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.

10.1021/acsmedchemlett.1c00343 http://scihub22266oqcxt.onion/10.1021/acsmedchemlett.1c00343 34786180!8525342!34786180     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       ACS+Med+Chem+Lett 2021 ; 12 (11): 1710-1717 Nephropedia Template TP {{tp|p=34786180|t=2021. On the Selectivity of Heparan Sulfate Recognition by SARS-CoV-2 Spike Glycoprotein |pdf=|usr=}}{{34786180}} gab.com Text On the Selectivity of Heparan Sulfate Recognition by SARS-CoV-2 Spike Glycoprotein JO: ACS Med Chem Lett http://www.kidney.de/pget.php?&tw=1&pmid=34786180 #FOAvip SARS-CoV-2 infects human cells through its surface spike glycoprotein (SgP), which relies on host cell surface heparan sulfate (HS) proteoglycans that facilitate interaction with the ACE2 receptor. Targeting this process could lead to inhibitors of early steps in viral entry. Screening a microarray of 24 HS oligosaccharides against recombinant S1 and receptor-binding domain (RBD) proteins led to identification of only eight sequences as potent antagonists; results that were supported by detailed dual-filter computational studies. Competitive studies using the HS microarray suggested almost equivalent importance of IdoA2S-GlcNS6S and GlcNS3S structures, which were supported by affinity studies. Exhaustive virtual screening on a library of >93?000 sequences led to a novel pharmacophore with at least two 3-O-sulfated GlcN residues that can engineer unique selectivity in recognizing the RBD. This work puts forward the key structural motif in HS that should lead to potent and selective HS or HS-like agents against SARS-CoV-2. Twit Text FOAVip On the Selectivity of Heparan Sulfate Recognition by SARS-CoV-2 Spike Glycoprotein ????ACS Med Chem Lett http://www.kidney.de/pget.php?&tw=1&pmid=34786180 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34786180 #FOAvip English Wikipedia <ref>{{Cite pmid|34786180}}</ref> On the Selectivity of Heparan Sulfate Recognition by SARS-CoV-2 Spike Glycoprotein #MMPMID34786180 Chittum JE; Sankaranarayanan NV; O'Hara CP; Desai UR ACS Med Chem Lett 2021[Nov]; 12 (11): 1710-1717 PMID34786180show ga SARS-CoV-2 infects human cells through its surface spike glycoprotein (SgP), which relies on host cell surface heparan sulfate (HS) proteoglycans that facilitate interaction with the ACE2 receptor. Targeting this process could lead to inhibitors of early steps in viral entry. Screening a microarray of 24 HS oligosaccharides against recombinant S1 and receptor-binding domain (RBD) proteins led to identification of only eight sequences as potent antagonists; results that were supported by detailed dual-filter computational studies. Competitive studies using the HS microarray suggested almost equivalent importance of IdoA2S-GlcNS6S and GlcNS3S structures, which were supported by affinity studies. Exhaustive virtual screening on a library of >93?000 sequences led to a novel pharmacophore with at least two 3-O-sulfated GlcN residues that can engineer unique selectivity in recognizing the RBD. This work puts forward the key structural motif in HS that should lead to potent and selective HS or HS-like agents against SARS-CoV-2. äOn the Selectivity of Heparan Sulfate Recognition by SARS-CoV-2 Spike (epmc).pdf DeepDyve Pubget Overpricing