PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2843239-4	1988	Modification of HDL3 by tetranitromethane (TNM) treatment, acetylation, reduction plus alkylation and 1,2-cyclohexanedione treatment derivatised tyrosine, lysine, cysteine and arginine residues, respectively, and caused alteration of the secondary structure of the HDL3 apolipoproteins to different extents.	Lysine	155-161	HDL3	Homo sapiens	16-20	
9555005-2	1998	Oxidation of HDL3 was monitored by measuring the following parameters: (i) formation of conjugated dienes, (ii) production of thiobarbituric acid reactive substances (TBARS), (iii) decrease in reactive lysine and (iv) tryptophan residues, (v) change in particle charge and (vi) diameter, and (vii) oligomerisation of apoA-I and apoA-II.	Lysine	202-208	HDL3	Homo sapiens	13-17	
1847886-3	1991	HDL3 was glycosylated in vitro to achieve up to 40-50% reductions in free-lysine residues.	Lysine	74-80	HDL3	Homo sapiens	0-4	
2302415-7	1990	Owing to the intricate contact between the lipidic core and the apolipoproteins, the Trp residues of human serum LDL and HDL3 are very rapidly oxidized, i.e., at least one order of magnitude faster than Tyr HDL and Lys LDL, which are believed to be involved in the binding of these lipoproteins to their cell receptors.	Lysine	215-218	HDL3	Homo sapiens	121-125	
2843239-0	1988	The secondary structure of apolipoproteins in human HDL3 particles after chemical modification of their tyrosine, lysine, cysteine or arginine residues.	Lysine	114-120	HDL3	Homo sapiens	52-56	
2986587-7	1985	Assuming a single receptor model, we found that 2.9 x 10(15) receptors/mg membrane protein bound with an affinity KD = 3.5 x 10(-7) M at 0 to 4 degrees C and KD = 1.9 x 10(-7) M at 37 degrees C. The binding was effectively competed with intact HDL3, with HDL3 that had undergone selective arginine and lysine residue modification, and with antibodies to apolipoproteins A-I and A-II.	Lysine	302-308	HDL3	Homo sapiens	244-248	
2986587-7	1985	Assuming a single receptor model, we found that 2.9 x 10(15) receptors/mg membrane protein bound with an affinity KD = 3.5 x 10(-7) M at 0 to 4 degrees C and KD = 1.9 x 10(-7) M at 37 degrees C. The binding was effectively competed with intact HDL3, with HDL3 that had undergone selective arginine and lysine residue modification, and with antibodies to apolipoproteins A-I and A-II.	Lysine	302-308	HDL3	Homo sapiens	255-259	
6089896-6	1984	We have also demonstrated, using whole intestinal mucosal cells, that lysine and arginine-modified HDL3 inhibited binding of normal 125I-labeled HDL3 to the same extent as normal excess HDL3.	Lysine	70-76	HDL3	Homo sapiens	145-149	
6089896-6	1984	We have also demonstrated, using whole intestinal mucosal cells, that lysine and arginine-modified HDL3 inhibited binding of normal 125I-labeled HDL3 to the same extent as normal excess HDL3.	Lysine	70-76	HDL3	Homo sapiens	145-149	
6405795-9	1983	On this basis, intact HDL3 was reacted with TNBS at 20 degrees C for 80 min and it could be considered that at least 10 of 22 primary amino groups of apolipoprotein A-I and 10 of 18 lysine residues of apolipoprotein A-II were exposed on the surface of HDL3 particles.	Lysine	182-188	HDL3	Homo sapiens	22-26