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10.1039/d0bm01244k http://scihub22266oqcxt.onion/10.1039/d0bm01244k 33231598!?!33231598 Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=33231598&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Biomater+Sci 2020 ; 8 (23): 6603-6610 Nephropedia Template TP {{tp|p=33231598|t=2020. The biomaterial polyphosphate blocks stoichiometric binding of the SARS-CoV-2 S-protein to the cellular ACE2 receptor |pdf=|usr=}}{{33231598}} gab.com Text The biomaterial polyphosphate blocks stoichiometric binding of the SARS-CoV-2 S-protein to the cellular ACE2 receptor JO: Biomater Sci http://www.kidney.de/pget.php?&tw=1&pmid=33231598 #FOAvip The effect of the polyanionic polymer of inorganic polyphosphate (polyP) involved in innate immunity on the binding of the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein to the cellular ACE2 receptor was studied. The RBD surface comprises a basic amino acid stretch of four arginine residues which interact with the physiological polyP (polyP(40)) and polyP(3). Subsequently, the interaction of RBD with ACE2 is sensitively inhibited. After the chemical modification of arginine, an increased inhibition by polyP, at a 1 : 1 molar ratio (polyP : RBP), is measured already at 0.1 mug mL(-1). Heparin was ineffective. The results suggest a potential therapeutic benefit of polyP against SARS-CoV-2 infection. Twit Text FOAVip The biomaterial polyphosphate blocks stoichiometric binding of the SARS-CoV-2 S-protein to the cellular ACE2 receptor ????Biomater Sci http://www.kidney.de/pget.php?&tw=1&pmid=33231598 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33231598 #FOAvip English Wikipedia <ref>{{Cite pmid|33231598}}</ref> The biomaterial polyphosphate blocks stoichiometric binding of the SARS-CoV-2 S-protein to the cellular ACE2 receptor #MMPMID33231598 Muller WEG; Neufurth M; Schepler H; Wang S; Tolba E; Schroder HC; Wang X Biomater Sci 2020[Dec]; 8 (23): 6603-6610 PMID33231598show ga The effect of the polyanionic polymer of inorganic polyphosphate (polyP) involved in innate immunity on the binding of the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein to the cellular ACE2 receptor was studied. The RBD surface comprises a basic amino acid stretch of four arginine residues which interact with the physiological polyP (polyP(40)) and polyP(3). Subsequently, the interaction of RBD with ACE2 is sensitively inhibited. After the chemical modification of arginine, an increased inhibition by polyP, at a 1 : 1 molar ratio (polyP : RBP), is measured already at 0.1 mug mL(-1). Heparin was ineffective. The results suggest a potential therapeutic benefit of polyP against SARS-CoV-2 infection. |Angiotensin-Converting Enzyme 2/chemistry/*metabolism[MESH] |Antiviral Agents/chemistry/*pharmacology[MESH] |Binding Sites[MESH] |Humans[MESH] |Molecular Docking Simulation[MESH] |Polyelectrolytes[MESH] |Polymers/chemistry/*pharmacology[MESH] |Polyphosphates/chemistry/*pharmacology[MESH] |Protein Binding/drug effects[MESH]The biomaterial polyphosphate blocks stoichiometric binding of the SAR(epmc).pdf DeepDyve Pubget Overpricing