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.

10.1126/science.abd0826 http://scihub22266oqcxt.onion/10.1126/science.abd0826 32703906!7402631!32703906     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       Science 2020 ; 369 (6510): 1501-1505 Nephropedia Template TP {{tp|p=32703906|t=2020. Structure-based design of prefusion-stabilized SARS-CoV-2 spikes |pdf=|usr=}}{{32703906}} gab.com Text Structure-based design of prefusion-stabilized SARS-CoV-2 spikes JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=32703906 #FOAvip The coronavirus disease 2019 (COVID-19) pandemic has led to accelerated efforts to develop therapeutics and vaccines. A key target of these efforts is the spike (S) protein, which is metastable and difficult to produce recombinantly. We characterized 100 structure-guided spike designs and identified 26 individual substitutions that increased protein yields and stability. Testing combinations of beneficial substitutions resulted in the identification of HexaPro, a variant with six beneficial proline substitutions exhibiting higher expression than its parental construct (by a factor of 10) as well as the ability to withstand heat stress, storage at room temperature, and three freeze-thaw cycles. A cryo-electron microscopy structure of HexaPro at a resolution of 3.2 angstroms confirmed that it retains the prefusion spike conformation. High-yield production of a stabilized prefusion spike protein will accelerate the development of vaccines and serological diagnostics for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Twit Text FOAVip Structure-based design of prefusion-stabilized SARS-CoV-2 spikes ????Science http://www.kidney.de/pget.php?&tw=1&pmid=32703906 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32703906 #FOAvip English Wikipedia <ref>{{Cite pmid|32703906}}</ref> Structure-based design of prefusion-stabilized SARS-CoV-2 spikes #MMPMID32703906 Hsieh CL; Goldsmith JA; Schaub JM; DiVenere AM; Kuo HC; Javanmardi K; Le KC; Wrapp D; Lee AG; Liu Y; Chou CW; Byrne PO; Hjorth CK; Johnson NV; Ludes-Meyers J; Nguyen AW; Park J; Wang N; Amengor D; Lavinder JJ; Ippolito GC; Maynard JA; Finkelstein IJ; McLellan JS Science 2020[Sep]; 369 (6510): 1501-1505 PMID32703906show ga The coronavirus disease 2019 (COVID-19) pandemic has led to accelerated efforts to develop therapeutics and vaccines. A key target of these efforts is the spike (S) protein, which is metastable and difficult to produce recombinantly. We characterized 100 structure-guided spike designs and identified 26 individual substitutions that increased protein yields and stability. Testing combinations of beneficial substitutions resulted in the identification of HexaPro, a variant with six beneficial proline substitutions exhibiting higher expression than its parental construct (by a factor of 10) as well as the ability to withstand heat stress, storage at room temperature, and three freeze-thaw cycles. A cryo-electron microscopy structure of HexaPro at a resolution of 3.2 angstroms confirmed that it retains the prefusion spike conformation. High-yield production of a stabilized prefusion spike protein will accelerate the development of vaccines and serological diagnostics for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). |*Amino Acid Substitution[MESH] |Betacoronavirus/*chemistry[MESH] |COVID-19 Vaccines[MESH] |Coronavirus Infections/prevention & control[MESH] |Cryoelectron Microscopy[MESH] |Humans[MESH] |Proline/chemistry[MESH] |Protein Domains[MESH] |Protein Stability[MESH] |SARS-CoV-2[MESH] |Spike Glycoprotein, Coronavirus/*chemistry[MESH]Structure-based design of prefusion-stabilized SARS-CoV-2 spikes (epmc).pdf DeepDyve Pubget Overpricing