PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
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
7911741-0	1994	Synthesis and biological activity of new 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) synthase inhibitors: 2-oxetanones with a side chain mimicking the folded structure of 1233A.	Propiolactone	110-122	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	41-97
7911741-3	1994	Among 1233A and its synthetic analogs, trans-3-hydroxymethyl-4-[2-(7-methoxycarbonyl-1-naphthyl)ethyl]-2-oxe tanone (23) showed the highest HMG-CoA synthase inhibitory activity in vitro.	trans-3-hydroxymethyl-4-[2-(7-methoxycarbonyl-1-naphthyl)ethyl]-2-oxe tanone	39-115	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	140-156
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
8094614-12	1993	These studies, as well as the kinetic evidence presented, suggest that the beta-lactone inhibitors acylate HMG-CoA synthase in a reaction which appears to be irreversible in vitro, but is easily reversed in cultured cells and in animals.	beta-Lactone	75-87	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	107-123
1346397-2	1992	Addition of A23187 to the human monocytic leukemia cell line THP-1 in the presence of fetal calf serum led to rapid increases in mRNA concentration of up to 40-fold for HMG-CoA synthase and 15-fold for HMG-CoA reductase with little or no change in FPP synthetase mRNA levels.	Calcimycin	12-18	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	169-185
1346397-4	1992	The increases in HMG-CoA synthase and HMG-CoA reductase mRNAs were maximal after treatment of THP-1 cells with 10 micrograms/ml A23187 for 3 h. The stimulation was blocked by actinomycin D but not by cycloheximide treatment.	Calcimycin	128-134	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	17-33
1346397-4	1992	The increases in HMG-CoA synthase and HMG-CoA reductase mRNAs were maximal after treatment of THP-1 cells with 10 micrograms/ml A23187 for 3 h. The stimulation was blocked by actinomycin D but not by cycloheximide treatment.	Dactinomycin	175-188	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	17-33
35506308-0	2022	HMGCS2 silencing attenuates high glucose-induced in vitro diabetic cardiomyopathy by increasing cell viability, and inhibiting apoptosis, inflammation, and oxidative stress.	Glucose	33-40	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	0-6
1346397-6	1992	Surprisingly, the addition of A23187 to THP-1 cells incubated in the presence of 25-hydroxycholesterol and mevalonic acid also led to significant increases in the mRNA levels for HMG-CoA reductase and HMG-CoA synthase.	Calcimycin	30-36	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	201-217
1346397-6	1992	Surprisingly, the addition of A23187 to THP-1 cells incubated in the presence of 25-hydroxycholesterol and mevalonic acid also led to significant increases in the mRNA levels for HMG-CoA reductase and HMG-CoA synthase.	25-hydroxycholesterol	81-102	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	201-217
1346397-6	1992	Surprisingly, the addition of A23187 to THP-1 cells incubated in the presence of 25-hydroxycholesterol and mevalonic acid also led to significant increases in the mRNA levels for HMG-CoA reductase and HMG-CoA synthase.	Mevalonic Acid	107-121	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	201-217
1346397-8	1992	Taken together, these data suggest that A23187 treatment results in increased transcription of HMG-CoA reductase, HMG-CoA synthase, and, in some cell types, FPP synthetase by a mechanism that does not involve de novo protein synthesis.	Calcimycin	40-46	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	114-130
34298684-8	2021	Notably, RNA-seq data showed that JQ1 + gemcitabine selectively inhibited HMGCS2 and APOC1 ~6-fold, compared to controls.	gemcitabine	40-51	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	74-80
34238920-0	2021	Fructose drives mitochondrial metabolic reprogramming in podocytes via Hmgcs2-stimulated fatty acid degradation.	Fructose	0-8	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	71-77
34238920-0	2021	Fructose drives mitochondrial metabolic reprogramming in podocytes via Hmgcs2-stimulated fatty acid degradation.	Fatty Acids	89-99	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	71-77
34260294-0	2021	HMGCS2 in metabolic pathways was associated with overall survival in hepatocellular carcinoma: A LASSO-derived study.	alachlor	97-102	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	0-6
34818540-5	2021	Intestinal knockout of Hmgcs2 results in marked loss of H3K9bhb-associated loci, suggesting that local production of beta-OHB is responsible for chromatin reprogramming within the SI crypt.	beta-ohb	117-125	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	23-29
34624592-2	2021	Here, we demonstrate decreased expression of the HMGCS2 gene in ccRCC, a critical enzyme for the synthesis of the ketone body beta-hydroxybutyrate (beta-OHB).	Ketones	114-120	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	49-55
34624592-2	2021	Here, we demonstrate decreased expression of the HMGCS2 gene in ccRCC, a critical enzyme for the synthesis of the ketone body beta-hydroxybutyrate (beta-OHB).	3-Hydroxybutyric Acid	126-146	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	49-55
34624592-2	2021	Here, we demonstrate decreased expression of the HMGCS2 gene in ccRCC, a critical enzyme for the synthesis of the ketone body beta-hydroxybutyrate (beta-OHB).	beta-ohb	148-156	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	49-55
34624592-5	2021	The transcription of HMGCS2 was possible to restore by treatment with 5-aza-2"-deoxycytidine and with the histone deacetylase inhibitor beta-OHB.	Decitabine	70-92	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	21-27
34624592-5	2021	The transcription of HMGCS2 was possible to restore by treatment with 5-aza-2"-deoxycytidine and with the histone deacetylase inhibitor beta-OHB.	beta-ohb	136-144	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	21-27
