Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1038/s41594-020-0469-6 http://scihub22266oqcxt.onion/10.1038/s41594-020-0469-6 32661423!ä!32661423 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Struct+Mol+Biol 2020 ; 27 (9): 846-854 Nephropedia Template TP {{tp|p=32661423|t=2020. Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interaction with ACE2 |pdf=|usr=}}{{32661423}} gab.com Text Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interaction with ACE2 JO: Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=32661423 #FOAvip The SARS-CoV-2 virus is more transmissible than previous coronaviruses and causes a more serious illness than influenza. The SARS-CoV-2 receptor binding domain (RBD) of the spike protein binds to the human angiotensin-converting enzyme 2 (ACE2) receptor as a prelude to viral entry into the cell. Using a naive llama single-domain antibody library and PCR-based maturation, we have produced two closely related nanobodies, H11-D4 and H11-H4, that bind RBD (K(D) of 39 and 12 nM, respectively) and block its interaction with ACE2. Single-particle cryo-EM revealed that both nanobodies bind to all three RBDs in the spike trimer. Crystal structures of each nanobody-RBD complex revealed how both nanobodies recognize the same epitope, which partly overlaps with the ACE2 binding surface, explaining the blocking of the RBD-ACE2 interaction. Nanobody-Fc fusions showed neutralizing activity against SARS-CoV-2 (4-6 nM for H11-H4, 18 nM for H11-D4) and additive neutralization with the SARS-CoV-1/2 antibody CR3022. Twit Text FOAVip Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interaction with ACE2 ????Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=32661423 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32661423 #FOAvip English Wikipedia <ref>{{Cite pmid|32661423}}</ref> Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interaction with ACE2 #MMPMID32661423 Huo J; Le Bas A; Ruza RR; Duyvesteyn HME; Mikolajek H; Malinauskas T; Tan TK; Rijal P; Dumoux M; Ward PN; Ren J; Zhou D; Harrison PJ; Weckener M; Clare DK; Vogirala VK; Radecke J; Moynie L; Zhao Y; Gilbert-Jaramillo J; Knight ML; Tree JA; Buttigieg KR; Coombes N; Elmore MJ; Carroll MW; Carrique L; Shah PNM; James W; Townsend AR; Stuart DI; Owens RJ; Naismith JH Nat Struct Mol Biol 2020[Sep]; 27 (9): 846-854 PMID32661423show ga The SARS-CoV-2 virus is more transmissible than previous coronaviruses and causes a more serious illness than influenza. The SARS-CoV-2 receptor binding domain (RBD) of the spike protein binds to the human angiotensin-converting enzyme 2 (ACE2) receptor as a prelude to viral entry into the cell. Using a naive llama single-domain antibody library and PCR-based maturation, we have produced two closely related nanobodies, H11-D4 and H11-H4, that bind RBD (K(D) of 39 and 12 nM, respectively) and block its interaction with ACE2. Single-particle cryo-EM revealed that both nanobodies bind to all three RBDs in the spike trimer. Crystal structures of each nanobody-RBD complex revealed how both nanobodies recognize the same epitope, which partly overlaps with the ACE2 binding surface, explaining the blocking of the RBD-ACE2 interaction. Nanobody-Fc fusions showed neutralizing activity against SARS-CoV-2 (4-6 nM for H11-H4, 18 nM for H11-D4) and additive neutralization with the SARS-CoV-1/2 antibody CR3022. |*Coronavirus Infections[MESH] |*Pandemics[MESH] |*Pneumonia, Viral[MESH] |Amino Acid Sequence[MESH] |Angiotensin-Converting Enzyme 2[MESH] |Antibodies, Neutralizing/*immunology/metabolism/ultrastructure[MESH] |Antibodies, Viral/*immunology/metabolism/ultrastructure[MESH] |Antibody Affinity[MESH] |Antigen-Antibody Reactions/immunology[MESH] |Betacoronavirus/*immunology/metabolism[MESH] |Binding, Competitive[MESH] |COVID-19[MESH] |Cryoelectron Microscopy[MESH] |Crystallography, X-Ray[MESH] |Epitopes/immunology[MESH] |Humans[MESH] |Immunoglobulin Fc Fragments/genetics/immunology[MESH] |Models, Molecular[MESH] |Peptide Library[MESH] |Peptidyl-Dipeptidase A/*metabolism/ultrastructure[MESH] |Protein Binding[MESH] |Protein Conformation[MESH] |Receptors, Virus/*metabolism/ultrastructure[MESH] |Recombinant Fusion Proteins/immunology/metabolism[MESH] |SARS-CoV-2[MESH] |Sequence Homology, Amino Acid[MESH] |Single-Domain Antibodies/*immunology/metabolism/ultrastructure[MESH]Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interactio(epmc).pdf DeepDyve Pubget Overpricing