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10.1016/j.bbrc.2020.11.026 http://scihub22266oqcxt.onion/10.1016/j.bbrc.2020.11.026 33220921!7664360!33220921     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biochem+Biophys+Res+Commun 2021 ; 538 (ä): 108-115 Nephropedia Template TP {{tp|p=33220921|t=2021. Functional importance of the D614G mutation in the SARS-CoV-2 spike protein |pdf=|usr=}}{{33220921}} gab.com Text Functional importance of the D614G mutation in the SARS-CoV-2 spike protein JO: Biochem Biophys Res Commun http://www.kidney.de/pget.php?&tw=1&pmid=33220921 #FOAvip Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is an enveloped virus which binds its cellular receptor angiotensin-converting enzyme 2 (ACE2) and enters hosts cells through the action of its spike (S) glycoprotein displayed on the surface of the virion. Compared to the reference strain of SARS-CoV-2, the majority of currently circulating isolates possess an S protein variant characterized by an aspartic acid-to-glycine substitution at amino acid position 614 (D614G). Residue 614 lies outside the receptor binding domain (RBD) and the mutation does not alter the affinity of monomeric S protein for ACE2. However, S(G614), compared to S(D614), mediates more efficient ACE2-mediated transduction of cells by S-pseudotyped vectors and more efficient infection of cells and animals by live SARS-CoV-2. This review summarizes and synthesizes the epidemiological and functional observations of the D614G spike mutation, with focus on the biochemical and cell-biological impact of this mutation and its consequences for S protein function. We further discuss the significance of these recent findings in the context of the current global pandemic. Twit Text FOAVip Functional importance of the D614G mutation in the SARS-CoV-2 spike protein ????Biochem Biophys Res Commun http://www.kidney.de/pget.php?&tw=1&pmid=33220921 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33220921 #FOAvip English Wikipedia <ref>{{Cite pmid|33220921}}</ref> Functional importance of the D614G mutation in the SARS-CoV-2 spike protein #MMPMID33220921 Jackson CB; Zhang L; Farzan M; Choe H Biochem Biophys Res Commun 2021[Jan]; 538 (ä): 108-115 PMID33220921show ga Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is an enveloped virus which binds its cellular receptor angiotensin-converting enzyme 2 (ACE2) and enters hosts cells through the action of its spike (S) glycoprotein displayed on the surface of the virion. Compared to the reference strain of SARS-CoV-2, the majority of currently circulating isolates possess an S protein variant characterized by an aspartic acid-to-glycine substitution at amino acid position 614 (D614G). Residue 614 lies outside the receptor binding domain (RBD) and the mutation does not alter the affinity of monomeric S protein for ACE2. However, S(G614), compared to S(D614), mediates more efficient ACE2-mediated transduction of cells by S-pseudotyped vectors and more efficient infection of cells and animals by live SARS-CoV-2. This review summarizes and synthesizes the epidemiological and functional observations of the D614G spike mutation, with focus on the biochemical and cell-biological impact of this mutation and its consequences for S protein function. We further discuss the significance of these recent findings in the context of the current global pandemic. |Amino Acid Substitution/genetics[MESH] |Aspartic Acid/genetics[MESH] |Binding Sites/genetics[MESH] |COVID-19/*virology[MESH] |Glycine/genetics[MESH] |Humans[MESH] |Mutation[MESH] |Protein Domains/genetics[MESH] |SARS-CoV-2/*genetics[MESH]Functional importance of the D614G mutation in the SARS-CoV-2 spike pr(epmc).pdf DeepDyve Pubget Overpricing