34624592-9	2021	In addition, we showed that ectopic expression of HMGCS2 boosts the intracellular levels of beta-OHB and that exogenously applied beta-OHB suppresses the motility and invasion of ccRCC.	beta-ohb	92-100	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	50-56
34087430-9	2021	Finally, HMGCS2 knockdown enhanced TNFalpha-induced reactive oxygen species (ROS) generation.	Reactive Oxygen Species	52-75	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	9-15
34087430-9	2021	Finally, HMGCS2 knockdown enhanced TNFalpha-induced reactive oxygen species (ROS) generation.	Reactive Oxygen Species	77-80	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	9-15
35506308-2	2022	The study was undertaken to identify possible hub genes associated with DCM progression through bioinformatics analysis and to validate the role of 3-hydroxy-3-methylglutaryl-CoA synthase 2 (HMGCS2) in DCM progression using a cellular model of high glucose (HG)-induced DCM.	Glucose	249-256	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	191-197
14151-2	1977	Acetyl-CoA reacts stoichiometrically with a cysteinyl sufhydryl group of avian liver 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase to yield acetyl-S-enzyme (Miziorko H.M., Clinkenbeard, K.D., Reed, W.D., and Lane, M.D.	Acetyl Coenzyme A	0-10	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	85-130
2568358-2	1989	Addition of either delipidized serum and mevinolin or low density lipoprotein, 25-hydroxycholesterol, or mevalonic acid to HepG2 cells resulted in rapid changes both in the levels of the mRNAs and in the rates of synthesis of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) synthase, HMG-CoA reductase, and farnesyl pyrophosphate synthetase (prenyltranferase).	Lovastatin	41-50	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	226-282
2568358-2	1989	Addition of either delipidized serum and mevinolin or low density lipoprotein, 25-hydroxycholesterol, or mevalonic acid to HepG2 cells resulted in rapid changes both in the levels of the mRNAs and in the rates of synthesis of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) synthase, HMG-CoA reductase, and farnesyl pyrophosphate synthetase (prenyltranferase).	25-hydroxycholesterol	79-100	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	226-282
2568358-2	1989	Addition of either delipidized serum and mevinolin or low density lipoprotein, 25-hydroxycholesterol, or mevalonic acid to HepG2 cells resulted in rapid changes both in the levels of the mRNAs and in the rates of synthesis of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) synthase, HMG-CoA reductase, and farnesyl pyrophosphate synthetase (prenyltranferase).	Mevalonic Acid	105-119	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	226-282
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.	Mevalonic Acid	34-44	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	59-115
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
14151-2	1977	Acetyl-CoA reacts stoichiometrically with a cysteinyl sufhydryl group of avian liver 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase to yield acetyl-S-enzyme (Miziorko H.M., Clinkenbeard, K.D., Reed, W.D., and Lane, M.D.	lysyl-cysteinyl-cysteinyl-arginyl-cysteinyl-lysine	44-53	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	85-130
2870496-2	1986	A technique based on differential sensitivity of this enzyme activity to inhibition by magnesium ion is described that allows the discrimination of expression of human and hamster HMG-CoA synthase in these hybrids.	Magnesium	87-96	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	180-196
4019518-2	1985	A somatic cell mutant (Mev-1) auxotrophic for mevalonate by virtue of a complete lack of detectable 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) synthase activity has been shown to demonstrate a requirement for a non-sterol mevalonate-derived product for regulation of synthesis of HMG-CoA reductase.	Mevalonic Acid	46-56	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	100-156
4019518-2	1985	A somatic cell mutant (Mev-1) auxotrophic for mevalonate by virtue of a complete lack of detectable 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) synthase activity has been shown to demonstrate a requirement for a non-sterol mevalonate-derived product for regulation of synthesis of HMG-CoA reductase.	sterol mevalonate	220-237	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	100-156
2862911-1	1985	3-Chloropropionyl coenzyme A (3-chloropropionyl-CoA) irreversibly inhibits avian liver 3-hydroxy-3-methylglutaryl-CoA synthase (HMG-CoA synthase).	3-chloropropionyl-coenzyme A	30-51	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	128-144
2862911-6	1985	While the acetylated enzyme formed upon incubation of HMG-CoA synthase with acetyl-CoA is labile to performic acid oxidation, the adduct formed upon 3-chloropropionyl-CoA inactivation is stable to such treatment.	Acetyl Coenzyme A	76-86	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	54-70
2862911-6	1985	While the acetylated enzyme formed upon incubation of HMG-CoA synthase with acetyl-CoA is labile to performic acid oxidation, the adduct formed upon 3-chloropropionyl-CoA inactivation is stable to such treatment.	peroxyformic acid	100-114	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	54-70
32969201-1	2020	BACKGROUND: 3-Hydroxy-3-methylglutaryl-CoA (HMG-CoA) synthase 2 gene (HMGCS2) encodes a mitochondrial enzyme catalyzing the first reaction of ketogenesis metabolic pathway which provides lipid-derived energy for various organs during times of carbohydrate deprivation, such as fasting.	Carbohydrates	243-255	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	70-76
32734614-4	2020	The expression of PPARalpha and HMGCS2 was detected by reverse transcription quantitative polymerase chain reaction in cardiomyocytes and high-glucose-cultured cardiomyocytes.	Glucose	143-150	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	32-38
