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10.1097/COH.0000000000000658 http://scihub22266oqcxt.onion/10.1097/COH.0000000000000658 33186231!ä!33186231 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Curr+Opin+HIV+AIDS 2021 ; 16 (1): 74-81 Nephropedia Template TP {{tp|p=33186231|t=2021. Structural basis of severe acute respiratory syndrome coronavirus 2 infection |pdf=|usr=}}{{33186231}} gab.com Text Structural basis of severe acute respiratory syndrome coronavirus 2 infection JO: Curr Opin HIV AIDS http://www.kidney.de/pget.php?&tw=1&pmid=33186231 #FOAvip PURPOSE OF REVIEW: The spike glycoprotein plays a critical role in severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection by recognizing the angiotensin converting enzyme 2 (ACE2) receptor and mediating fusion of the viral envelope with the cell membrane. It is also the major target for neutralizing antibodies and vaccines. This review summarizes recent studies on the structure and function of spike glycoprotein, which revealed the structural basis of SARS-CoV-2 infection. RECENT FINDINGS: SARS-CoV-2 spike glycoprotein, similar to those of SARS-CoV and Middle East respiratory syndrome coronavirus, spontaneously samples different prefusion states with the receptor-binding domain (RBD) adopting 'up' or 'down' conformations, and the RBD 'down' to 'up' conformational change is required for ACE2 binding. Receptor binding and spike glycoprotein priming by host proteases such as furin and transmembrane protease serine 2 induce pre to postfusion conformational changes of the spike trimer that enable membrane fusion. Interactions between SARS-CoV-2 RBD and ACE2 were elucidated at atomic resolution using high-resolution crystal structures. These structures, together with adapted and remodeled SARS-CoV-2 strains, further revealed critical residues of the spike glycoprotein for SARS-CoV-2 infection and cross-species transmission. SUMMARY: Recent studies on SARS-CoV-2 spike glycoprotein provide important structural knowledge for a better understanding of the molecular mechanisms of SARS-CoV-2 infection and cross-species transmission. Twit Text FOAVip Structural basis of severe acute respiratory syndrome coronavirus 2 infection ????Curr Opin HIV AIDS http://www.kidney.de/pget.php?&tw=1&pmid=33186231 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33186231 #FOAvip English Wikipedia <ref>{{Cite pmid|33186231}}</ref> Structural basis of severe acute respiratory syndrome coronavirus 2 infection #MMPMID33186231 Ge J; Zhang S; Zhang L; Wang X Curr Opin HIV AIDS 2021[Jan]; 16 (1): 74-81 PMID33186231show ga PURPOSE OF REVIEW: The spike glycoprotein plays a critical role in severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection by recognizing the angiotensin converting enzyme 2 (ACE2) receptor and mediating fusion of the viral envelope with the cell membrane. It is also the major target for neutralizing antibodies and vaccines. This review summarizes recent studies on the structure and function of spike glycoprotein, which revealed the structural basis of SARS-CoV-2 infection. RECENT FINDINGS: SARS-CoV-2 spike glycoprotein, similar to those of SARS-CoV and Middle East respiratory syndrome coronavirus, spontaneously samples different prefusion states with the receptor-binding domain (RBD) adopting 'up' or 'down' conformations, and the RBD 'down' to 'up' conformational change is required for ACE2 binding. Receptor binding and spike glycoprotein priming by host proteases such as furin and transmembrane protease serine 2 induce pre to postfusion conformational changes of the spike trimer that enable membrane fusion. Interactions between SARS-CoV-2 RBD and ACE2 were elucidated at atomic resolution using high-resolution crystal structures. These structures, together with adapted and remodeled SARS-CoV-2 strains, further revealed critical residues of the spike glycoprotein for SARS-CoV-2 infection and cross-species transmission. SUMMARY: Recent studies on SARS-CoV-2 spike glycoprotein provide important structural knowledge for a better understanding of the molecular mechanisms of SARS-CoV-2 infection and cross-species transmission. |Angiotensin-Converting Enzyme 2/chemistry/genetics/metabolism[MESH] |Animals[MESH] |Binding Sites[MESH] |COVID-19/enzymology/genetics/*virology[MESH] |Humans[MESH] |Protein Binding[MESH] |SARS-CoV-2/chemistry/genetics/*metabolism[MESH]Structural basis of severe acute respiratory syndrome coronavirus 2 in(epmc).pdf DeepDyve Pubget Overpricing