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10.1016/j.biopha.2020.110559 http://scihub22266oqcxt.onion/10.1016/j.biopha.2020.110559 32768882!7395593!32768882     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       Biomed+Pharmacother 2020 ; 130 (ä): 110559 Nephropedia Template TP {{tp|p=32768882|t=2020. Targeting SARS-CoV2 Spike Protein Receptor Binding Domain by Therapeutic Antibodies |pdf=|usr=}}{{32768882}} gab.com Text Targeting SARS-CoV2 Spike Protein Receptor Binding Domain by Therapeutic Antibodies JO: Biomed Pharmacother http://www.kidney.de/pget.php?&tw=1&pmid=32768882 #FOAvip As the number of people infected with the newly identified 2019 novel coronavirus (SARS-CoV2) is continuously increasing every day, development of potential therapeutic platforms is vital. Based on the comparatively high similarity of receptor-binding domain (RBD) in SARS-CoV2 and SARS-CoV, it seems crucial to assay the cross-reactivity of anti-SARS-CoV monoclonal antibodies (mAbs) with SARS-CoV2 spike (S)-protein. Indeed, developing mAbs targeting SARS-CoV2 S-protein RBD could show novel applications for rapid and sensitive development of potential epitope-specific vaccines (ESV). Herein, we present an overview on the discovery of new CoV followed by some explanation on the SARS-CoV2 S-protein RBD site. Furthermore, we surveyed the novel therapeutic mAbs for targeting S-protein RBD such as S230, 80R, F26G18, F26G19, CR3014, CR3022, M396, and S230.15. Afterwards, the mechanism of interaction of RBD and different mAbs were explained and it was suggested that one of the SARS-CoV-specific human mAbs, namely CR3022, could show the highest binding affinity with SARS-CoV2 S-protein RBD. Finally, some ongoing challenges and future prospects for rapid and sensitive advancement of therapeutic mAbs targeting S-protein RBD were discussed. In conclusion, it may be proposed that this review may pave the way for recognition of RBD and different mAbs to develop potential therapeutic ESV. Twit Text FOAVip Targeting SARS-CoV2 Spike Protein Receptor Binding Domain by Therapeutic Antibodies ????Biomed Pharmacother http://www.kidney.de/pget.php?&tw=1&pmid=32768882 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32768882 #FOAvip English Wikipedia <ref>{{Cite pmid|32768882}}</ref> Targeting SARS-CoV2 Spike Protein Receptor Binding Domain by Therapeutic Antibodies #MMPMID32768882 Hussain A; Hasan A; Nejadi Babadaei MM; Bloukh SH; Chowdhury MEH; Sharifi M; Haghighat S; Falahati M Biomed Pharmacother 2020[Oct]; 130 (ä): 110559 PMID32768882show ga As the number of people infected with the newly identified 2019 novel coronavirus (SARS-CoV2) is continuously increasing every day, development of potential therapeutic platforms is vital. Based on the comparatively high similarity of receptor-binding domain (RBD) in SARS-CoV2 and SARS-CoV, it seems crucial to assay the cross-reactivity of anti-SARS-CoV monoclonal antibodies (mAbs) with SARS-CoV2 spike (S)-protein. Indeed, developing mAbs targeting SARS-CoV2 S-protein RBD could show novel applications for rapid and sensitive development of potential epitope-specific vaccines (ESV). Herein, we present an overview on the discovery of new CoV followed by some explanation on the SARS-CoV2 S-protein RBD site. Furthermore, we surveyed the novel therapeutic mAbs for targeting S-protein RBD such as S230, 80R, F26G18, F26G19, CR3014, CR3022, M396, and S230.15. Afterwards, the mechanism of interaction of RBD and different mAbs were explained and it was suggested that one of the SARS-CoV-specific human mAbs, namely CR3022, could show the highest binding affinity with SARS-CoV2 S-protein RBD. Finally, some ongoing challenges and future prospects for rapid and sensitive advancement of therapeutic mAbs targeting S-protein RBD were discussed. In conclusion, it may be proposed that this review may pave the way for recognition of RBD and different mAbs to develop potential therapeutic ESV. |*Pandemics[MESH] |Amino Acid Sequence[MESH] |Antibodies, Monoclonal/chemistry/*immunology/metabolism[MESH] |Antibodies, Neutralizing/chemistry/*immunology/metabolism[MESH] |Antibodies, Viral/chemistry/*immunology/metabolism[MESH] |Antibody Affinity[MESH] |Antigen-Antibody Reactions[MESH] |Antigens, Viral/*immunology/metabolism[MESH] |Betacoronavirus/*immunology[MESH] |Binding Sites, Antibody[MESH] |COVID-19[MESH] |COVID-19 Vaccines[MESH] |Coronavirus Infections/*immunology/prevention & control[MESH] |Coronavirus/chemistry/immunology[MESH] |Epitopes/immunology[MESH] |Humans[MESH] |Models, Molecular[MESH] |Phylogeny[MESH] |Pneumonia, Viral/*immunology[MESH] |Protein Binding[MESH] |Protein Conformation[MESH] |Protein Domains[MESH] |SARS-CoV-2[MESH] |Sequence Alignment[MESH] |Sequence Homology, Amino Acid[MESH] |Spike Glycoprotein, Coronavirus/chemistry/*immunology/metabolism[MESH]Targeting SARS-CoV2 Spike Protein Receptor Binding Domain by Therapeut(epmc).pdf DeepDyve Pubget Overpricing