32734614-12	2020	HMGCS2 silencing was shown to inhibit HMGCS2 expression to suppress the apoptosis of high-glucose-induced cardiomyocytes and the loss of MMP, reduce the accumulation of ROS, and promote cardiomyocyte proliferation.	Glucose	90-97	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	0-6
32734614-12	2020	HMGCS2 silencing was shown to inhibit HMGCS2 expression to suppress the apoptosis of high-glucose-induced cardiomyocytes and the loss of MMP, reduce the accumulation of ROS, and promote cardiomyocyte proliferation.	Glucose	90-97	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	38-44
32734614-12	2020	HMGCS2 silencing was shown to inhibit HMGCS2 expression to suppress the apoptosis of high-glucose-induced cardiomyocytes and the loss of MMP, reduce the accumulation of ROS, and promote cardiomyocyte proliferation.	Reactive Oxygen Species	169-172	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	0-6
32734614-12	2020	HMGCS2 silencing was shown to inhibit HMGCS2 expression to suppress the apoptosis of high-glucose-induced cardiomyocytes and the loss of MMP, reduce the accumulation of ROS, and promote cardiomyocyte proliferation.	Reactive Oxygen Species	169-172	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	38-44
31766193-3	2019	Pemafibrate most profoundly induces HMGCS2 and PDK4, which regulate the rate-limiting step of ketogenesis and glucose oxidation, respectively, compared to other fatty acid metabolic genes in human hepatocytes.	Glucose	110-117	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	36-42
32635582-7	2020	We found that HCC cells with HMGCS2 downregulation possess altered lipid metabolism that increases fatty acid, triglyceride, and cholesterol synthesis.	Fatty Acids	99-109	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	29-35
32635582-7	2020	We found that HCC cells with HMGCS2 downregulation possess altered lipid metabolism that increases fatty acid, triglyceride, and cholesterol synthesis.	Triglycerides	111-123	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	29-35
32635582-7	2020	We found that HCC cells with HMGCS2 downregulation possess altered lipid metabolism that increases fatty acid, triglyceride, and cholesterol synthesis.	Cholesterol	129-140	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	29-35
32635582-9	2020	In conclusion, these results demonstrate that the downregulation of HMGCS2 attenuates the protective effect of the KD by shifting ketone production to enhance de novo lipogenesis in HCC.	Ketones	130-136	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	68-74
31779269-0	2019	HMGCS2 Mediates Ketone Production and Regulates the Proliferation and Metastasis of Hepatocellular Carcinoma.	Ketones	16-22	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	0-6
31779269-3	2019	The aims of this study were to verify the mechanisms and therapeutic potential of the ketogenesis rate-limiting enzyme 3-Hydroxymethylglutaryl-CoA synthase 2 (HMGCS2) in HCC.	3-hydroxy-3-methylglutaryl-coenzyme A	119-146	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	159-165
31779269-6	2019	In our investigation of the molecular mechanisms of HMGCS2 in HCC, we showed that knockdown of HMGCS2 decreased ketone production, which promoted cell proliferation, cell migration, and xenograft tumorigenesis by enhancing c-Myc/cyclinD1 and EMT signaling and by suppressing the caspase-dependent apoptosis pathway.	Ketones	112-118	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	52-58
31779269-6	2019	In our investigation of the molecular mechanisms of HMGCS2 in HCC, we showed that knockdown of HMGCS2 decreased ketone production, which promoted cell proliferation, cell migration, and xenograft tumorigenesis by enhancing c-Myc/cyclinD1 and EMT signaling and by suppressing the caspase-dependent apoptosis pathway.	Ketones	112-118	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	95-101
31779269-7	2019	Ketone body treatment reduced the proliferation- and migration-promoting effects of HMGCS2 knockdown in cells.	Ketones	0-6	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	84-90
31779269-8	2019	In contrast, HMGCS2 overexpression increased the intracellular ketone level and inhibited cell proliferation, cell migration, and xenograft tumorigenesis.	Ketones	63-69	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	13-19
30322448-2	2018	We investigated the evolution of HMGCS2, the key enzyme required for ketone body biosynthesis (ketogenesis).	Ketones	69-75	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	33-39
31546785-2	2019	Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase 2 (HMGCS2), a rate-limiting ketogenic enzyme in the synthesis of ketone body beta-hydroxybutyrate (betaHB), contributes to the regulation of intestinal cell differentiation.	3-Hydroxybutyric Acid	131-151	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	57-63
31546785-2	2019	Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase 2 (HMGCS2), a rate-limiting ketogenic enzyme in the synthesis of ketone body beta-hydroxybutyrate (betaHB), contributes to the regulation of intestinal cell differentiation.	3-Hydroxybutyric Acid	153-159	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	57-63
31442404-2	2019	Here we show that, in the mammalian small intestine, the expression of Hmgcs2 (3-hydroxy-3-methylglutaryl-CoA synthetase 2), the gene encoding the rate-limiting enzyme in the production of ketone bodies, including beta-hydroxybutyrate (betaOHB), distinguishes self-renewing Lgr5+ stem cells (ISCs) from differentiated cell types.	Ketones	189-195	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	71-77
31442404-2	2019	Here we show that, in the mammalian small intestine, the expression of Hmgcs2 (3-hydroxy-3-methylglutaryl-CoA synthetase 2), the gene encoding the rate-limiting enzyme in the production of ketone bodies, including beta-hydroxybutyrate (betaOHB), distinguishes self-renewing Lgr5+ stem cells (ISCs) from differentiated cell types.	Ketones	189-195	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	79-122
