PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15514256-8	2004	When HepG2 cells were transiently transfected with HMG CoA synthase and LDL receptor reporter plasmids there was an increase in expression in response to soy extract or isoflavone treatment from both of these promoters, but this induction was blunted in the presence of sterols (P < 0.05).	Sterols	270-277	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	51-67	
19706283-1	2010	3-Hydroxy-3-methylglutaryl-CoA (HMG-CoA) synthase catalyzes the first physiologically irreversible step in biosynthesis of isoprenoids and sterols from acetyl-CoA.	Sterols	139-146	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	0-49	
19706283-2	2010	Inhibition of enzyme activity by beta-lactone-containing natural products correlates with substantial diminution of sterol synthesis, identifying HMG-CoA synthase as a potential drug target and suggesting that identification of effective inhibitors would be valuable.	Sterols	116-122	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	146-162	
9604010-4	1998	To understand the sterol-dependent transcriptional regulation by these factors in detail, we have examined the regulation of the 3-hydroxy-3-methylglutaryl coenzyme A (HMG CoA) synthase and squalene synthase genes, whose promoters have multiple potential sterol regulatory elements (SRE, SREBP binding site) and NF-Y binding sites.	Sterols	18-24	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	129-185	
9651391-8	1998	We conclude that when cells are incubated in the absence of sterols, the transcriptional activation of the HMG-CoA synthase, HMG-CoA reductase, FPP synthase, and low density lipoprotein receptor genes is dependent on a specific interaction between SREBP, which is bound to the promoter DNA, and the amino-terminal domain (amino acids 1-451) of CBP.	Sterols	60-67	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	107-123	
9604010-9	1998	The involvement of multiple responsive elements in the transcription of HMG CoA synthase and squalene synthase seems to induce a higher level of sterol-dependent regulation (3.5 to 5.	Sterols	145-151	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	72-88	
9604010-12	1998	These results agree with the findings that the distances between the two motifs in the known sterol responsive elements in several genes, including the human HMG CoA synthase and squalene synthase genes, are in this range.	Sterols	93-99	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	158-174	
8947512-1	1996	Sterol regulatory element (SRE) has been recognized to regulate various key genes coding for especially low density lipoprotein (LDL)-receptor, 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase and HMG-CoA synthase known to play a crucial role in the cholesterol feedback mechanism.	Sterols	0-6	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	206-222	
7940020-5	1994	RNA blotting analysis indicated that these transfectants were able to increase HMG-CoA synthase gene transcripts in response to sterol removal.	Sterols	128-134	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	79-95	
1346397-1	1992	We report that the sterol-mediated suppression of the mRNA levels of three cholesterogenic enzymes, 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase, HMG-CoA synthase, and farnesyl diphosphate (FPP) synthetase is partially overcome by the calcium ionophore A23187.	Sterols	19-25	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	159-175	
2904178-1	1988	Two enzymes of mammalian cellular mevalonate biosynthesis, 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) synthase and HMG-CoA reductase, have been shown to be regulated by exogenous sterols.	Sterols	184-191	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	59-115