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10.1016/j.bbrc.2021.06.100 http://scihub22266oqcxt.onion/10.1016/j.bbrc.2021.06.100 34246830!8249750!34246830     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=34246830&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 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 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 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 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biochem+Biophys+Res+Commun 2021 ; 569 (ä): 154-160 Nephropedia Template TP {{tp|p=34246830|t=2021. Analysis of SARS-CoV-2 nucleocapsid phosphoprotein N variations in the binding site to human 14-3-3 proteins |pdf=|usr=}}{{34246830}} gab.com Text Analysis of SARS-CoV-2 nucleocapsid phosphoprotein N variations in the binding site to human 14-3-3 proteins JO: Biochem Biophys Res Commun http://www.kidney.de/pget.php?&tw=1&pmid=34246830 #FOAvip The SARS-CoV-2 N protein binds several cell host proteins including 14-3-3gamma, a well-characterized regulatory protein. However, the biological function of this interaction is not completely understood. We analyzed the variability of approximately 90 000 sequences of the SARS-CoV-2 N protein, particularly, its mutations in disordered regions containing binding motifs for 14-3-3 proteins. We studied how these mutations affect the binding energy to 14-3-3gamma and found that changes positively affecting the predicted interaction with 14-3-3gamma are the most successfully spread, with the highest prevalence in the phylogenetic tree. Although most residues are highly conserved within the 14-3-3 binding site, compensatory mutations to maintain the interaction energy of N-14-3-3gamma were found, including half of the current variants of concern and interest. Our results suggest that binding of N to 14-3-3gamma is beneficial for the virus, thus targeting this viral-host protein-protein interaction seems an attractive approach to explore antiviral strategies. Twit Text FOAVip Analysis of SARS-CoV-2 nucleocapsid phosphoprotein N variations in the binding site to human 14-3-3 proteins ????Biochem Biophys Res Commun http://www.kidney.de/pget.php?&tw=1&pmid=34246830 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34246830 #FOAvip English Wikipedia <ref>{{Cite pmid|34246830}}</ref> Analysis of SARS-CoV-2 nucleocapsid phosphoprotein N variations in the binding site to human 14-3-3 proteins #MMPMID34246830 Del Veliz S; Rivera L; Bustos DM; Uhart M Biochem Biophys Res Commun 2021[Sep]; 569 (ä): 154-160 PMID34246830show ga The SARS-CoV-2 N protein binds several cell host proteins including 14-3-3gamma, a well-characterized regulatory protein. However, the biological function of this interaction is not completely understood. We analyzed the variability of approximately 90 000 sequences of the SARS-CoV-2 N protein, particularly, its mutations in disordered regions containing binding motifs for 14-3-3 proteins. We studied how these mutations affect the binding energy to 14-3-3gamma and found that changes positively affecting the predicted interaction with 14-3-3gamma are the most successfully spread, with the highest prevalence in the phylogenetic tree. Although most residues are highly conserved within the 14-3-3 binding site, compensatory mutations to maintain the interaction energy of N-14-3-3gamma were found, including half of the current variants of concern and interest. Our results suggest that binding of N to 14-3-3gamma is beneficial for the virus, thus targeting this viral-host protein-protein interaction seems an attractive approach to explore antiviral strategies. |14-3-3 Proteins/*metabolism[MESH] |Binding Sites[MESH] |Coronavirus Nucleocapsid Proteins/*analysis/genetics/*metabolism[MESH] |Humans[MESH] |Mutation/genetics[MESH] |Phosphoproteins/analysis/genetics/metabolism[MESH] |Phosphorylation[MESH] |Phylogeny[MESH]Analysis of SARS-CoV-2 nucleocapsid phosphoprotein N variations in the(epmc).pdf DeepDyve Pubget Overpricing