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10.1038/s41598-021-88809-0 http://scihub22266oqcxt.onion/10.1038/s41598-021-88809-0 33958613!8102525!33958613     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 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       Sci+Rep 2021 ; 11 (1): 9682 Nephropedia Template TP {{tp|p=33958613|t=2021. Rapid development of neutralizing and diagnostic SARS-COV-2 mouse monoclonal antibodies |pdf=|usr=}}{{33958613}} gab.com Text Rapid development of neutralizing and diagnostic SARS-COV-2 mouse monoclonal antibodies JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=33958613 #FOAvip The need for high-affinity, SARS-CoV-2-specific monoclonal antibodies (mAbs) is critical in the face of the global COVID-19 pandemic, as such reagents can have important diagnostic, research, and therapeutic applications. Of greatest interest is the ~ 300 amino acid receptor binding domain (RBD) within the S1 subunit of the spike protein because of its key interaction with the human angiotensin converting enzyme 2 (hACE2) receptor present on many cell types, especially lung epithelial cells. We report here the development and functional characterization of 29 nM-affinity mouse SARS-CoV-2 mAbs created by an accelerated immunization and hybridoma screening process. Differing functions, including binding of diverse protein epitopes, viral neutralization, impact on RBD-hACE2 binding, and immunohistochemical staining of infected lung tissue, were correlated with variable gene usage and sequence. Twit Text FOAVip Rapid development of neutralizing and diagnostic SARS-COV-2 mouse monoclonal antibodies ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=33958613 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33958613 #FOAvip English Wikipedia <ref>{{Cite pmid|33958613}}</ref> Rapid development of neutralizing and diagnostic SARS-COV-2 mouse monoclonal antibodies #MMPMID33958613 Chapman AP; Tang X; Lee JR; Chida A; Mercer K; Wharton RE; Kainulainen M; Harcourt JL; Martines RB; Schroeder M; Zhao L; Bryksin A; Zhou B; Bergeron E; Bollweg BC; Tamin A; Thornburg N; Wentworth DE; Petway D; Bagarozzi DA Jr; Finn MG; Goldstein JM Sci Rep 2021[May]; 11 (1): 9682 PMID33958613show ga The need for high-affinity, SARS-CoV-2-specific monoclonal antibodies (mAbs) is critical in the face of the global COVID-19 pandemic, as such reagents can have important diagnostic, research, and therapeutic applications. Of greatest interest is the ~ 300 amino acid receptor binding domain (RBD) within the S1 subunit of the spike protein because of its key interaction with the human angiotensin converting enzyme 2 (hACE2) receptor present on many cell types, especially lung epithelial cells. We report here the development and functional characterization of 29 nM-affinity mouse SARS-CoV-2 mAbs created by an accelerated immunization and hybridoma screening process. Differing functions, including binding of diverse protein epitopes, viral neutralization, impact on RBD-hACE2 binding, and immunohistochemical staining of infected lung tissue, were correlated with variable gene usage and sequence. |Animals[MESH] |Antibodies, Monoclonal/*immunology[MESH] |Antibodies, Neutralizing/*immunology[MESH] |Antibodies, Viral/*immunology[MESH] |COVID-19 Serological Testing[MESH] |COVID-19/diagnosis/*immunology[MESH] |Epitopes/immunology[MESH] |Female[MESH] |Humans[MESH] |Immunization[MESH] |Mice[MESH] |Mice, Inbred BALB C[MESH] |Models, Molecular[MESH] |SARS-CoV-2/*immunology/isolation & purification[MESH]Rapid development of neutralizing and diagnostic SARS-COV-2 mouse mono(epmc).pdf DeepDyve Pubget Overpricing