31442404-2	2019	Here we show that, in the mammalian small intestine, the expression of Hmgcs2 (3-hydroxy-3-methylglutaryl-CoA synthetase 2), the gene encoding the rate-limiting enzyme in the production of ketone bodies, including beta-hydroxybutyrate (betaOHB), distinguishes self-renewing Lgr5+ stem cells (ISCs) from differentiated cell types.	3-Hydroxybutyric Acid	214-234	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	71-77
31442404-2	2019	Here we show that, in the mammalian small intestine, the expression of Hmgcs2 (3-hydroxy-3-methylglutaryl-CoA synthetase 2), the gene encoding the rate-limiting enzyme in the production of ketone bodies, including beta-hydroxybutyrate (betaOHB), distinguishes self-renewing Lgr5+ stem cells (ISCs) from differentiated cell types.	3-Hydroxybutyric Acid	214-234	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	79-122
31442404-2	2019	Here we show that, in the mammalian small intestine, the expression of Hmgcs2 (3-hydroxy-3-methylglutaryl-CoA synthetase 2), the gene encoding the rate-limiting enzyme in the production of ketone bodies, including beta-hydroxybutyrate (betaOHB), distinguishes self-renewing Lgr5+ stem cells (ISCs) from differentiated cell types.	betaohb	236-243	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	71-77
31442404-2	2019	Here we show that, in the mammalian small intestine, the expression of Hmgcs2 (3-hydroxy-3-methylglutaryl-CoA synthetase 2), the gene encoding the rate-limiting enzyme in the production of ketone bodies, including beta-hydroxybutyrate (betaOHB), distinguishes self-renewing Lgr5+ stem cells (ISCs) from differentiated cell types.	betaohb	236-243	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	79-122
31442404-3	2019	Hmgcs2 loss depletes betaOHB levels in Lgr5+ ISCs and skews their differentiation toward secretory cell fates, which can be rescued by exogenous betaOHB and class I histone deacetylase (HDAC) inhibitor treatment.	betaohb	21-28	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	0-6
31442404-3	2019	Hmgcs2 loss depletes betaOHB levels in Lgr5+ ISCs and skews their differentiation toward secretory cell fates, which can be rescued by exogenous betaOHB and class I histone deacetylase (HDAC) inhibitor treatment.	betaohb	145-152	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	0-6
30567295-8	2018	Canonical pathway analysis, using Ingenuity Pathway Analysis software, revealed that the only genes in the "superpathway of cholesterol biosynthesis" were Idi1 (upregulated) and Hmgcs2 (downregulated).	Cholesterol	124-135	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	178-184
28888048-7	2018	While peroxysome proliferator activated receptor alpha (PPAR-alpha) agonist WY14643 increased HMGCS2 expression, this treatment was unable to affect PUFA-mediated regulation of HMGCS2 expression.	pirinixic acid	76-83	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	94-100
30392254-6	2018	The 5-years disease-specific survival (DSS) in down HMGCS2 expression group (14 months) was poorer than those in normal expression group (20 months; P=0.002).	dss	39-42	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	52-58
30392254-7	2018	In addition, multivariate Cox regression analysis showed that HMGCS2 expression (Wald=7.136, P=0.008) was an independent risk factor for DSS.	dss	137-140	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	62-68
28888048-8	2018	Forkhead box O1 (FoxO1) inhibitor AS1842856 reduced HMGCS2 expression and suppressed induction promoted by fatty acids.	5-amino-7-(cyclohexylamino)-1-ethyl-6-fluoro-4-oxo-1,4-dihydroquinoline-3-carboxylic acid	34-43	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	52-58
29523524-0	2018	Genome Wide Association Study Identifies the HMGCS2 Locus to be Associated With Chlorthalidone Induced Glucose Increase in Hypertensive Patients.	Chlorthalidone	80-94	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	45-51
29523524-6	2018	Among blacks, an intronic single-nucleotide polymorphism (rs9943291) in the HMGCS2 was associated with increase in glucose levels following chlorthalidone treatment (ss=12.5; P=4.17x10-8).	Glucose	115-122	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	76-82
24722248-6	2014	Moreover, we demonstrate that miR-29 fine-tunes FOXA2-mediated activation of key lipid metabolism genes, including PPARGC1A, HMGCS2, and ABHD5.	mir-29	30-36	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	125-131
29523524-6	2018	Among blacks, an intronic single-nucleotide polymorphism (rs9943291) in the HMGCS2 was associated with increase in glucose levels following chlorthalidone treatment (ss=12.5; P=4.17x10-8).	Chlorthalidone	140-154	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	76-82
29523524-7	2018	G-allele carriers of HMGCS2 had higher glucose levels (glucose change=+16.29 mg/dL) post chlorthalidone treatment compared with noncarriers of G allele (glucose change=+2.80 mg/dL).	Glucose	39-46	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	21-27
29523524-7	2018	G-allele carriers of HMGCS2 had higher glucose levels (glucose change=+16.29 mg/dL) post chlorthalidone treatment compared with noncarriers of G allele (glucose change=+2.80 mg/dL).	Chlorthalidone	89-103	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	21-27
29523524-10	2018	HMGCS2, a part of the HMG-CoA synthase family, is important for ketogenesis and cholesterol synthesis pathways that are essential in glucose homeostasis.	Cholesterol	80-91	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	0-6
29523524-11	2018	CONCLUSIONS: These results suggest that HMGCS2 is a promising candidate gene involved in chlorthalidone and Hydrochlorothiazide (HCTZ)-induced glucose change.	Chlorthalidone	89-103	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	40-46
29523524-11	2018	CONCLUSIONS: These results suggest that HMGCS2 is a promising candidate gene involved in chlorthalidone and Hydrochlorothiazide (HCTZ)-induced glucose change.	Hydrochlorothiazide	108-127	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	40-46
