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10.1038/s41467-020-18387-8 http://scihub22266oqcxt.onion/10.1038/s41467-020-18387-8 32913273!7483421!32913273     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2020 ; 11 (1): 4528 Nephropedia Template TP {{tp|p=32913273|t=2020. Humanized single domain antibodies neutralize SARS-CoV-2 by targeting the spike receptor binding domain |pdf=|usr=}}{{32913273}} gab.com Text Humanized single domain antibodies neutralize SARS-CoV-2 by targeting the spike receptor binding domain JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=32913273 #FOAvip Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spreads worldwide and leads to an unprecedented medical burden and lives lost. Neutralizing antibodies provide efficient blockade for viral infection and are a promising category of biological therapies. Here, using SARS-CoV-2 spike receptor-binding domain (RBD) as a bait, we generate a panel of humanized single domain antibodies (sdAbs) from a synthetic library. These sdAbs reveal binding kinetics with the equilibrium dissociation constant (K(D)) of 0.99-35.5 nM. The monomeric sdAbs show half maximal neutralization concentration (EC(50)) of 0.0009-0.07 microg/mL and 0.13-0.51 microg/mL against SARS-CoV-2 pseudotypes, and authentic SARS-CoV-2, respectively. Competitive ligand-binding experiments suggest that the sdAbs either completely block or significantly inhibit the association between SARS-CoV-2 RBD and viral entry receptor ACE2. Fusion of the human IgG1 Fc to sdAbs improve their neutralization activity by up to ten times. These results support neutralizing sdAbs as a potential alternative for antiviral therapies. Twit Text FOAVip Humanized single domain antibodies neutralize SARS-CoV-2 by targeting the spike receptor binding domain ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=32913273 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32913273 #FOAvip English Wikipedia <ref>{{Cite pmid|32913273}}</ref> Humanized single domain antibodies neutralize SARS-CoV-2 by targeting the spike receptor binding domain #MMPMID32913273 Chi X; Liu X; Wang C; Zhang X; Li X; Hou J; Ren L; Jin Q; Wang J; Yang W Nat Commun 2020[Sep]; 11 (1): 4528 PMID32913273show ga Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spreads worldwide and leads to an unprecedented medical burden and lives lost. Neutralizing antibodies provide efficient blockade for viral infection and are a promising category of biological therapies. Here, using SARS-CoV-2 spike receptor-binding domain (RBD) as a bait, we generate a panel of humanized single domain antibodies (sdAbs) from a synthetic library. These sdAbs reveal binding kinetics with the equilibrium dissociation constant (K(D)) of 0.99-35.5 nM. The monomeric sdAbs show half maximal neutralization concentration (EC(50)) of 0.0009-0.07 microg/mL and 0.13-0.51 microg/mL against SARS-CoV-2 pseudotypes, and authentic SARS-CoV-2, respectively. Competitive ligand-binding experiments suggest that the sdAbs either completely block or significantly inhibit the association between SARS-CoV-2 RBD and viral entry receptor ACE2. Fusion of the human IgG1 Fc to sdAbs improve their neutralization activity by up to ten times. These results support neutralizing sdAbs as a potential alternative for antiviral therapies. |Angiotensin-Converting Enzyme 2[MESH] |Animals[MESH] |Antibodies, Neutralizing/*immunology/pharmacology[MESH] |COVID-19[MESH] |Chlorocebus aethiops[MESH] |Coronavirus Infections/drug therapy/*virology[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Immunoglobulin G[MESH] |Models, Molecular[MESH] |Pandemics[MESH] |Peptidyl-Dipeptidase A/metabolism[MESH] |Pneumonia, Viral/drug therapy/*virology[MESH] |Protein Binding[MESH] |Receptors, Virus/immunology[MESH] |Single-Domain Antibodies/*immunology/pharmacology[MESH] |Spike Glycoprotein, Coronavirus/*immunology/metabolism[MESH]Humanized single domain antibodies neutralize SARS-CoV-2 by targeting (epmc).pdf DeepDyve Pubget Overpricing