PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
8148817-3	1994	When delipidated apo B was treated with linoleic acid 13-mono-hydroperoxide (LOOH) and trans-2-octenal (octenal), apo B became fluorescent and its Lys and histidine (His) residues were decreased.	trans-2-Octenal	95-102	apolipoprotein B	Mus musculus	17-22
8148817-3	1994	When delipidated apo B was treated with linoleic acid 13-mono-hydroperoxide (LOOH) and trans-2-octenal (octenal), apo B became fluorescent and its Lys and histidine (His) residues were decreased.	trans-2-Octenal	95-102	apolipoprotein B	Mus musculus	114-119
8148817-4	1994	When delipidated apo B, partially methylated at the epsilon-amino groups of Lys residues, was treated with LOOH and octenal, fluorescence was not produced and the free Lys residues were not decreased.	trans-2-Octenal	116-123	apolipoprotein B	Mus musculus	17-22
8148817-5	1994	LOOH- and octenal-modified delipidated apo B were recognized by mouse peritoneal macrophages.	trans-2-Octenal	10-17	apolipoprotein B	Mus musculus	39-44
8148817-8	1994	Neutralization of positively charged Lys residues of apo B by modification with LOOH and octenal may be requisite for recognition.	trans-2-Octenal	89-96	apolipoprotein B	Mus musculus	53-58
8148817-9	1994	Bovine serum albumin modified with LOOH and octenal prevented the recognition of the modified apo B, indicating that none of the intrinsic structure of apo B is required for recognition.	trans-2-Octenal	44-51	apolipoprotein B	Mus musculus	94-99