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10.1016/j.cell.2020.03.045 http://scihub22266oqcxt.onion/10.1016/j.cell.2020.03.045 32275855!7144619!32275855     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell 2020 ; 181 (4): 894-904.e9 Nephropedia Template TP {{tp|p=32275855|t=2020. Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2 |pdf=|usr=}}{{32275855}} gab.com Text Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2 JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=32275855 #FOAvip The recent emergence of a novel coronavirus (SARS-CoV-2) in China has caused significant public health concerns. Recently, ACE2 was reported as an entry receptor for SARS-CoV-2. In this study, we present the crystal structure of the C-terminal domain of SARS-CoV-2 (SARS-CoV-2-CTD) spike (S) protein in complex with human ACE2 (hACE2), which reveals a hACE2-binding mode similar overall to that observed for SARS-CoV. However, atomic details at the binding interface demonstrate that key residue substitutions in SARS-CoV-2-CTD slightly strengthen the interaction and lead to higher affinity for receptor binding than SARS-RBD. Additionally, a panel of murine monoclonal antibodies (mAbs) and polyclonal antibodies (pAbs) against SARS-CoV-S1/receptor-binding domain (RBD) were unable to interact with the SARS-CoV-2 S protein, indicating notable differences in antigenicity between SARS-CoV and SARS-CoV-2. These findings shed light on the viral pathogenesis and provide important structural information regarding development of therapeutic countermeasures against the emerging virus. Twit Text FOAVip Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2 ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=32275855 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32275855 #FOAvip English Wikipedia <ref>{{Cite pmid|32275855}}</ref> Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2 #MMPMID32275855 Wang Q; Zhang Y; Wu L; Niu S; Song C; Zhang Z; Lu G; Qiao C; Hu Y; Yuen KY; Wang Q; Zhou H; Yan J; Qi J Cell 2020[May]; 181 (4): 894-904.e9 PMID32275855show ga The recent emergence of a novel coronavirus (SARS-CoV-2) in China has caused significant public health concerns. Recently, ACE2 was reported as an entry receptor for SARS-CoV-2. In this study, we present the crystal structure of the C-terminal domain of SARS-CoV-2 (SARS-CoV-2-CTD) spike (S) protein in complex with human ACE2 (hACE2), which reveals a hACE2-binding mode similar overall to that observed for SARS-CoV. However, atomic details at the binding interface demonstrate that key residue substitutions in SARS-CoV-2-CTD slightly strengthen the interaction and lead to higher affinity for receptor binding than SARS-RBD. Additionally, a panel of murine monoclonal antibodies (mAbs) and polyclonal antibodies (pAbs) against SARS-CoV-S1/receptor-binding domain (RBD) were unable to interact with the SARS-CoV-2 S protein, indicating notable differences in antigenicity between SARS-CoV and SARS-CoV-2. These findings shed light on the viral pathogenesis and provide important structural information regarding development of therapeutic countermeasures against the emerging virus. |*Virus Internalization[MESH] |Amino Acid Sequence[MESH] |Angiotensin-Converting Enzyme 2[MESH] |Betacoronavirus/*chemistry/physiology[MESH] |Epitopes[MESH] |Humans[MESH] |Models, Molecular[MESH] |Peptidyl-Dipeptidase A/*chemistry/metabolism[MESH] |Phylogeny[MESH] |Protein Domains[MESH] |SARS-CoV-2[MESH] |Sequence Alignment[MESH] |Severe acute respiratory syndrome-related coronavirus/chemistry/physiology[MESH]Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE(epmc).pdf DeepDyve Pubget Overpricing