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10.7717/peerj.10666 http://scihub22266oqcxt.onion/10.7717/peerj.10666 33505806!7789862!33505806     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=33505806&cmd=llinks): Failed to open stream: HTTP request failed! 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Identification and molecular characterization of mutations in nucleocapsid phosphoprotein of SARS-CoV-2 |pdf=|usr=}}{{33505806}} gab.com Text Identification and molecular characterization of mutations in nucleocapsid phosphoprotein of SARS-CoV-2 JO: PeerJ http://www.kidney.de/pget.php?&tw=1&pmid=33505806 #FOAvip SARS-CoV-2 genome encodes four structural proteins that include the spike glycoprotein, membrane protein, envelope protein and nucleocapsid phosphoprotein (N-protein). The N-protein interacts with viral genomic RNA and helps in packaging. As SARS-CoV-2 spread to almost all countries worldwide within 2-3 months, it also acquired mutations in its RNA genome. Therefore, this study was conducted with an aim to identify the variations present in N-protein of SARS-CoV-2. Here, we analysed 4,163 reported sequence of N-protein from United States of America (USA) and compared them with the first reported sequence from Wuhan, China. Our study identified 107 mutations that reside all over the N-protein. Further, we show the high rate of mutations in intrinsically disordered regions (IDRs) of N-protein. Our study show 45% residues of IDR2 harbour mutations. The RNA-binding domain (RBD) and dimerization domain of N-protein also have mutations at key residues. We further measured the effect of these mutations on N-protein stability and dynamicity and our data reveals that multiple mutations can cause considerable alterations. Altogether, our data strongly suggests that N-protein is one of the mutational hotspot proteins of SARS-CoV-2 that is changing rapidly and these mutations can potentially interferes with various aspects of N-protein functions including its interaction with RNA, oligomerization and signalling events. Twit Text FOAVip Identification and molecular characterization of mutations in nucleocapsid phosphoprotein of SARS-CoV-2 ????PeerJ http://www.kidney.de/pget.php?&tw=1&pmid=33505806 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33505806 #FOAvip English Wikipedia <ref>{{Cite pmid|33505806}}</ref> Identification and molecular characterization of mutations in nucleocapsid phosphoprotein of SARS-CoV-2 #MMPMID33505806 Azad GK PeerJ 2021[]; 9 (ä): e10666 PMID33505806show ga SARS-CoV-2 genome encodes four structural proteins that include the spike glycoprotein, membrane protein, envelope protein and nucleocapsid phosphoprotein (N-protein). The N-protein interacts with viral genomic RNA and helps in packaging. As SARS-CoV-2 spread to almost all countries worldwide within 2-3 months, it also acquired mutations in its RNA genome. Therefore, this study was conducted with an aim to identify the variations present in N-protein of SARS-CoV-2. Here, we analysed 4,163 reported sequence of N-protein from United States of America (USA) and compared them with the first reported sequence from Wuhan, China. Our study identified 107 mutations that reside all over the N-protein. Further, we show the high rate of mutations in intrinsically disordered regions (IDRs) of N-protein. Our study show 45% residues of IDR2 harbour mutations. The RNA-binding domain (RBD) and dimerization domain of N-protein also have mutations at key residues. We further measured the effect of these mutations on N-protein stability and dynamicity and our data reveals that multiple mutations can cause considerable alterations. Altogether, our data strongly suggests that N-protein is one of the mutational hotspot proteins of SARS-CoV-2 that is changing rapidly and these mutations can potentially interferes with various aspects of N-protein functions including its interaction with RNA, oligomerization and signalling events. äIdentification and molecular characterization of mutations in nucleoca(epmc).pdf DeepDyve Pubget Overpricing