PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3643213-5	1987	A specific, metal ion-independent interaction between Ba and C3b was subsequently demonstrated by use of the cross-linking reagent dithiobis(succinimidyl propionate).	Barium	54-56	complement C3	Homo sapiens	61-64	
35420644-8	2022	In all patients, aqueous Ba, C3a, and albumin levels were strongly correlated with vitreous levels (Spearman correlation coefficient of 0.8 for Ba and C3a and 0.7 for albumin; all P values < 0.0001).	Barium	25-27	complement C3	Homo sapiens	151-154	
2433342-11	1987	The data suggest that a binding site for C3b on intact B is located on the Ba portion of the molecule.	Barium	75-77	complement C3	Homo sapiens	41-44	
3643213-7	1987	In contrast, most of the Ba fragment undergoes rapid dissociation, but there is also evidence to suggest the establishment of a new equilibrium due to the ability of Ba to rebind to C3b.	Barium	166-168	complement C3	Homo sapiens	182-185	
3159752-3	1985	C3b,Bb formation was measured by the concentration of Ba, released when C3b,B is activated.	Barium	54-56	complement C3	Homo sapiens	0-3	
3159752-3	1985	C3b,Bb formation was measured by the concentration of Ba, released when C3b,B is activated.	Barium	54-56	complement C3	Homo sapiens	72-75	
10966820-1	2000	Factor B is a key component of the alternative pathway of complement and is cleaved by factor D into the Ba and Bb fragments in the presence of activated C3 (C3b or C3(H(2)O)).	Barium	105-107	complement C3	Homo sapiens	154-156	
10966820-1	2000	Factor B is a key component of the alternative pathway of complement and is cleaved by factor D into the Ba and Bb fragments in the presence of activated C3 (C3b or C3(H(2)O)).	Barium	105-107	complement C3	Homo sapiens	158-161	
10966820-1	2000	Factor B is a key component of the alternative pathway of complement and is cleaved by factor D into the Ba and Bb fragments in the presence of activated C3 (C3b or C3(H(2)O)).	Barium	105-107	complement C3	Homo sapiens	165-174