/pget.php?&tw=1&pmid=32749662 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32749662 #FOAvip English Wikipedia <ref>{{Cite pmid|32749662}}</ref> SARS-CoV-2 nucleocapsid and Nsp3 binding: an in silico study #MMPMID32749662 Khan MT; Zeb MT; Ahsan H; Ahmed A; Ali A; Akhtar K; Malik SI; Cui Z; Ali S; Khan AS; Ahmad M; Wei DQ; Irfan M Arch Microbiol 2021[Jan]; 203 (1): 59-66 PMID32749662show ga Severe acute respiratory syndrome virus 2 (SARS-CoV-2) belongs to the single-stranded positive-sense RNA family. The virus contains a large genome that encodes four structural proteins, small envelope (E), matrix (M), nucleocapsid phosphoprotein (N), spike (S), and 16 nonstructural proteins (nsp1-16) that together, ensure replication of the virus in the host cell. Among these proteins, the interactions of N and Nsp3 are essential that links the viral genome for processing. The N proteins reside at CoV RNA synthesis sites known as the replication-transcription complexes (RTCs). The N-terminal of N has RNA-binding domain (N-NTD), capturing the RNA genome while the C-terminal domain (N-CTD) anchors the viral Nsp3, a component of RTCs. Although the structural information has been recently released, the residues involved in contacts between N-CTD with Nsp3 are still unknown. To find the residues involved in interactions between two proteins, three-dimensional structures of both proteins were retrieved and docked using HADDOCK. Residues at N-CTD were detected in interaction with L499, R500, K501, V502, P503, T504, D505, N506, Y507, I508, T509, K529, K530K532, S533 of Nsp3 and N-NTD to synthesize SARS-CoV-2 RNA. The interaction between Nsp3 and CTD of N protein may be a potential drug target. The current study provides information for better understanding the interaction between N protein and Nsp3 that could be a possible target for future inhibitors. |COVID-19 Drug Treatment[MESH] |Computer Simulation[MESH] |Coronavirus Nucleocapsid Proteins/genetics/*metabolism[MESH] |Coronavirus Papain-Like Proteases/genetics/*metabolism[MESH] |Crystallography, X-Ray[MESH] |Drug Design[MESH] |Genome, Viral[MESH] |Humans[MESH] |Molecular Docking Simulation[MESH] |Nucleocapsid/metabolism[MESH] |Protein Binding/physiology[MESH] |RNA-Binding Proteins/metabolism[MESH] |SARS-CoV-2/*metabolism[MESH]SARS-CoV-2 nucleocapsid and Nsp3 binding: an in silico study (epmc).pdf DeepDyve Pubget Overpricing