PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
2730657-5	1989	Thus, protein synthesis is required for 25-hydroxycholesterol dependent suppression of HMG-CoA reductase mRNA.	Hydroxycholesterols	43-61	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	87-104
2567731-2	1989	In this paper, we assess the relative degree of regulation of the rate-limiting enzyme of isoprenoid biosynthesis, 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, by sterol and nonsterol products of mevalonate by utilizing cultured Chinese hamster ovary cells blocked in sterol synthesis.	Terpenes	90-100	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	115-172
2567731-2	1989	In this paper, we assess the relative degree of regulation of the rate-limiting enzyme of isoprenoid biosynthesis, 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, by sterol and nonsterol products of mevalonate by utilizing cultured Chinese hamster ovary cells blocked in sterol synthesis.	Mevalonic Acid	210-220	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	115-172
2567731-2	1989	In this paper, we assess the relative degree of regulation of the rate-limiting enzyme of isoprenoid biosynthesis, 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, by sterol and nonsterol products of mevalonate by utilizing cultured Chinese hamster ovary cells blocked in sterol synthesis.	Sterols	177-183	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	115-172
2794782-1	1989	Chemical synthesis of 5 beta-cholest-8-ene-3 beta,15 alpha-diol and its effects on 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in CHO-K1 cells.	5 beta-cholest-8-ene-3 beta,15 alpha-diol	22-63	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	83-130
2794782-5	1989	5 beta-Cholest-8-ene-3 beta,15 alpha-diol was found to be highly active in the lowering of the levels of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in Chinese hamster ovary cells and only slightly less active than the corresponding sterol (5 alpha-cholest-8-ene-3 beta,15 alpha-diol) with the trans A-B ring junction.	beta-cholest-8-ene-3 beta,15 alpha-diol	2-41	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	105-152
3663697-1	1987	Mutants resistant to compactin, an inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase, have been previously isolated from the Chinese hamster V79 cell line.	mevastatin	21-30	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	48-95
2917146-0	1989	Treatment of CHO-K1 cells with 25-hydroxycholesterol produces a more rapid loss of 3-hydroxy-3-methylglutaryl-coenzyme A reductase activity than can be accounted for by enzyme turnover.	25-hydroxycholesterol	31-52	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	83-130
3170653-1	1988	In order to investigate a requirement for isoprenoid compounds in the cell cycle, DNA synthesis was examined in cultured Chinese hamster ovary cells in which mevalonate biosynthesis was blocked with mevinolin, a competitive inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase.	Lovastatin	199-208	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	237-294
6643457-1	1983	3-Hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase) converts HMG-CoA to mevalonate, a key intermediate in the formation of cholesterol and several nonsterol isoprenoid compounds.	3-hydroxy-3-methylglutaryl-coenzyme A	49-56	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	0-47
3624255-0	1987	Modulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase by azole antimycotics requires lanosterol demethylation, but not 24,25-epoxylanosterol formation.	Azoles	65-70	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	14-61
3624255-0	1987	Modulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase by azole antimycotics requires lanosterol demethylation, but not 24,25-epoxylanosterol formation.	Lanosterol	93-103	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	14-61
3624255-5	1987	Both demethylase inhibitors produced a biphasic modulation of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase, the rate-limiting enzyme in the cholesterol biosynthetic pathway.	Cholesterol	153-164	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	62-119
2874807-2	1986	Acetoacetyl CoA thiolase, HMG CoA synthase and HMG CoA reductase activities were elevated in the mevinolin resistant line, KH 2.0.	Lovastatin	97-106	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	47-64
3995584-1	1985	3-Hydroxy-3-methylglutaryl coenzyme A reductase (HMG CoA reductase) is a single polypeptide chain with two contiguous domains: a soluble domain (548 amino acids) that catalyzes the rate-controlling step in cholesterol synthesis and a membrane-bound domain (339 amino acids) that anchors the protein to the endoplasmic reticulum (ER).	Cholesterol	206-217	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	0-66