29523524-11	2018	CONCLUSIONS: These results suggest that HMGCS2 is a promising candidate gene involved in chlorthalidone and Hydrochlorothiazide (HCTZ)-induced glucose change.	Hydrochlorothiazide	129-133	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	40-46
26408941-8	2016	Our further analysis led to identification of an enzymatic switch comprising the enzymes Hmgcs2 (3-hydroxy-3-methylglutaryl-CoA synthase) and Auh (AU RNA binding protein/enoyl-CoA hydratase) which connects leucine degradation with cholesterol synthesis.	Cholesterol	231-242	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	89-95
28867541-5	2017	Inhibition of ERK phosphorylation by PD098059 markedly attenuated the malignant phenotypes mediated by HMGCS2 siRNA.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	37-45	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	103-109
28512002-7	2017	PDH catalyzes the oxidative decarboxylation of pyruvate into acetyl CoA, SDH oxidizes succinate into fumarate, and HMGCS2 controls the synthesis of the ketone body beta-hydroxybutyrate.	Ketones	152-158	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	115-121
28512002-7	2017	PDH catalyzes the oxidative decarboxylation of pyruvate into acetyl CoA, SDH oxidizes succinate into fumarate, and HMGCS2 controls the synthesis of the ketone body beta-hydroxybutyrate.	3-Hydroxybutyric Acid	164-184	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	115-121
28320515-3	2017	Here we report that overexpression of HMGCS2 decreased levels of APP and related CTFs (carboxy-terminal fragments), which was largely prevented by an autophagic inhibitor chloroquine.	Chloroquine	171-182	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	38-44
28320515-4	2017	In addition, HMGCS2 enhancement of autophagic marker LC3II was diminished by rapamycin, an inhibitor of mechanistic target of rapamycin.	Sirolimus	77-86	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	13-19
28320515-5	2017	Moreover, deprivation of EBSS (Earle"s Balanced Salt Solution) significantly augmented the effect of HMGCS2 on LC3II, while acetoacetate reversed the reduction of LC3II, APP and CTFs which was induced by HMGCS2 knockdown.	ebss	25-29	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	101-107
28320515-5	2017	Moreover, deprivation of EBSS (Earle"s Balanced Salt Solution) significantly augmented the effect of HMGCS2 on LC3II, while acetoacetate reversed the reduction of LC3II, APP and CTFs which was induced by HMGCS2 knockdown.	ebss	25-29	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	204-210
28320515-5	2017	Moreover, deprivation of EBSS (Earle"s Balanced Salt Solution) significantly augmented the effect of HMGCS2 on LC3II, while acetoacetate reversed the reduction of LC3II, APP and CTFs which was induced by HMGCS2 knockdown.	earle"s balanced salt solution	31-61	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	101-107
28320515-8	2017	Collectively, HMGCS2 shares with ketone bodies common features in autophagic clearance of APP and CTFs, suggesting that ketone bodies play an important role in HMGCS2 regulation of the autophagy.	Ketones	120-126	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	14-20
28320515-8	2017	Collectively, HMGCS2 shares with ketone bodies common features in autophagic clearance of APP and CTFs, suggesting that ketone bodies play an important role in HMGCS2 regulation of the autophagy.	Ketones	120-126	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	160-166
27174168-8	2016	Distinct gene clusters controlling BA and lipid homeostasis (FGF(R), APO and FABP family members, HMGCS2) and drug metabolism (CYP, UGT and SULT family members) were significantly modulated by CDCA.	Chenodeoxycholic Acid	193-197	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	98-104
24898254-3	2014	From a microarray analysis, we found that RPE cells express particularly high levels of the mitochondrial HMG-CoA synthase 2 (Hmgcs2) compared with all other tissues (except the liver and colon), leading to the hypothesis that RPE cells, like hepatocytes, can produce beta-hydroxybutyrate (beta-HB) from fatty acids.	3-Hydroxybutyric Acid	268-288	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	126-132
24898254-3	2014	From a microarray analysis, we found that RPE cells express particularly high levels of the mitochondrial HMG-CoA synthase 2 (Hmgcs2) compared with all other tissues (except the liver and colon), leading to the hypothesis that RPE cells, like hepatocytes, can produce beta-hydroxybutyrate (beta-HB) from fatty acids.	3-Hydroxybutyric Acid	290-297	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	126-132
24898254-3	2014	From a microarray analysis, we found that RPE cells express particularly high levels of the mitochondrial HMG-CoA synthase 2 (Hmgcs2) compared with all other tissues (except the liver and colon), leading to the hypothesis that RPE cells, like hepatocytes, can produce beta-hydroxybutyrate (beta-HB) from fatty acids.	Fatty Acids	304-315	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	126-132
19515767-5	2009	Among genes in the cholesterol pathways, I found that mRNA levels of hydroxymethylglutaryl-coenzyme A (HMG-CoA) synthase, squalene epoxidase, and acyl-CoA:cholesterol acyltransferase (ACAT), ACAT2, small heterodimer partner, and low-density lipoprotein receptor (LDLR)-related proteins were significantly changed in the cells.	Cholesterol	19-30	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	69-120
21952825-1	2012	The genes HMGCS2 and HMGCL encode the two main enzymes for ketone-body synthesis, mitochondrial HMG-CoA synthase and HMG-CoA lyase.	Ketones	59-65	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	10-16
21952825-1	2012	The genes HMGCS2 and HMGCL encode the two main enzymes for ketone-body synthesis, mitochondrial HMG-CoA synthase and HMG-CoA lyase.	Ketones	59-65	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	96-112
21791663-6	2011	Ceestatin binds to 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) synthase and irreversibly inhibits HMG-CoA synthase in a dose-dependent manner.	ceestatin	0-9	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	19-75
