PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
33655075-0	2021	Correction to "The SARS-COV-2 Spike Protein Binds Sialic Acids, and Enables Rapid Detection in a Lateral Flow Point of Care Diagnostic Device".	Sialic Acids	50-62	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	30-35	
33909065-8	2021	Further, the ACE2 glycosylation mutants indicate that sialic acids on ACE2 receptor prevent ACE2-spike protein interaction.	Sialic Acids	54-66	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	97-102	
34572394-4	2021	Sialic acids binding to the N-terminal domain of the Spike protein are known to be crucial for viral entry into humans, and the role of Galectin-3 as a mediator of lung fibrosis has long been the object of study since its levels have been found to be abnormally high in alveolar macrophages following lung injury.	Sialic Acids	0-12	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	53-58	
33420022-4	2021	Next, we show that sialic acids present on ACE2 prevent efficient spike/ACE2-interaction.	Sialic Acids	19-31	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	66-71	
33269329-0	2020	The SARS-COV-2 Spike Protein Binds Sialic Acids and Enables Rapid Detection in a Lateral Flow Point of Care Diagnostic Device.	Sialic Acids	35-47	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	15-20	
32562764-3	2020	Furthermore, it is emphasized that the viral spike protein is prevented from binding gangliosides, which are composed of a glycosphingolipid with one or more sialic acids, in the presence of chloroquine or hydroxychloroquine.	Sialic Acids	158-170	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	45-50	
34506921-2	2021	Recent evidence suggests that along with angiotensin converting enzyme 2, certain cell surface sialic acids (Sia) may function as receptors for binding SARS-CoV-2 spike protein.	Sialic Acids	95-107	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	163-168	
34368076-0	2021	Identification of Potential Binding Sites of Sialic Acids on the RBD Domain of SARS-CoV-2 Spike Protein.	Sialic Acids	45-57	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	90-95	
34368076-4	2021	SARS-CoV-2 shares similar sequences of the spike protein with the Middle East Respiratory Syndrome Coronavirus (MERS-CoV), which can invade host cells by binding to either DPP4 or sialic acids.	Sialic Acids	180-192	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	43-48	
34368076-9	2021	This study shows that sialic acids can moderately interact with the spike protein of SARS-CoV-2 by binding between the two RBDs of the spike protein, indicating it could be a potential secondary or auxiliary receptor of SARS-CoV-2.	Sialic Acids	22-34	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	68-73	
34368076-9	2021	This study shows that sialic acids can moderately interact with the spike protein of SARS-CoV-2 by binding between the two RBDs of the spike protein, indicating it could be a potential secondary or auxiliary receptor of SARS-CoV-2.	Sialic Acids	22-34	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	135-140	
35191576-0	2022	The SARS-CoV-2 Spike Glycoprotein Directly Binds Exogeneous Sialic Acids:  A NMR View.	Sialic Acids	60-72	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	15-20	
35191576-2	2022	The NMR-based distinction between the signals of those sialic acids in the glycans covalently attached to the spike protein and those belonging to the exogenous a2,3 and a2,6 sialyl N-Acetyllactosamine ligands has been achieved by synthesizing uniformly 13C-labelled trisaccharides at the sialic acid and galactose moieties.	Sialic Acids	55-67	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	110-115