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.

10.3390/ijms22052268 http://scihub22266oqcxt.onion/10.3390/ijms22052268 33668756!7956771!33668756     free     free     free Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\33668756.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Int+J+Mol+Sci 2021 ; 22 (5): ä Nephropedia Template TP {{tp|p=33668756|t=2021. Characterization of Critical Determinants of ACE2-SARS CoV-2 RBD Interaction |pdf=|usr=}}{{33668756}} gab.com Text Characterization of Critical Determinants of ACE2-SARS CoV-2 RBD Interaction JO: Int J Mol Sci http://www.kidney.de/pget.php?&tw=1&pmid=33668756 #FOAvip Despite sequence similarity to SARS-CoV-1, SARS-CoV-2 has demonstrated greater widespread virulence and unique challenges to researchers aiming to study its pathogenicity in humans. The interaction of the viral receptor binding domain (RBD) with its main host cell receptor, angiotensin-converting enzyme 2 (ACE2), has emerged as a critical focal point for the development of anti-viral therapeutics and vaccines. In this study, we selectively identify and characterize the impact of mutating certain amino acid residues in the RBD of SARS-CoV-2 and in ACE2, by utilizing our recently developed NanoBiT technology-based biosensor as well as pseudotyped-virus infectivity assays. Specifically, we examine the mutational effects on RBD-ACE2 binding ability, efficacy of competitive inhibitors, as well as neutralizing antibody activity. We also look at the implications the mutations may have on virus transmissibility, host susceptibility, and the virus transmission path to humans. These critical determinants of virus-host interactions may provide more effective targets for ongoing vaccines, drug development, and potentially pave the way for determining the genetic variation underlying disease severity. Twit Text FOAVip Characterization of Critical Determinants of ACE2-SARS CoV-2 RBD Interaction ????Int J Mol Sci http://www.kidney.de/pget.php?&tw=1&pmid=33668756 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33668756 #FOAvip English Wikipedia <ref>{{Cite pmid|33668756}}</ref> Characterization of Critical Determinants of ACE2-SARS CoV-2 RBD Interaction #MMPMID33668756 Brown EEF; Rezaei R; Jamieson TR; Dave J; Martin NT; Singaravelu R; Crupi MJF; Boulton S; Tucker S; Duong J; Poutou J; Pelin A; Yasavoli-Sharahi H; Taha Z; Arulanandam R; Surendran A; Ghahremani M; Austin B; Matar C; Diallo JS; Bell JC; Ilkow CS; Azad T Int J Mol Sci 2021[Feb]; 22 (5): ä PMID33668756show ga Despite sequence similarity to SARS-CoV-1, SARS-CoV-2 has demonstrated greater widespread virulence and unique challenges to researchers aiming to study its pathogenicity in humans. The interaction of the viral receptor binding domain (RBD) with its main host cell receptor, angiotensin-converting enzyme 2 (ACE2), has emerged as a critical focal point for the development of anti-viral therapeutics and vaccines. In this study, we selectively identify and characterize the impact of mutating certain amino acid residues in the RBD of SARS-CoV-2 and in ACE2, by utilizing our recently developed NanoBiT technology-based biosensor as well as pseudotyped-virus infectivity assays. Specifically, we examine the mutational effects on RBD-ACE2 binding ability, efficacy of competitive inhibitors, as well as neutralizing antibody activity. We also look at the implications the mutations may have on virus transmissibility, host susceptibility, and the virus transmission path to humans. These critical determinants of virus-host interactions may provide more effective targets for ongoing vaccines, drug development, and potentially pave the way for determining the genetic variation underlying disease severity. |Amino Acid Sequence[MESH] |Angiotensin-Converting Enzyme 2/*chemistry/genetics/*metabolism[MESH] |Antibodies, Neutralizing/immunology[MESH] |Antiviral Agents/pharmacology[MESH] |Binding Sites[MESH] |COVID-19 Drug Treatment[MESH] |COVID-19/immunology/*metabolism/*virology[MESH] |HEK293 Cells[MESH] |Host Microbial Interactions[MESH] |Humans[MESH] |Models, Molecular[MESH] |Mutation[MESH] |Protein Binding[MESH] |Protein Interaction Domains and Motifs[MESH] |Receptors, Virus/chemistry/metabolism[MESH] |SARS-CoV-2/drug effects/*metabolism[MESH] |Sequence Alignment[MESH]Characterization of Critical Determinants of ACE2-SARS CoV-2 RBD Inter(epmc).pdf DeepDyve Pubget Overpricing