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10.1016/j.bbrep.2021.101023 http://scihub22266oqcxt.onion/10.1016/j.bbrep.2021.101023 34013072!8120451!34013072     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=34013072&cmd=llinks): Failed to open stream: HTTP request failed! 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Sequence and structural analysis of COVID-19 E and M proteins with MERS virus E and M proteins-A comparative study |pdf=|usr=}}{{34013072}} gab.com Text Sequence and structural analysis of COVID-19 E and M proteins with MERS virus E and M proteins-A comparative study JO: Biochem Biophys Rep http://www.kidney.de/pget.php?&tw=1&pmid=34013072 #FOAvip The outbreak of SARS in 2003, MERS in 2012, and now COVID-19 in 2019 has demonstrated that Coronaviruses are capable of causing primary lethal infections in humans, and the pandemic is now a global concern. The COVID-19 belongs to the beta coronavirus family encoding 29 proteins, of which four are structural, the Spike, Membrane, Envelope, and Nucleocapsid proteins. Here we have analyzed and compared the Membrane (M) and Envelope (E) proteins of COVID-19 and MERS with SARS and Bat viruses. The sequence analysis of conserved regions of both E and M proteins revealed that many regions of COVID-19 are similar to Bat and SARS viruses while the MERS virus showed variations. The essential binding motifs found in SARS appeared in COVID-19. Besides, the M protein of COVID-19 showed a distinct serine phosphorylation site in the C-terminal domain, which looked like a catalytic triad seen in serine proteases. A Dileucine motif occurred many times in the sequence of the M protein of all the four viruses compared. Concerning the structural part, the COVID-19 E protein showed more similarity to Bat while MERS shared similarity with the SARS virus. The M protein of both COVID-19 and MERS displayed variations in the structure. The interaction between M and E proteins was also studied to know the additional binding regions. Our study highlights the critical motifs and structural regions to be considered for further research to design better inhibitors for the infection caused by these viruses. Twit Text FOAVip Sequence and structural analysis of COVID-19 E and M proteins with MERS virus E and M proteins-A comparative study ????Biochem Biophys Rep http://www.kidney.de/pget.php?&tw=1&pmid=34013072 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34013072 #FOAvip English Wikipedia <ref>{{Cite pmid|34013072}}</ref> Sequence and structural analysis of COVID-19 E and M proteins with MERS virus E and M proteins-A comparative study #MMPMID34013072 Aldaais EA; Yegnaswamy S; Albahrani F; Alsowaiket F; Alramadan S Biochem Biophys Rep 2021[Jul]; 26 (ä): 101023 PMID34013072show ga The outbreak of SARS in 2003, MERS in 2012, and now COVID-19 in 2019 has demonstrated that Coronaviruses are capable of causing primary lethal infections in humans, and the pandemic is now a global concern. The COVID-19 belongs to the beta coronavirus family encoding 29 proteins, of which four are structural, the Spike, Membrane, Envelope, and Nucleocapsid proteins. Here we have analyzed and compared the Membrane (M) and Envelope (E) proteins of COVID-19 and MERS with SARS and Bat viruses. The sequence analysis of conserved regions of both E and M proteins revealed that many regions of COVID-19 are similar to Bat and SARS viruses while the MERS virus showed variations. The essential binding motifs found in SARS appeared in COVID-19. Besides, the M protein of COVID-19 showed a distinct serine phosphorylation site in the C-terminal domain, which looked like a catalytic triad seen in serine proteases. A Dileucine motif occurred many times in the sequence of the M protein of all the four viruses compared. Concerning the structural part, the COVID-19 E protein showed more similarity to Bat while MERS shared similarity with the SARS virus. The M protein of both COVID-19 and MERS displayed variations in the structure. The interaction between M and E proteins was also studied to know the additional binding regions. Our study highlights the critical motifs and structural regions to be considered for further research to design better inhibitors for the infection caused by these viruses. äSequence and structural analysis of COVID-19 E and M proteins with MER(epmc).pdf DeepDyve Pubget Overpricing