PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11502879-0	2001	Glutathione peroxidase-1 overexpression prevents ceramide production and partially inhibits apoptosis in doxorubicin-treated human breast carcinoma cells.	Doxorubicin	105-116	glutathione peroxidase 1	Homo sapiens	0-24	
11502879-3	2001	We selectively investigated the interaction of seleno-glutathione peroxidase-1 (GPx-1), the major enzyme responsible for peroxide detoxification in mammalian cells, with the cytotoxic response of T47D human breast cancer cells to doxorubicin, an anticancer drug known to promote production of ROS and apoptotic mediator ceramide.	Doxorubicin	230-241	glutathione peroxidase 1	Homo sapiens	47-78	
11502879-3	2001	We selectively investigated the interaction of seleno-glutathione peroxidase-1 (GPx-1), the major enzyme responsible for peroxide detoxification in mammalian cells, with the cytotoxic response of T47D human breast cancer cells to doxorubicin, an anticancer drug known to promote production of ROS and apoptotic mediator ceramide.	Doxorubicin	230-241	glutathione peroxidase 1	Homo sapiens	80-85	
11502879-6	2001	The glutathione precursor, N-acetylcysteine also partially protected T47D/H3 cells from the lethal effect of doxorubicin, whereas L-buthionine-(S,R)-sulfoximine, an inhibitor of glutathione biosynthesis, sensitized both GPx-1--deficient and -proficient cells.	Doxorubicin	109-120	glutathione peroxidase 1	Homo sapiens	220-225	
11502879-10	2001	Taken together, these results indicate that GPx-1 can regulate doxorubicin-induced cell death signaling at least in part by interfering with the activation of the sphingomyelin-ceramide pathway.	Doxorubicin	63-74	glutathione peroxidase 1	Homo sapiens	44-49