21035732-2	2010	Herein, we report the biochemical characterization of BryR, the 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase (HMGS) homolog implicated in beta-branching at C13 and C21 of the core ring system from the bryostatin metabolic pathway (Bry).	Bryostatins	202-212	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	64-109
23943793-4	2014	These Fe-S cluster-deficient muscles showed a dramatic up-regulation of the ketogenic enzyme HMGCS2 and the secreted protein FGF21 (fibroblast growth factor 21).	Iron	6-10	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	93-99
24315375-6	2013	Finally, mutation of hypersuccinylated residues K83 and K310 on HMGCS2 to glutamic acid strongly inhibits enzymatic activity.	L-arabinitol	56-60	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	64-70
24315375-6	2013	Finally, mutation of hypersuccinylated residues K83 and K310 on HMGCS2 to glutamic acid strongly inhibits enzymatic activity.	Glutamic Acid	74-87	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	64-70
23082721-8	2012	Finally, using human breast cancer tumor samples, we directly confirmed that the enzymes associated with ketone body production (HMGCS2, HMGCL and BDH1) were preferentially expressed in the tumor stroma.	Ketones	105-111	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	129-135
23082722-4	2012	For this purpose, we generated hTERT-immortalized fibroblasts overexpressing the rate-limiting enzymes that promote ketone body production, namely BDH1 and HMGCS2.	Ketones	116-122	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	156-162
23082722-12	2012	In summary, ketone bodies behave as onco-metabolites, and we directly show that the enzymes HMGCS2, ACAT1/2 and OXCT1/2 are bona fide metabolic oncogenes.	Ketones	12-18	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	92-98
22531971-9	2012	Divalproex sodium also inhibited PPARalpha and decreased the messenger RNA expressions of 3-hydroxy-3-methylglutaryl-CoA synthase 2 and carnitine palmitoyltransferase 1A.	Valproic Acid	0-17	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	90-131
21791663-6	2011	Ceestatin binds to 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) synthase and irreversibly inhibits HMG-CoA synthase in a dose-dependent manner.	ceestatin	0-9	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	102-118
21791663-9	2011	CONCLUSIONS: Ceestatin therefore exerts its anti-HCV effects through inhibition of HMG-CoA synthase.	ceestatin	13-22	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	83-99
21502324-0	2011	Human HMGCS2 regulates mitochondrial fatty acid oxidation and FGF21 expression in HepG2 cell line.	Fatty Acids	37-47	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	6-12
21502324-1	2011	HMGCS2 (hydroxymethylglutaryl CoA synthase 2), the gene that regulates ketone body production, is barely expressed in cultured cell lines.	Ketones	71-77	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	0-6
21502324-1	2011	HMGCS2 (hydroxymethylglutaryl CoA synthase 2), the gene that regulates ketone body production, is barely expressed in cultured cell lines.	Ketones	71-77	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	8-44
21502324-2	2011	In this study, we restored HMGCS2 expression and activity in HepG2 cells, thus showing that the wild type enzyme can induce fatty acid beta-oxidation (FAO) and ketogenesis, whereas a catalytically inactive mutant C166A did not generate either process.	Fatty Acids	124-134	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	27-33
21502324-5	2011	These results indicate that HMGCS2 expression is both sufficient and necessary to the control of fatty acid oxidation in these cells.	Fatty Acids	97-107	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	28-34
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
19706283-1	2010	3-Hydroxy-3-methylglutaryl-CoA (HMG-CoA) synthase catalyzes the first physiologically irreversible step in biosynthesis of isoprenoids and sterols from acetyl-CoA.	Acetyl Coenzyme A	152-162	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.	beta-Lactone	33-45	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	146-162
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
19885625-6	2009	Up-regulation of cholesterol synthesis-associated genes, including HMG-CoA reductase, HMG-CoA synthase, farnesyl-diphosphate synthase and squalene synthase, confirmed enhanced de novo cholesterol synthesis.	Cholesterol	17-28	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	86-102
18313239-0	2008	Mitochondrial protein thiol modifications in acetaminophen hepatotoxicity: effect on HMG-CoA synthase.	Sulfhydryl Compounds	22-27	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	85-101
18313239-0	2008	Mitochondrial protein thiol modifications in acetaminophen hepatotoxicity: effect on HMG-CoA synthase.	Acetaminophen	45-58	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	85-101
18313239-7	2008	However, 3-hydroxy-3-methylglutaryl coenzyme A synthase 2 (HMG-CoA synthase) had significantly decreased levels of reduced thiols and activity after APAP treatment.	Sulfhydryl Compounds	123-129	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	59-75
18313239-7	2008	However, 3-hydroxy-3-methylglutaryl coenzyme A synthase 2 (HMG-CoA synthase) had significantly decreased levels of reduced thiols and activity after APAP treatment.	Acetaminophen	149-153	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	59-75
18313239-8	2008	HMG-CoA synthase is a key regulatory enzyme in ketogenesis and possesses a number of critical cysteines in the active site.	Cysteine	94-103	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	0-16
16940161-1	2006	HMGCS2, the gene that regulates ketone body production, is expressed in liver and several extrahepatic tissues, such as the colon.	Ketones	32-38	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	0-6