3838796-0	1985	Sterols accelerate degradation of hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase encoded by a constitutively expressed cDNA.	Sterols	0-7	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	42-89
3838796-1	1985	A recombinant plasmid containing a full-length cDNA for hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase was introduced by calcium phosphate-mediated transfection into UT-2 cells, a mutant line of Chinese hamster ovary cells that lack 3-hydroxy-3-methylglutaryl coenzyme A reductase activity and thus require low density lipoprotein-cholesterol and mevalonate for growth.	calcium phosphate	130-147	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	64-111
3838796-1	1985	A recombinant plasmid containing a full-length cDNA for hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase was introduced by calcium phosphate-mediated transfection into UT-2 cells, a mutant line of Chinese hamster ovary cells that lack 3-hydroxy-3-methylglutaryl coenzyme A reductase activity and thus require low density lipoprotein-cholesterol and mevalonate for growth.	Mevalonic Acid	356-366	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	64-111
3880763-0	1985	Reduced glutathione in Chinese hamster ovary cells protects against inactivation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by 2-mercaptoethanol disulfide.	1,2-ethanedithiol	135-162	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	84-131
6643457-1	1983	3-Hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase) converts HMG-CoA to mevalonate, a key intermediate in the formation of cholesterol and several nonsterol isoprenoid compounds.	Cholesterol	139-150	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	0-47
6643457-1	1983	3-Hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase) converts HMG-CoA to mevalonate, a key intermediate in the formation of cholesterol and several nonsterol isoprenoid compounds.	Cholesterol	139-150	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	49-66
6643457-1	1983	3-Hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase) converts HMG-CoA to mevalonate, a key intermediate in the formation of cholesterol and several nonsterol isoprenoid compounds.	Terpenes	173-183	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	0-47
6643457-1	1983	3-Hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase) converts HMG-CoA to mevalonate, a key intermediate in the formation of cholesterol and several nonsterol isoprenoid compounds.	Terpenes	173-183	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	49-66
3771561-10	1986	24(R)-Hydroxycholesterol and its 24(S) epimer exhibited affinity for the binding protein and repressed 3-hydroxy-3-methylglutaryl-CoA reductase.	(r)-hydroxycholesterol	2-24	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	103-143
2411835-0	1985	Role of mevalonate in regulation of cholesterol synthesis and 3-hydroxy-3-methylglutaryl coenzyme A reductase in cultured cells and their cytoplasts.	Mevalonic Acid	8-18	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	62-109
2411835-1	1985	H4-II-E-C3 hepatoma cells in culture respond to lipid-depleted media and to mevinolin with increased sterol synthesis from [14C]acetate and rise of 3-hydroxy-3-methylglutaryl coenzyme A reductase levels.	Lovastatin	76-85	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	148-195
3880763-0	1985	Reduced glutathione in Chinese hamster ovary cells protects against inactivation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by 2-mercaptoethanol disulfide.	Glutathione	8-19	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	84-131
6705048-0	1984	Increase in membrane cholesterol: a possible trigger for degradation of HMG CoA reductase and crystalloid endoplasmic reticulum in UT-1 cells.	Cholesterol	21-32	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	72-89
6705048-1	1984	The crystalloid endoplasmic reticulum (ER) houses large amounts of HMG CoA reductase, the rate-controlling enzyme in cholesterol synthesis.	Cholesterol	117-128	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	67-84
6139093-1	1983	Decreased activities of both 3-hydroxy-3-methylglutaryl coenzyme A (HMG CoA) synthase and HMG CoA reductase are observed in the presence of sterol in the Chinese hamster ovary (CHO) fibroblast.	Sterols	140-146	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	90-107
6139093-3	1983	Permanently repressed levels of both HMG CoA synthase and HMG CoA reductase activities are observed in another CHO mutant, phenotypically a mevalonate auxotroph.	cho	111-114	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	58-75
