PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
32995772-3	2020	The furin cleavage product of SARS-CoV-2 Spike protein takes advantage of the vascular endothelial growth factor A (VEGF-A) binding site on NRP-1 which accommodates a polybasic stretch ending in a C-terminal arginine.	Arginine	208-216	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	41-46	
33162891-6	2020	We found 25 such arginine residues, including 2 in the spike protein and 10 in the nucleoprotein.	Arginine	17-25	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	55-60	
35231586-0	2022	Addition of arginine hydrochloride and proline to the culture medium enhances recombinant protein expression in Brevibacillus choshinensis: The case of RBD of SARS-CoV-2 spike protein and its antibody.	Arginine	12-34	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	170-175	
32362314-2	2020	The viral spike protein mediates SARS-CoV-2 entry into host cells and harbors a S1/S2 cleavage site containing multiple arginine residues (multibasic) not found in closely related animal coronaviruses.	Arginine	120-128	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	10-15	
33787218-3	2021	The furin cleavage product of SARS-CoV-2 Spike protein takes advantage of the vascular endothelial growth factor A (VEGF-A) binding site on NRP-1 which accommodates a polybasic stretch ending in a C-terminal arginine.	Arginine	208-216	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	41-46	
34960779-6	2021	This results in an optimized directionality of arginine residues involved in interaction of spike with the furin binding pocket, thus improving proteolytic exposure of the viral protein.	Arginine	47-55	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	92-97	
34722943-4	2021	SARS-CoV-2 S protein binds to neuropilin-1 (NRP1) by virtue of a CendR motif which terminates with either an arginine or lysine.	Arginine	109-117	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	11-12	
34200372-9	2021	A mutant form of the spike protein, lacking the arginine-rich putative furin cleavage site, interacted only weakly with cells and had a lower affinity for unfractionated and low-molecular-weight heparin than the wild-type spike protein.	Arginine	48-56	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	21-26	
34284575-0	2021	Comprehensive O-Glycosylation Analysis of the SARS-CoV-2 Spike Protein with Biomimetic Trp-Arg Materials.	Arginine	91-94	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	57-62	
35549865-9	2022	Of interest, restoration of NO by L-arginine may attenuate SARS-CoV-2 infection through different mechanisms, including reduction binding of SARS-CoV-2 to ACE2, inhibition of transmembrane protease serine type 2 (TMPRSS2) a critical for activation of SARS-CoV-2 spike protein and cellular entry, inhibition proliferation and replication of SARS-CoV-2, and prevention of SARS-CoV-2-induced coagulopathy.	Arginine	34-44	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	262-267	
35214759-5	2022	The study further shows the formation of dynamically interchangeable and persistent networks of salt-bridges at the Spike-Furin interface in SARS-CoV-2 involving the three arginines (R682, R683, R685) of the FLCSSpike with several anionic residues (E230, E236, D259, D264, D306) coming from Furin, strategically distributed around its catalytic triad.	Arginine	172-181	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	116-121	
35458513-3	2022	Accordingly, point mutations that result in an increase in electropositively charged residues, e.g., arginine and lysine, especially in the RBD of spike proteins in the SARS-CoV-2 variants, could contribute to their spreading capacity by favoring their recognition by the electronegatively charged ACE2 receptors.	Arginine	101-109	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	147-152	
35432786-6	2022	Additionally, semi-stable docking of bisartans at the arginine-rich furin-cleavage site of the SARS-CoV-2 spike protein (residues 681-686) required for virus entry into host cells, suggest bisartans may inhibit furin action thereby retarding viral entry into host cells.	Arginine	54-62	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	106-111