PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9633924-3	1998	The inhibitory effects of HDL3 on inositol 1,4,5-tris-phosphate formation and intracellular calcium mobilization were abolished after covalent modification of HDL3 with dimethylsuberimidate.	Dimethyl Suberimidate	169-189	HDL3	Homo sapiens	26-30	
9633924-3	1998	The inhibitory effects of HDL3 on inositol 1,4,5-tris-phosphate formation and intracellular calcium mobilization were abolished after covalent modification of HDL3 with dimethylsuberimidate.	Dimethyl Suberimidate	169-189	HDL3	Homo sapiens	159-163	
1466659-2	1992	Cholesterol-loaded cells interacted with native apolipoprotein (apo) E-free high density lipoprotein3 (HDL)3 as well as with dimethyl suberimidate-modified HDL3 (DMS-HDL3).	Dimethyl Suberimidate	125-146	HDL3	Homo sapiens	156-160	
1466659-2	1992	Cholesterol-loaded cells interacted with native apolipoprotein (apo) E-free high density lipoprotein3 (HDL)3 as well as with dimethyl suberimidate-modified HDL3 (DMS-HDL3).	Dimethyl Suberimidate	125-146	HDL3	Homo sapiens	166-170	
1892880-4	1991	At identical concentrations, HDL3 and dimethylsuberimidate treated-HDL3 promoted similar efflux, suggesting that efflux did not depend on specific binding of HDL3 to the cell surface.	Dimethyl Suberimidate	38-58	HDL3	Homo sapiens	67-71	
1892880-4	1991	At identical concentrations, HDL3 and dimethylsuberimidate treated-HDL3 promoted similar efflux, suggesting that efflux did not depend on specific binding of HDL3 to the cell surface.	Dimethyl Suberimidate	38-58	HDL3	Homo sapiens	67-71	
3379343-9	1988	To determine the role of cross-linking of apoproteins to each other in the inhibition, we used the bifunctional reagent dimethylsuberimidate (DMS) to cross-link the apoproteins in HDL3.	Dimethyl Suberimidate	120-140	HDL3	Homo sapiens	180-184	
3379343-9	1988	To determine the role of cross-linking of apoproteins to each other in the inhibition, we used the bifunctional reagent dimethylsuberimidate (DMS) to cross-link the apoproteins in HDL3.	Dimethyl Suberimidate	142-145	HDL3	Homo sapiens	180-184	
8743192-6	1996	Furthermore, the effect of HDL3 was abolished after covalent modification of HDL3 with dimethylsuberimidate and was not observed in platelets from Glanzmann thrombasthenia type 1 which do not express GP IIb/IIIa, as well as in platelets preincubated with anti-GP IIb/IIIa polyclonal antibodies.	Dimethyl Suberimidate	87-107	HDL3	Homo sapiens	27-31	
8743192-6	1996	Furthermore, the effect of HDL3 was abolished after covalent modification of HDL3 with dimethylsuberimidate and was not observed in platelets from Glanzmann thrombasthenia type 1 which do not express GP IIb/IIIa, as well as in platelets preincubated with anti-GP IIb/IIIa polyclonal antibodies.	Dimethyl Suberimidate	87-107	HDL3	Homo sapiens	77-81	
1402404-7	1992	Efflux mediated by dimethyl suberimidate-treated HDL3, which does not interact with high affinity HDL receptors, was similar to efflux induced by native HDL3 after all fatty acid treatments.	Dimethyl Suberimidate	19-40	HDL3	Homo sapiens	49-53	
1930148-7	1991	Covalent modification of the apoproteins of HDL3 with dimethyl suberimidate or tetranitromethane did not inhibit the HDL3-induced rise in [Ca2+]i.	Dimethyl Suberimidate	54-75	HDL3	Homo sapiens	44-48	
2397248-2	1990	The labeled HDL3 was modified by cross-linking of apoproteins with dimethylsuberimidate (DMS) to inhibit binding to HDL specific receptors.	Dimethyl Suberimidate	67-87	HDL3	Homo sapiens	12-16	
2397248-2	1990	The labeled HDL3 was modified by cross-linking of apoproteins with dimethylsuberimidate (DMS) to inhibit binding to HDL specific receptors.	Dimethyl Suberimidate	89-92	HDL3	Homo sapiens	12-16