6139093-3	1983	Permanently repressed levels of both HMG CoA synthase and HMG CoA reductase activities are observed in another CHO mutant, phenotypically a mevalonate auxotroph.	Mevalonic Acid	140-150	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	58-75
6139093-4	1983	Mevinolin, a competitive inhibitor of HMG CoA reductase, has no effect on HMG CoA synthase activity measured in vitro.	Lovastatin	0-9	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	38-55
6139093-5	1983	Incubation of CHO cells with sublethal concentrations of mevinolin produces an inhibition of the conversion of [14C]acetate to cholesterol and results in elevated levels of both HMG CoA synthase and HMG CoA reductase activities.	cho	14-17	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	199-216
6643457-7	1983	The activities of acetoacetyl-CoA thiolase and HMG-CoA synthase, the two enzymes that precede HMG-CoA reductase in the cholesterol biosynthetic pathway, were normal or slightly elevated in UT-2 cells.	Cholesterol	119-130	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	94-111
6643457-1	1983	3-Hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase) converts HMG-CoA to mevalonate, a key intermediate in the formation of cholesterol and several nonsterol isoprenoid compounds.	Mevalonic Acid	88-98	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	0-47
6139093-5	1983	Incubation of CHO cells with sublethal concentrations of mevinolin produces an inhibition of the conversion of [14C]acetate to cholesterol and results in elevated levels of both HMG CoA synthase and HMG CoA reductase activities.	Lovastatin	57-66	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	199-216
6643457-1	1983	3-Hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase) converts HMG-CoA to mevalonate, a key intermediate in the formation of cholesterol and several nonsterol isoprenoid compounds.	Mevalonic Acid	88-98	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	49-66
6553055-0	1983	Inhibition of degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by mevinolin.	Lovastatin	80-89	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	29-76
6685129-1	1983	The crystalloid endoplasmic reticulum (ER) consists of hexagonally packed membrane tubules that contain 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMG CoA reductase), an intrinsic membrane protein that catalyses the rate-limiting step in cholesterol synthesis.	Cholesterol	244-255	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	96-170
7085625-0	1982	Analysis of regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in a somatic cell mutant auxotrophic for mevalonate.	Mevalonic Acid	115-125	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	26-73
6863296-1	1983	32P-labeled cDNA probes were used to study levels of genomic DNA and regulation of mRNA for 3-hydroxy-3-methylglutaryl coenzyme A reductase in UT-1 cells, a clone of compactin-resistant Chinese hamster ovary cells that have a 100-1000-fold increase in the amount of reductase protein.	Phosphorus-32	0-3	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	92-139
7126620-1	1982	The activity of the rate-limiting enzyme of the cholesterol biosynthetic pathway, 3-hydroxy-3-methylglutaryl coenzyme A reductase in Chinese hamster ovary (CHO) cells decreased more rapidly in cells treated with 25-hydroxycholesterol alone (t 1/2 = 1.5 h) than in those incubated with cycloheximide alone (t 1/2 = 5 h).	Cholesterol	48-59	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	82-129
7126620-1	1982	The activity of the rate-limiting enzyme of the cholesterol biosynthetic pathway, 3-hydroxy-3-methylglutaryl coenzyme A reductase in Chinese hamster ovary (CHO) cells decreased more rapidly in cells treated with 25-hydroxycholesterol alone (t 1/2 = 1.5 h) than in those incubated with cycloheximide alone (t 1/2 = 5 h).	25-hydroxycholesterol	212-233	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	82-129
7126620-1	1982	The activity of the rate-limiting enzyme of the cholesterol biosynthetic pathway, 3-hydroxy-3-methylglutaryl coenzyme A reductase in Chinese hamster ovary (CHO) cells decreased more rapidly in cells treated with 25-hydroxycholesterol alone (t 1/2 = 1.5 h) than in those incubated with cycloheximide alone (t 1/2 = 5 h).	Cycloheximide	285-298	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	82-129
6951166-1	1982	We have developed a line of Chinese hamster ovary cells with a 500-fold increase in 3-hydroxy-3-methylglutaryl-coenzyme A reductase, the membrane-bound enzyme that controls cholesterol synthesis.	Cholesterol	173-184	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	84-131
