PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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