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.chembiol.2021.06.008 http://scihub22266oqcxt.onion/10.1016/j.chembiol.2021.06.008 34246414!8249686!34246414     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Chem+Biol 2022 ; 29 (1): 74-83.e4 Nephropedia Template TP {{tp|p=34246414|t=2022. SARS-COV-2 spike binding to ACE2 in living cells monitored by TR-FRET |pdf=|usr=}}{{34246414}} gab.com Text SARS-COV-2 spike binding to ACE2 in living cells monitored by TR-FRET JO: Cell Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=34246414 #FOAvip Targeting the interaction between the SARS-CoV-2 spike protein and human ACE2, its primary cell membrane receptor, is a promising therapeutic strategy to prevent viral entry. Recent in vitro studies revealed that the receptor binding domain (RBD) of the spike protein plays a prominent role in ACE2 binding, yet a simple and quantitative assay for monitoring this interaction in a cellular environment is lacking. Here, we developed an RBD-ACE2 binding assay that is based on time-resolved FRET, which reliably monitors the interaction in a physiologically relevant and cellular context. Because it is modular, the assay can monitor the impact of different cellular components, such as heparan sulfate, lipids, and membrane proteins on the RBD-ACE2 interaction and it can be extended to the full-length spike protein. The assay is HTS compatible and can detect small-molecule competitive and allosteric modulators of the RBD-ACE2 interaction with high relevance for SARS-CoV-2 therapeutics. Twit Text FOAVip SARS-COV-2 spike binding to ACE2 in living cells monitored by TR-FRET ????Cell Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=34246414 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34246414 #FOAvip English Wikipedia <ref>{{Cite pmid|34246414}}</ref> SARS-COV-2 spike binding to ACE2 in living cells monitored by TR-FRET #MMPMID34246414 Cecon E; Burridge M; Cao L; Carter L; Ravichandran R; Dam J; Jockers R Cell Chem Biol 2022[Jan]; 29 (1): 74-83.e4 PMID34246414show ga Targeting the interaction between the SARS-CoV-2 spike protein and human ACE2, its primary cell membrane receptor, is a promising therapeutic strategy to prevent viral entry. Recent in vitro studies revealed that the receptor binding domain (RBD) of the spike protein plays a prominent role in ACE2 binding, yet a simple and quantitative assay for monitoring this interaction in a cellular environment is lacking. Here, we developed an RBD-ACE2 binding assay that is based on time-resolved FRET, which reliably monitors the interaction in a physiologically relevant and cellular context. Because it is modular, the assay can monitor the impact of different cellular components, such as heparan sulfate, lipids, and membrane proteins on the RBD-ACE2 interaction and it can be extended to the full-length spike protein. The assay is HTS compatible and can detect small-molecule competitive and allosteric modulators of the RBD-ACE2 interaction with high relevance for SARS-CoV-2 therapeutics. |*Fluorescence Resonance Energy Transfer[MESH] |Angiotensin-Converting Enzyme 2/*chemistry[MESH] |Cells, Cultured[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Protein Binding[MESH] |Spike Glycoprotein, Coronavirus/*chemistry[MESH]SARS-COV-2 spike binding to ACE2 in living cells monitored by TR-FRET (epmc).pdf DeepDyve Pubget Overpricing