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.abb9983 http://scihub22266oqcxt.onion/10.1126/science.abb9983 32366695!7199903!32366695     free     free     free       Science 2020 ; 369 (6501): 330-333 Nephropedia Template TP {{tp|p=32366695|t=2020. Site-specific glycan analysis of the SARS-CoV-2 spike |pdf=|usr=}}{{32366695}} gab.com Text Site-specific glycan analysis of the SARS-CoV-2 spike JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=32366695 #FOAvip The emergence of the betacoronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of coronavirus disease 2019 (COVID-19), represents a considerable threat to global human health. Vaccine development is focused on the principal target of the humoral immune response, the spike (S) glycoprotein, which mediates cell entry and membrane fusion. The SARS-CoV-2 S gene encodes 22 N-linked glycan sequons per protomer, which likely play a role in protein folding and immune evasion. Here, using a site-specific mass spectrometric approach, we reveal the glycan structures on a recombinant SARS-CoV-2 S immunogen. This analysis enables mapping of the glycan-processing states across the trimeric viral spike. We show how SARS-CoV-2 S glycans differ from typical host glycan processing, which may have implications in viral pathobiology and vaccine design. Twit Text FOAVip Site-specific glycan analysis of the SARS-CoV-2 spike ????Science http://www.kidney.de/pget.php?&tw=1&pmid=32366695 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32366695 #FOAvip English Wikipedia <ref>{{Cite pmid|32366695}}</ref> Site-specific glycan analysis of the SARS-CoV-2 spike #MMPMID32366695 Watanabe Y; Allen JD; Wrapp D; McLellan JS; Crispin M Science 2020[Jul]; 369 (6501): 330-333 PMID32366695show ga The emergence of the betacoronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of coronavirus disease 2019 (COVID-19), represents a considerable threat to global human health. Vaccine development is focused on the principal target of the humoral immune response, the spike (S) glycoprotein, which mediates cell entry and membrane fusion. The SARS-CoV-2 S gene encodes 22 N-linked glycan sequons per protomer, which likely play a role in protein folding and immune evasion. Here, using a site-specific mass spectrometric approach, we reveal the glycan structures on a recombinant SARS-CoV-2 S immunogen. This analysis enables mapping of the glycan-processing states across the trimeric viral spike. We show how SARS-CoV-2 S glycans differ from typical host glycan processing, which may have implications in viral pathobiology and vaccine design. |Betacoronavirus/*chemistry[MESH] |Binding Sites[MESH] |COVID-19[MESH] |Coronavirus Infections[MESH] |Glycopeptides/chemistry/immunology[MESH] |Glycosylation[MESH] |Humans[MESH] |Mass Spectrometry[MESH] |Models, Molecular[MESH] |Oligosaccharides/chemistry[MESH] |Pandemics[MESH] |Pneumonia, Viral[MESH] |Polysaccharides/*chemistry[MESH] |Protein Structure, Tertiary[MESH] |Recombinant Proteins/chemistry/immunology[MESH] |SARS-CoV-2[MESH]Site-specific glycan analysis of the SARS-CoV-2 spike (epmc).pdf DeepDyve Pubget Overpricing