PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33406838-0 2021 N- and O-Glycosylation of the SARS-CoV-2 Spike Protein. Nitrogen 0-1 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 41-46 33578036-0 2021 Nanoluciferase complementation-based bioreporter reveals the importance of N-linked glycosylation of SARS-CoV-2 Spike for viral entry. Nitrogen 0-1 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 112-117 32518941-0 2021 Identification of 22 N-glycosites on spike glycoprotein of SARS-CoV-2 and accessible surface glycopeptide motifs: Implications for vaccination and antibody therapeutics. Nitrogen 21-22 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 37-42 33377107-1 2020 This protocol describes an integrated approach for analyzing site-specific N- and O-linked glycosylation of SARS-CoV-2 spike protein by mass spectrometry. Nitrogen 75-76 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 119-124 33409271-3 2020 The receptor-binding domain (RBD) of the 2019-nCoV spike (S) protein contains disulfide bonds and N-linked glycosylations, therefore, it is typically produced by secretion. Nitrogen 98-99 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 51-56 33409271-3 2020 The receptor-binding domain (RBD) of the 2019-nCoV spike (S) protein contains disulfide bonds and N-linked glycosylations, therefore, it is typically produced by secretion. Nitrogen 98-99 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 58-59 32363391-0 2020 Deducing the N- and O-glycosylation profile of the spike protein of novel coronavirus SARS-CoV-2. Nitrogen 13-14 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 51-56 32363391-3 2020 The spike protein is comprised of two protein subunits (S1 and S2), which together possess 22 potential N-glycosylation sites. Nitrogen 104-105 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 4-9 32363391-5 2020 We have characterized the quantitative N-glycosylation profile on spike protein and interestingly, observed unexpected O-glycosylation modifications on the receptor-binding domain of spike protein subunit S1. Nitrogen 39-40 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 66-71 32363391-5 2020 We have characterized the quantitative N-glycosylation profile on spike protein and interestingly, observed unexpected O-glycosylation modifications on the receptor-binding domain of spike protein subunit S1. Nitrogen 39-40 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 183-188 32363391-7 2020 Our data on the N- and O-glycosylation are strengthened by extensive manual interpretation of each glycopeptide spectra in addition to using bioinformatics tools to confirm the complexity of glycosylation in the spike protein. Nitrogen 16-17 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 212-217 33064451-3 2020 We conducted a comprehensive mass spectrometric analysis of the N-glycosylation profiles of the SARS-CoV-2 spike proteins using signature ions-triggered electron-transfer/higher-energy collision dissociation (EThcD) mass spectrometry. Nitrogen 64-65 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 107-112 33232205-3 2020 By using a panel of rabbit antisera against virions and five structural proteins together with a convalescent serum, the spike (S) glycoprotein was shown to be N-linked glycosylated, PNGase F-sensitive, endoglycosidase H-resistant and cleaved by Furin-like proteases into S1 and S2 subunits. Nitrogen 160-161 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 121-126 33064451-4 2020 The patterns of N-glycosylation within the recombinant ectodomain and S1 subunit of the SARS-CoV-2 spike protein were characterized using this approach. Nitrogen 16-17 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 99-104 34661088-0 2021 The effect of N-glycosylation of SARS-CoV-2 spike protein on the virus interaction with the host cell ACE2 receptor. Nitrogen 14-15 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 44-49 33077685-0 2021 Site-specific N-glycosylation Characterization of Recombinant SARS-CoV-2 Spike Proteins. Nitrogen 14-15 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 73-78 32944295-3 2020 We model the trimeric Spike protein, including flexible loops and all N-glycosylation sites, in order to elucidate accessible epitopes for antibody-based diagnostics, therapeutics and vaccine development. Nitrogen 70-71 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 22-27 32404529-6 2020 Some ACE2 proteins even tolerate the loss or acquisition of N-glycosylation sites located near the S interface. Nitrogen 60-61 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 0-1 34876606-0 2021 N-glycosylation profiles of the SARS-CoV-2 spike D614G mutant and its ancestral protein characterized by advanced mass spectrometry. Nitrogen 0-1 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 43-48 34876606-4 2021 In this report, we used mass spectrometry techniques to characterize and compare the N-glycosylation of the wild type (S-614D) or variant (S-614G) SARS-CoV-2 spike glycoproteins prepared under identical conditions. Nitrogen 85-86 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 158-163 34839261-9 2021 FINDINGS: The receptor binding domain and three distinct SARS-CoV-2 surface N-glycosylation sites among 57,311 spike proteins retrieved from the NCBI-Virus-database are highly evolutionarily conserved (99.67%) and are involved in ACE2 interaction. Nitrogen 76-77 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 111-116 34869209-1 2021 The SARS-CoV-2 spike protein is heavily glycosylated, having 22 predicted N-glycosylation sites per monomer. Nitrogen 74-75 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 15-20 34869209-10 2021 Comparison of the whole cell-derived WA1 and D614G spike proteins revealed that N-glycosites local to the mutation site appeared to be more readily detected, hinting that these sites are more exposed to glycosylation machinery. Nitrogen 80-81 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 51-56 34327998-8 2021 Comparisons of GADS for N-glycosylated sites on several proteins, especially the SARS-CoV-2 spike protein, demonstrate the potential reproducibility of GADS and their utility for comparing site-specific distributions. Nitrogen 24-25 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 92-97 34494876-11 2021 Finally, we found that hACE2 N-glycosylation is required for an efficient viral entry of SARS-CoV/SARS-CoV-2 S pseudotyped viruses, which may be the result of low cell surface expression of the deglycosylated ACE2 receptor. Nitrogen 29-30 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 109-110 34631661-7 2021 We identified 21 and 19 out of the 22 predicted N-glycosites of the SARS-CoV-2 S proteins produced in CHO and HEK, respectively. Nitrogen 48-49 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 79-80 35164559-1 2022 Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) extensively N-glycosylates its spike proteins, which are necessary for host cell invasion and the target of both vaccines and immunotherapies. Nitrogen 73-74 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 92-97