PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12006395-10	2002	Postprandial FFA and hydroxybutyric acid (as a marker of hepatic FFA oxidation) were significantly higher in FCHL patients than in control subjects, and the early postprandial C3 rise was negatively correlated with the postprandial FFA and hydroxybutyric acid concentrations.	Fatty Acids, Nonesterified	65-68	complement C3	Homo sapiens	176-178	
12006395-12	2002	Therefore, an impaired postprandial C3 response may be associated with impaired peripheral postprandial FFA uptake and, consequently, lead to increased hepatic FFA flux and very low density lipoprotein overproduction.	Fatty Acids, Nonesterified	104-107	complement C3	Homo sapiens	36-38	
19278558-2	2009	The objective of this paper is to describe systems biology methods for identifying pathways involved in liver toxicity induced by free fatty acids (FFA) and tumor necrosis factor (TNF)-alpha in human hepatoblastoma cells (HepG2/C3A).	Fatty Acids, Nonesterified	130-146	complement C3	Homo sapiens	228-231	
18052188-1	2008	The objective of this study was to identify pathways that regulate the cytotoxicity induced by free fatty acids (FFAs) in human hepatoblastoma cells (HepG2/C3A).	Fatty Acids, Nonesterified	95-111	complement C3	Homo sapiens	156-159	
17570844-5	2007	RESULTS: This paper presents a systems approach that integrates gene expression and cytotoxicity profiles to identify a network of pathways involved in free fatty acid (FFA) and tumor necrosis factor-alpha (TNF-alpha) induced cytotoxicity in human hepatoblastoma cells (HepG2/C3A).	Fatty Acids, Nonesterified	152-167	complement C3	Homo sapiens	276-279	
17570844-5	2007	RESULTS: This paper presents a systems approach that integrates gene expression and cytotoxicity profiles to identify a network of pathways involved in free fatty acid (FFA) and tumor necrosis factor-alpha (TNF-alpha) induced cytotoxicity in human hepatoblastoma cells (HepG2/C3A).	Fatty Acids, Nonesterified	169-172	complement C3	Homo sapiens	276-279	
17245758-1	2007	Acylation stimulating protein (ASP) is a fragment of the third component of complement (C3) that is generated in the presence of chylomicron, and plays a role in the synthesis of triacylglycerol by transporting free fatty acids into adipocytes.	Fatty Acids, Nonesterified	211-227	complement C3	Homo sapiens	76-90	
11826668-5	2002	Complement component 3 (C3) plays an important role in the uptake of free fatty acids by the peripheral cells and their esterification to triglycerides.	Fatty Acids, Nonesterified	69-85	complement C3	Homo sapiens	0-22	
11826668-5	2002	Complement component 3 (C3) plays an important role in the uptake of free fatty acids by the peripheral cells and their esterification to triglycerides.	Fatty Acids, Nonesterified	69-85	complement C3	Homo sapiens	24-26	
11826668-6	2002	Since C3 is also involved in the pathogenesis of the insulin resistance syndrome, and since a deviant FFA metabolism with an increased FFA flux to the liver may induce insulin resistance, it is hypothesized that C3 may form the missing link between FFA metabolism and insulin resistance.	Fatty Acids, Nonesterified	102-105	complement C3	Homo sapiens	212-214	
11826668-6	2002	Since C3 is also involved in the pathogenesis of the insulin resistance syndrome, and since a deviant FFA metabolism with an increased FFA flux to the liver may induce insulin resistance, it is hypothesized that C3 may form the missing link between FFA metabolism and insulin resistance.	Fatty Acids, Nonesterified	135-138	complement C3	Homo sapiens	212-214