7135162-3	1982	Cholesterol biosynthesis, 3-hydroxy-3-methylglutaryl coenzyme A reductase activity, and growth of the mutant cells were coordinately resistant to oxygenated sterols in the culture medium, and this resistance was expressed as a dominant trait in somatic cell hybrids of the wild-type and mutant cells.	Sterols	157-164	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	26-73
7240242-1	1981	ML236B is a potent competitive inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase) (EC 1.1.1.34), the major regulatory enzyme in cholesterol biosynthesis.	mevastatin	0-6	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	44-91
7197282-2	1981	Treatment of CHO-K1 cells with CTAB or ethanol at concentrations that produce comparable increases of membrane fluidity produce to 2- to 3-fold increase of microsomal membrane cholesterol to phospholipid ratio and a 2- to 3-fold increase of the activity of the rate-limiting enzyme of cholesterol biosynthesis, 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase.	Cetrimonium	31-35	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	311-368
7197282-2	1981	Treatment of CHO-K1 cells with CTAB or ethanol at concentrations that produce comparable increases of membrane fluidity produce to 2- to 3-fold increase of microsomal membrane cholesterol to phospholipid ratio and a 2- to 3-fold increase of the activity of the rate-limiting enzyme of cholesterol biosynthesis, 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase.	Ethanol	39-46	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	311-368
7240242-1	1981	ML236B is a potent competitive inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase) (EC 1.1.1.34), the major regulatory enzyme in cholesterol biosynthesis.	Cholesterol	158-169	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	44-91
7240196-0	1981	Evidence indicating that inactivation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by low density lipoprotein or by 25-hydroxycholesterol requires mediator protein(s) with rapid turnover rate.	25-hydroxycholesterol	122-143	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	41-88
33240873-5	2020	3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR) protein levels were increased in mutant cells, whereas HMGCR activity was significantly decreased, resulting in reduced cholesterol synthesis.	Cholesterol	169-180	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	0-40
33240873-5	2020	3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR) protein levels were increased in mutant cells, whereas HMGCR activity was significantly decreased, resulting in reduced cholesterol synthesis.	Cholesterol	169-180	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	42-47
33240873-5	2020	3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR) protein levels were increased in mutant cells, whereas HMGCR activity was significantly decreased, resulting in reduced cholesterol synthesis.	Cholesterol	169-180	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	104-109
17090658-1	2007	The pivotal event for sterol-induced degradation of the cholesterol biosynthetic enzyme HMG-CoA reductase is binding of its membrane domain to Insig proteins in the endoplasmic reticulum.	Sterols	22-28	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	88-105
29374057-2	2018	For example, high sterol concentrations can stimulate degradation of the rate-limiting cholesterol biosynthetic enzyme 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase, HMGCR).	Sterols	18-24	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	119-166
29374057-2	2018	For example, high sterol concentrations can stimulate degradation of the rate-limiting cholesterol biosynthetic enzyme 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase, HMGCR).	Sterols	18-24	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	187-192
29374057-2	2018	For example, high sterol concentrations can stimulate degradation of the rate-limiting cholesterol biosynthetic enzyme 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase, HMGCR).	Cholesterol	87-98	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	119-166
29374057-2	2018	For example, high sterol concentrations can stimulate degradation of the rate-limiting cholesterol biosynthetic enzyme 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase, HMGCR).	Cholesterol	87-98	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	187-192
29374057-6	2018	We found that knockdown of both ring finger protein 145 (Rnf145) and gp78 genes abrogates sterol-induced degradation of HMGCR in CHO cells.	Sterols	90-96	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	120-125
29374057-9	2018	Of note, amino acid substitutions in the YLYF or of Cys-537 completely abolished RNF145-mediated HMGCR degradation.	Cysteine	52-55	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	97-102
