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.

10.1016/j.str.2021.05.014 http://scihub22266oqcxt.onion/10.1016/j.str.2021.05.014 34111408!8188728!34111408     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=34111408&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 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 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 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 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Structure 2021 ; 29 (7): 655-663.e4 Nephropedia Template TP {{tp|p=34111408|t=2021. Structural basis for accommodation of emerging B 1 351 and B 1 1 7 variants by two potent SARS-CoV-2 neutralizing antibodies |pdf=|usr=}}{{34111408}} gab.com Text Structural basis for accommodation of emerging B 1 351 and B 1 1 7 variants by two potent SARS-CoV-2 neutralizing antibodies JO: Structure http://www.kidney.de/pget.php?&tw=1&pmid=34111408 #FOAvip Emerging SARS-CoV-2 strains, B.1.1.7 and B.1.351, from the UK and South Africa, respectively, show decreased neutralization by monoclonal antibodies and convalescent or vaccinee sera raised against the original wild-type virus, and are thus of clinical concern. However, the neutralization potency of two antibodies, 1-57 and 2-7, which target the receptor-binding domain (RBD) of the spike, was unaffected by these emerging strains. Here, we report cryo-EM structures of 1-57 and 2-7 in complex with spike, revealing each of these antibodies to utilize a distinct mechanism to bypass or accommodate RBD mutations. Notably, each antibody represented an immune response with recognition distinct from those of frequent antibody classes. Moreover, many epitope residues recognized by 1-57 and 2-7 were outside hotspots of evolutionary pressure for ACE2 binding and neutralizing antibody escape. We suggest the therapeutic use of antibodies, such as 1-57 and 2-7, which target less prevalent epitopes, could ameliorate issues of monoclonal antibody escape. Twit Text FOAVip Structural basis for accommodation of emerging B 1 351 and B 1 1 7 variants by two potent SARS-CoV-2 neutralizing antibodies ????Structure http://www.kidney.de/pget.php?&tw=1&pmid=34111408 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34111408 #FOAvip English Wikipedia <ref>{{Cite pmid|34111408}}</ref> Structural basis for accommodation of emerging B 1 351 and B 1 1 7 variants by two potent SARS-CoV-2 neutralizing antibodies #MMPMID34111408 Cerutti G; Rapp M; Guo Y; Bahna F; Bimela J; Reddem ER; Yu J; Wang P; Liu L; Huang Y; Ho DD; Kwong PD; Sheng Z; Shapiro L Structure 2021[Jul]; 29 (7): 655-663.e4 PMID34111408show ga Emerging SARS-CoV-2 strains, B.1.1.7 and B.1.351, from the UK and South Africa, respectively, show decreased neutralization by monoclonal antibodies and convalescent or vaccinee sera raised against the original wild-type virus, and are thus of clinical concern. However, the neutralization potency of two antibodies, 1-57 and 2-7, which target the receptor-binding domain (RBD) of the spike, was unaffected by these emerging strains. Here, we report cryo-EM structures of 1-57 and 2-7 in complex with spike, revealing each of these antibodies to utilize a distinct mechanism to bypass or accommodate RBD mutations. Notably, each antibody represented an immune response with recognition distinct from those of frequent antibody classes. Moreover, many epitope residues recognized by 1-57 and 2-7 were outside hotspots of evolutionary pressure for ACE2 binding and neutralizing antibody escape. We suggest the therapeutic use of antibodies, such as 1-57 and 2-7, which target less prevalent epitopes, could ameliorate issues of monoclonal antibody escape. |Angiotensin-Converting Enzyme 2/*chemistry/genetics/immunology/metabolism[MESH] |Antibodies, Monoclonal/*chemistry/genetics/immunology/metabolism[MESH] |Antibodies, Neutralizing/*chemistry/genetics/immunology/metabolism[MESH] |Antibodies, Viral/*chemistry/genetics/immunology/metabolism[MESH] |Binding Sites[MESH] |Cloning, Molecular[MESH] |Cryoelectron Microscopy[MESH] |Epitopes/chemistry/genetics/immunology/metabolism[MESH] |Gene Expression[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Models, Molecular[MESH] |Mutation[MESH] |Protein Binding[MESH] |Protein Conformation, alpha-Helical[MESH] |Protein Conformation, beta-Strand[MESH] |Protein Interaction Domains and Motifs[MESH] |Receptors, Virus/*chemistry/genetics/immunology/metabolism[MESH] |Recombinant Proteins/chemistry/genetics/immunology/metabolism[MESH] |SARS-CoV-2/*chemistry/genetics/immunology/metabolism[MESH]Structural basis for accommodation of emerging B 1 351 and B 1 1 7 var(epmc).pdf DeepDyve Pubget Overpricing