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10.1016/j.cell.2021.02.032 http://scihub22266oqcxt.onion/10.1016/j.cell.2021.02.032 33756110!7891125!33756110     free     free     free 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       Cell 2021 ; 184 (8): 2183-2200.e22 Nephropedia Template TP {{tp|p=33756110|t=2021. The antigenic anatomy of SARS-CoV-2 receptor binding domain |pdf=|usr=}}{{33756110}} gab.com Text The antigenic anatomy of SARS-CoV-2 receptor binding domain JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=33756110 #FOAvip Antibodies are crucial to immune protection against SARS-CoV-2, with some in emergency use as therapeutics. Here, we identify 377 human monoclonal antibodies (mAbs) recognizing the virus spike and focus mainly on 80 that bind the receptor binding domain (RBD). We devise a competition data-driven method to map RBD binding sites. We find that although antibody binding sites are widely dispersed, neutralizing antibody binding is focused, with nearly all highly inhibitory mAbs (IC(50) < 0.1 mug/mL) blocking receptor interaction, except for one that binds a unique epitope in the N-terminal domain. Many of these neutralizing mAbs use public V-genes and are close to germline. We dissect the structural basis of recognition for this large panel of antibodies through X-ray crystallography and cryoelectron microscopy of 19 Fab-antigen structures. We find novel binding modes for some potently inhibitory antibodies and demonstrate that strongly neutralizing mAbs protect, prophylactically or therapeutically, in animal models. Twit Text FOAVip The antigenic anatomy of SARS-CoV-2 receptor binding domain ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=33756110 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33756110 #FOAvip English Wikipedia <ref>{{Cite pmid|33756110}}</ref> The antigenic anatomy of SARS-CoV-2 receptor binding domain #MMPMID33756110 Dejnirattisai W; Zhou D; Ginn HM; Duyvesteyn HME; Supasa P; Case JB; Zhao Y; Walter TS; Mentzer AJ; Liu C; Wang B; Paesen GC; Slon-Campos J; Lopez-Camacho C; Kafai NM; Bailey AL; Chen RE; Ying B; Thompson C; Bolton J; Fyfe A; Gupta S; Tan TK; Gilbert-Jaramillo J; James W; Knight M; Carroll MW; Skelly D; Dold C; Peng Y; Levin R; Dong T; Pollard AJ; Knight JC; Klenerman P; Temperton N; Hall DR; Williams MA; Paterson NG; Bertram FKR; Siebert CA; Clare DK; Howe A; Radecke J; Song Y; Townsend AR; Huang KA; Fry EE; Mongkolsapaya J; Diamond MS; Ren J; Stuart DI; Screaton GR Cell 2021[Apr]; 184 (8): 2183-2200.e22 PMID33756110show ga Antibodies are crucial to immune protection against SARS-CoV-2, with some in emergency use as therapeutics. Here, we identify 377 human monoclonal antibodies (mAbs) recognizing the virus spike and focus mainly on 80 that bind the receptor binding domain (RBD). We devise a competition data-driven method to map RBD binding sites. We find that although antibody binding sites are widely dispersed, neutralizing antibody binding is focused, with nearly all highly inhibitory mAbs (IC(50) < 0.1 mug/mL) blocking receptor interaction, except for one that binds a unique epitope in the N-terminal domain. Many of these neutralizing mAbs use public V-genes and are close to germline. We dissect the structural basis of recognition for this large panel of antibodies through X-ray crystallography and cryoelectron microscopy of 19 Fab-antigen structures. We find novel binding modes for some potently inhibitory antibodies and demonstrate that strongly neutralizing mAbs protect, prophylactically or therapeutically, in animal models. |Animals[MESH] |Antibodies, Monoclonal/*immunology[MESH] |Antibodies, Neutralizing/*immunology[MESH] |Antibodies, Viral/*immunology[MESH] |Binding Sites, Antibody[MESH] |CHO Cells[MESH] |COVID-19/*immunology[MESH] |Chlorocebus aethiops[MESH] |Cricetulus[MESH] |Epitopes[MESH] |Female[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Male[MESH] |Mice[MESH] |Mice, Transgenic[MESH] |Models, Molecular[MESH] |Protein Binding[MESH] |Protein Structure, Tertiary[MESH] |SARS-CoV-2/immunology[MESH] |Spike Glycoprotein, Coronavirus/*immunology[MESH]The antigenic anatomy of SARS-CoV-2 receptor binding domain (epmc).pdf DeepDyve Pubget Overpricing