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10.1093/glycob/cwaa085 http://scihub22266oqcxt.onion/10.1093/glycob/cwaa085 32886791!7499654!32886791     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Glycobiology 2021 ; 31 (3): 181-187 Nephropedia Template TP {{tp|p=32886791|t=2021. Site-specific characterization of SARS-CoV-2 spike glycoprotein receptor-binding domain |pdf=|usr=}}{{32886791}} gab.com Text Site-specific characterization of SARS-CoV-2 spike glycoprotein receptor-binding domain JO: Glycobiology http://www.kidney.de/pget.php?&tw=1&pmid=32886791 #FOAvip The novel coronavirus SARS-CoV-2, the infective agent causing COVID-19, is having a global impact both in terms of human disease as well as socially and economically. Its heavily glycosylated spike glycoprotein is fundamental for the infection process, via its receptor-binding domains interaction with the glycoprotein angiotensin-converting enzyme 2 on human cell surfaces. We therefore utilized an integrated glycomic and glycoproteomic analytical strategy to characterize both N- and O- glycan site-specific glycosylation within the receptor-binding domain. We demonstrate the presence of complex-type N-glycans with unusual fucosylated LacdiNAc at both sites N331 and N343 and a single site of O-glycosylation on T323. Twit Text FOAVip Site-specific characterization of SARS-CoV-2 spike glycoprotein receptor-binding domain ????Glycobiology http://www.kidney.de/pget.php?&tw=1&pmid=32886791 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32886791 #FOAvip English Wikipedia <ref>{{Cite pmid|32886791}}</ref> Site-specific characterization of SARS-CoV-2 spike glycoprotein receptor-binding domain #MMPMID32886791 Antonopoulos A; Broome S; Sharov V; Ziegenfuss C; Easton RL; Panico M; Dell A; Morris HR; Haslam SM Glycobiology 2021[Apr]; 31 (3): 181-187 PMID32886791show ga The novel coronavirus SARS-CoV-2, the infective agent causing COVID-19, is having a global impact both in terms of human disease as well as socially and economically. Its heavily glycosylated spike glycoprotein is fundamental for the infection process, via its receptor-binding domains interaction with the glycoprotein angiotensin-converting enzyme 2 on human cell surfaces. We therefore utilized an integrated glycomic and glycoproteomic analytical strategy to characterize both N- and O- glycan site-specific glycosylation within the receptor-binding domain. We demonstrate the presence of complex-type N-glycans with unusual fucosylated LacdiNAc at both sites N331 and N343 and a single site of O-glycosylation on T323. |*SARS-CoV-2/chemistry/genetics/metabolism[MESH] |Angiotensin-Converting Enzyme 2/chemistry/metabolism[MESH] |Binding Sites/genetics[MESH] |COVID-19/metabolism/*virology[MESH] |Carbohydrate Conformation[MESH] |Carbohydrate Sequence[MESH] |Glycomics[MESH] |Glycosylation[MESH] |HEK293 Cells[MESH] |Host Microbial Interactions[MESH] |Humans[MESH] |Pandemics[MESH] |Protein Binding[MESH] |Protein Interaction Domains and Motifs[MESH] |Proteomics[MESH] |Receptors, Virus/chemistry/metabolism[MESH] |Recombinant Proteins/chemistry/genetics/metabolism[MESH] |Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization[MESH]Site-specific characterization of SARS-CoV-2 spike glycoprotein recept(epmc).pdf DeepDyve Pubget Overpricing