PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10641795-5	1999	We observed time-dependent losses of apoB histidine, lysine and glycine.	Histidine	42-51	apolipoprotein B	Homo sapiens	37-41	
9890644-10	1999	The former sites may be primarily histidine residues of apolipoprotein B-100 that are oxidized to 2-oxo-histidine in the presence of Cu and AA or DHA, thus explaining, at least in part, the unusual inhibitory effect of vitamin C on Cu-induced LDL oxidation.	Histidine	34-43	apolipoprotein B	Homo sapiens	56-76	
27406964-2	1997	Cu(2+) may play an important role in LDL oxidation by binding to histidine residues of apolipoprotein B-100 (apo B) and initiating and propagating lipid peroxidation.	Histidine	65-74	apolipoprotein B	Homo sapiens	87-107	
9409331-0	1997	Copper ions promote peroxidation of low density lipoprotein lipid by binding to histidine residues of apolipoprotein B100, but they are reduced at other sites on LDL.	Histidine	80-89	apolipoprotein B	Homo sapiens	102-121	
9409331-5	1997	In the current studies, we used diethylpyrocarbonate (DEPC) to modify the histidine residues of apolipoprotein B100, the major protein in LDL.	Histidine	74-83	apolipoprotein B	Homo sapiens	96-115	
9409331-12	1997	These observations suggest that peroxidation of the lipids in LDL can proceed with normal kinetics only when Cu2+ binds preferentially to sites on apolipoprotein B100 that contain histidine residues.	Histidine	180-189	apolipoprotein B	Homo sapiens	147-166	
7670940-6	1995	In the Finnish population, allele frequencies of the rare alleles of the apoB 1887 (Asn-->Ser) and apoB 1896 (His-->Arg) polymorphisms were .02 and .11, respectively.	Histidine	110-113	apolipoprotein B	Homo sapiens	99-103	
8910407-3	1996	Here we describe the application of highly specific tandem mass spectrometric techniques to the first characterization of lipid-modified LDL by demonstrating the addition of 4-hydroxy-2-nonenal to histidine residues of apolipoprotein B-100, following oxidation of LDL.	Histidine	197-206	apolipoprotein B	Homo sapiens	219-239	
7918471-3	1994	We here present direct evidence that HNE derivatization of LDL forms Michael addition-type adducts of HNE with histidine and lysine residues of apolipoprotein B-100 (apoB) and also demonstrate the utility of an antibody specific to the HNE adducts generated in the LDL treated with HNE or oxidatively modified by Cu2+ or cultured endothelial cells.	Histidine	111-120	apolipoprotein B	Homo sapiens	144-164	
7918471-3	1994	We here present direct evidence that HNE derivatization of LDL forms Michael addition-type adducts of HNE with histidine and lysine residues of apolipoprotein B-100 (apoB) and also demonstrate the utility of an antibody specific to the HNE adducts generated in the LDL treated with HNE or oxidatively modified by Cu2+ or cultured endothelial cells.	Histidine	111-120	apolipoprotein B	Homo sapiens	166-170