15994924-2	2005	The most striking pattern observed was a PDGF-dependent activation of at least 25 genes involved with biosynthesis and/or uptake of cholesterol and isoprenoids, including mevalonate pyrophosphate decarboxylase, 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) synthase, HMG-CoA reductase, and low-density lipoprotein receptor.	Cholesterol	132-143	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	211-267
15498869-2	2004	Uniquely among condensing enzymes, 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase (HMGS) catalyzes the formation of a carbon-carbon bond by activating the methyl group of an acetylated cysteine.	Carbon	117-123	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	35-80
15498869-2	2004	Uniquely among condensing enzymes, 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase (HMGS) catalyzes the formation of a carbon-carbon bond by activating the methyl group of an acetylated cysteine.	Carbon	124-130	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	35-80
15498869-2	2004	Uniquely among condensing enzymes, 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase (HMGS) catalyzes the formation of a carbon-carbon bond by activating the methyl group of an acetylated cysteine.	Cysteine	184-192	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	35-80
10772388-3	2000	Cholesterol synthesis in the epidermis is correlated with changes in mRNA levels for key enzymes, such as HMG-CoA synthase and HMG-CoA reductase, which have been previously demonstrated to be coordinately regulated by the sterol regulatory element binding proteins (SREBPs).	Cholesterol	0-11	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	106-122
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).	Isoflavones	169-179	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	51-67
12419552-4	2002	For example, statins modulate activation of the class-I transcription factor sterol responsive element-binding protein (SREBP), whose target genes including hydroxyl-methyl-glutaryl acetyl Coenzyme-A (HMG-CoA) reductase, HMG-CoA synthase, and the low-density lipoprotein receptor, all of which are involved in cholesterol and fatty acid metabolism.	Cholesterol	310-321	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	221-237
12419552-4	2002	For example, statins modulate activation of the class-I transcription factor sterol responsive element-binding protein (SREBP), whose target genes including hydroxyl-methyl-glutaryl acetyl Coenzyme-A (HMG-CoA) reductase, HMG-CoA synthase, and the low-density lipoprotein receptor, all of which are involved in cholesterol and fatty acid metabolism.	Fatty Acids	326-336	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	221-237
12119189-2	2002	When cells are deprived of cholesterol, proteolytic cleavage releases the NH(2)-terminal domain of SREBP-2 that binds and activates the promoters of SREBP-2-regulated genes including the genes encoding the low-density lipoprotein (LDL) receptor, 3-hydroxymethyl-3-glutaryl-(HMG-)CoA-synthase, and HMG-CoA-reductase.	Cholesterol	27-38	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	206-291
12044893-2	2002	Using a ligand of PPAR gamma, troglitazone or pioglitazone, we have shown that the expression of two genes involved in cholesterol biosynthesis, 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) synthase and HMG-CoA reductase, were increased by activation of PPAR gamma through a PPAR response element (PPRE) in THP-1 macrophages.	Troglitazone	30-42	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	145-201
12044893-2	2002	Using a ligand of PPAR gamma, troglitazone or pioglitazone, we have shown that the expression of two genes involved in cholesterol biosynthesis, 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) synthase and HMG-CoA reductase, were increased by activation of PPAR gamma through a PPAR response element (PPRE) in THP-1 macrophages.	Pioglitazone	46-58	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	145-201
12044893-2	2002	Using a ligand of PPAR gamma, troglitazone or pioglitazone, we have shown that the expression of two genes involved in cholesterol biosynthesis, 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) synthase and HMG-CoA reductase, were increased by activation of PPAR gamma through a PPAR response element (PPRE) in THP-1 macrophages.	Cholesterol	119-130	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	145-201
11479731-6	2001	Whereas wild-type cDNA of the HMGCS2 gene reverted the auxotrophy for mevalonate, the cDNAs of the mutants did not.	Mevalonic Acid	70-80	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	30-36
11108725-4	2000	In the current study we identify the peroxisomal targeting signals required for four other enzymes of the cholesterol biosynthetic pathway: acetoacetyl-CoA (AA-CoA) thiolase, 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) synthase, mevalonate diphosphate decarboxylase (MPPD), and farnesyl diphosphate (FPP) synthase.	Cholesterol	106-117	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	175-231
10748155-10	2000	Demonstration of a significant upfield shift for the methyl protons of HMG-CoA synthase"s acetyl-S-enzyme reaction intermediate suggests a hydrophobic active site environment that could elevate the pK(a) of Glu(95) as required to support its function as a general acid.	Glutamic Acid	207-210	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	71-87
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
10772388-7	2000	However, unlike sterols, 50 microM oleic acid increase the steady state mRNA levels of HMG-CoA synthase and the activity of the HMG-CoA synthase promoter.	Oleic Acid	35-45	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	87-103
10772388-7	2000	However, unlike sterols, 50 microM oleic acid increase the steady state mRNA levels of HMG-CoA synthase and the activity of the HMG-CoA synthase promoter.	Oleic Acid	35-45	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	128-144
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
9651391-7	1998	Induction of endogenous FPP synthase and HMG-CoA synthase mRNAs, in response to cellular cholesterol depletion, was prevented when cells expressed Gal4-CBP(1-451).	Cholesterol	89-100	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	41-57
