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10.1126/science.abb2507 http://scihub22266oqcxt.onion/10.1126/science.abb2507 32075877!7164637!32075877     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Science 2020 ; 367 (6483): 1260-1263 Nephropedia Template TP {{tp|p=32075877|t=2020. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation |pdf=|usr=}}{{32075877}} gab.com Text Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=32075877 #FOAvip The outbreak of a novel coronavirus (2019-nCoV) represents a pandemic threat that has been declared a public health emergency of international concern. The CoV spike (S) glycoprotein is a key target for vaccines, therapeutic antibodies, and diagnostics. To facilitate medical countermeasure development, we determined a 3.5-angstrom-resolution cryo-electron microscopy structure of the 2019-nCoV S trimer in the prefusion conformation. The predominant state of the trimer has one of the three receptor-binding domains (RBDs) rotated up in a receptor-accessible conformation. We also provide biophysical and structural evidence that the 2019-nCoV S protein binds angiotensin-converting enzyme 2 (ACE2) with higher affinity than does severe acute respiratory syndrome (SARS)-CoV S. Additionally, we tested several published SARS-CoV RBD-specific monoclonal antibodies and found that they do not have appreciable binding to 2019-nCoV S, suggesting that antibody cross-reactivity may be limited between the two RBDs. The structure of 2019-nCoV S should enable the rapid development and evaluation of medical countermeasures to address the ongoing public health crisis. Twit Text FOAVip Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation ????Science http://www.kidney.de/pget.php?&tw=1&pmid=32075877 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32075877 #FOAvip English Wikipedia <ref>{{Cite pmid|32075877}}</ref> Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation #MMPMID32075877 Wrapp D; Wang N; Corbett KS; Goldsmith JA; Hsieh CL; Abiona O; Graham BS; McLellan JS Science 2020[Mar]; 367 (6483): 1260-1263 PMID32075877show ga The outbreak of a novel coronavirus (2019-nCoV) represents a pandemic threat that has been declared a public health emergency of international concern. The CoV spike (S) glycoprotein is a key target for vaccines, therapeutic antibodies, and diagnostics. To facilitate medical countermeasure development, we determined a 3.5-angstrom-resolution cryo-electron microscopy structure of the 2019-nCoV S trimer in the prefusion conformation. The predominant state of the trimer has one of the three receptor-binding domains (RBDs) rotated up in a receptor-accessible conformation. We also provide biophysical and structural evidence that the 2019-nCoV S protein binds angiotensin-converting enzyme 2 (ACE2) with higher affinity than does severe acute respiratory syndrome (SARS)-CoV S. Additionally, we tested several published SARS-CoV RBD-specific monoclonal antibodies and found that they do not have appreciable binding to 2019-nCoV S, suggesting that antibody cross-reactivity may be limited between the two RBDs. The structure of 2019-nCoV S should enable the rapid development and evaluation of medical countermeasures to address the ongoing public health crisis. |Angiotensin-Converting Enzyme 2[MESH] |Antibodies, Monoclonal/immunology[MESH] |Antibodies, Viral/immunology[MESH] |Betacoronavirus/*chemistry/immunology/metabolism/ultrastructure[MESH] |Cross Reactions[MESH] |Cryoelectron Microscopy[MESH] |Image Processing, Computer-Assisted[MESH] |Models, Molecular[MESH] |Peptidyl-Dipeptidase A/metabolism[MESH] |Protein Binding[MESH] |Protein Conformation[MESH] |Protein Domains[MESH] |Protein Multimerization[MESH] |Receptors, Coronavirus[MESH] |Receptors, Virus/metabolism[MESH] |SARS-CoV-2[MESH] |Severe acute respiratory syndrome-related coronavirus/chemistry/immunology/ultrastructure[MESH]Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation(epmc).pdf DeepDyve Pubget Overpricing