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
9610773-4	1998	In particular, the activities and mRNA for the biosynthetic enzymes, 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase and HMG-CoA synthase are low in liver biopsy specimens isolated from affected individuals, suggesting replete intracellular cholesterol pools.	Cholesterol	251-262	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	131-147
9430668-1	1998	3-Hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) synthase, a key regulatory enzyme in the pathway for endogenous cholesterol synthesis, is a target for negative feedback regulation by cholesterol.	Cholesterol	112-123	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	0-56
9548596-7	1998	HMG-CoA synthase and LDL binding were inhibited equally by 7-dehydrocholesterol and cholesterol.	7-dehydrocholesterol	59-79	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	0-16
9548596-7	1998	HMG-CoA synthase and LDL binding were inhibited equally by 7-dehydrocholesterol and cholesterol.	Cholesterol	68-79	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	0-16
9430668-1	1998	3-Hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) synthase, a key regulatory enzyme in the pathway for endogenous cholesterol synthesis, is a target for negative feedback regulation by cholesterol.	Cholesterol	183-194	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	0-56
9063904-2	1997	Avian hydroxymethylglutaryl-CoA (HMG-CoA) synthase is inactivated by oxobutylsulfoxyl-CoA in a time-dependent fashion.	oxobutylsulfoxyl-coa	69-89	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	6-50
11671524-1	1997	Four chiral forms of the beta-lactone DU-6622 (3-hydroxy-2-(hydroxymethyl)-5-[7-(methoxycarbonyl)naphthalen-1-yl]pentanoic acid 1,3-lactone) were prepared to investigate their inhibitory activity against 3-hydroxy-3-methylglutarly-CoA (HMG-CoA) synthase.	beta-Lactone	25-37	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	204-253
11671524-1	1997	Four chiral forms of the beta-lactone DU-6622 (3-hydroxy-2-(hydroxymethyl)-5-[7-(methoxycarbonyl)naphthalen-1-yl]pentanoic acid 1,3-lactone) were prepared to investigate their inhibitory activity against 3-hydroxy-3-methylglutarly-CoA (HMG-CoA) synthase.	DU 6622	38-45	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	204-253
11671524-2	1997	The (2R,3R)-beta-lactone isomer (+)-8a, having the same stereochemistry as that of the fungal beta-lactone 1233A, showed the most potent HMG-CoA synthase inhibitory activity (IC(50): 0.098 &mgr;M).	(2r,3r)-beta-lactone	4-24	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	137-153
11671524-2	1997	The (2R,3R)-beta-lactone isomer (+)-8a, having the same stereochemistry as that of the fungal beta-lactone 1233A, showed the most potent HMG-CoA synthase inhibitory activity (IC(50): 0.098 &mgr;M).	(+)-8a	32-38	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	137-153
11671524-2	1997	The (2R,3R)-beta-lactone isomer (+)-8a, having the same stereochemistry as that of the fungal beta-lactone 1233A, showed the most potent HMG-CoA synthase inhibitory activity (IC(50): 0.098 &mgr;M).	beta-Lactone	12-24	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	137-153
11671524-4	1997	Thus, it was concluded that the (2R,3R) stereochemistry of the beta-lactone ring is responsible for HMG-CoA synthase inhibition.	beta-Lactone	63-75	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	100-116
9406821-5	1997	By northern blotting, the steady-state mRNA levels for HMG-CoA reductase, HMG-CoA synthase, farnesyl pyrophosphate synthase, and squalene synthase, key enzymes for cholesterol synthesis, all increased significantly after barrier disruption by either acetone or tape stripping.	Acetone	250-257	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	74-90
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
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.	Cholesterol	259-270	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	206-222
8619637-10	1996	Thus, like several other genes in the cholesterol biosynthetic pathway, including the 3-hydroxy-3-methylglutaryl coenzyme A (HMG CoA) synthase, HMG CoA reductase, squalene synthase, and farnesyl diphosphate synthase, the expression of the human CYP51 is suppressed by oxysterols.	Cholesterol	38-49	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	86-142
7887956-1	1995	In a cultured human hepatoblastoma cell line, Hep G2, chenodeoxycholic acid (CDCA) induced LDL receptor mRNA levels approximately 4 fold and mRNA levels for HMG-CoA reductase and HMG-CoA synthase two fold.	Chenodeoxycholic Acid	54-75	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	179-195
7887956-1	1995	In a cultured human hepatoblastoma cell line, Hep G2, chenodeoxycholic acid (CDCA) induced LDL receptor mRNA levels approximately 4 fold and mRNA levels for HMG-CoA reductase and HMG-CoA synthase two fold.	Chenodeoxycholic Acid	77-81	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	179-195
8558080-2	1995	32P-labeled cRNA fragments for genes of human LDLR and the enzymes HMG-CoA synthase (HMGS), HMG-CoA reductase (HMGR), mevalonate kinase (MK), farnesyl pyrophosphate synthase (FPPS), and squalene synthase (SQS) were prepared by in vitro transcription.	Phosphorus-32	0-3	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	67-83
8558080-2	1995	32P-labeled cRNA fragments for genes of human LDLR and the enzymes HMG-CoA synthase (HMGS), HMG-CoA reductase (HMGR), mevalonate kinase (MK), farnesyl pyrophosphate synthase (FPPS), and squalene synthase (SQS) were prepared by in vitro transcription.	Phosphorus-32	0-3	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	85-89
8558080-5	1995	When cells were cultured in DMEM supplemented with 10% fetal calf serum (FCS), mRNA levels of FPPS, SQS, and LDLR were about 4- to 7-fold higher than those of HMGS, HMGR, and MK.	dmem	28-32	3-hydroxy-3-methylglutaryl-CoA synthase 2	Homo sapiens	159-163