29374057-10	2018	In summary, our study reveals that RNF145, along with gp78, promotes HMGCR degradation in response to elevated sterol levels and identifies residues essential for RNF145 function.	Sterols	111-117	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	69-74
19514934-1	2009	The 3-hydroxy-3-methylglutaryl (HMG)-coenzyme A reductase inhibitor, lovastatin (lova), has been reported to both sensitize to, and protect against, the toxic effects of the antitumor anthracycline doxorubicin (dox) in cellular and in vivo systems.	Lovastatin	69-79	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	4-57
19514934-1	2009	The 3-hydroxy-3-methylglutaryl (HMG)-coenzyme A reductase inhibitor, lovastatin (lova), has been reported to both sensitize to, and protect against, the toxic effects of the antitumor anthracycline doxorubicin (dox) in cellular and in vivo systems.	Lovastatin	69-73	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	4-57
19514934-1	2009	The 3-hydroxy-3-methylglutaryl (HMG)-coenzyme A reductase inhibitor, lovastatin (lova), has been reported to both sensitize to, and protect against, the toxic effects of the antitumor anthracycline doxorubicin (dox) in cellular and in vivo systems.	Anthracyclines	184-197	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	4-57
19514934-1	2009	The 3-hydroxy-3-methylglutaryl (HMG)-coenzyme A reductase inhibitor, lovastatin (lova), has been reported to both sensitize to, and protect against, the toxic effects of the antitumor anthracycline doxorubicin (dox) in cellular and in vivo systems.	Doxorubicin	198-209	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	4-57
19514934-1	2009	The 3-hydroxy-3-methylglutaryl (HMG)-coenzyme A reductase inhibitor, lovastatin (lova), has been reported to both sensitize to, and protect against, the toxic effects of the antitumor anthracycline doxorubicin (dox) in cellular and in vivo systems.	Doxorubicin	198-201	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	4-57
17090658-1	2007	The pivotal event for sterol-induced degradation of the cholesterol biosynthetic enzyme HMG-CoA reductase is binding of its membrane domain to Insig proteins in the endoplasmic reticulum.	Cholesterol	56-67	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	88-105
10946023-1	2000	CHO cells expressing the liver-specific gene product cholesterol-7alpha-hydroxylase showed a 6-fold increase in the biosynthesis of [(14)C]cholesterol from [(14)C]acetate, as well as increased enzymatic activities of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase and squalene synthase.	Cholesterol	53-64	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	217-274
15247248-0	2004	Isolation of mutant cells lacking Insig-1 through selection with SR-12813, an agent that stimulates degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase.	SR 12813	65-73	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	115-162
15352124-0	2004	Proto oncogene/eukaryotic translation initiation factor (eIF) 4E attenuates mevalonate-mediated regulation of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase synthesis.	Mevalonic Acid	76-86	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	110-167
10625499-0	2000	Characterization of peroxisomal 3-hydroxy-3-methylglutaryl coenzyme A reductase in UT2 cells: sterol biosynthesis, phosphorylation, degradation, and statin inhibition.	Sterols	94-100	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	32-79
9087171-1	1997	Although UT-2 cells, a mutant clone of Chinese hamster ovary cells, have been shown to require mevalonate for growth due to a deficiency in 3-hydroxy-3-methylglutaryl-CoA reductase, the precise mevalonate-derived product(s) essential for proliferation has not been identified.	Mevalonic Acid	95-105	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	140-180
7713903-4	1995	In the presence of BFA (1 microgram/ml), 25-hydroxycholesterol-mediated suppression of mRNAs for HMG-CoA reductase, the low density lipoprotein receptor, and farnesyl-diphosphate synthase was almost completely blocked.	Brefeldin A	19-22	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	97-114
8898195-5	1996	SCAP has multiple membrane-spanning regions, five of which resemble the sterol-sensing domain of HMG CoA reductase, an endoplasmic reticulum enzyme whose degradation is accelerated by sterols.	Sterols	184-191	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	97-114
7713903-4	1995	In the presence of BFA (1 microgram/ml), 25-hydroxycholesterol-mediated suppression of mRNAs for HMG-CoA reductase, the low density lipoprotein receptor, and farnesyl-diphosphate synthase was almost completely blocked.	25-hydroxycholesterol	41-62	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	97-114
7713903-8	1995	Monensin was also found to block the effects of 25-hydroxycholesterol on suppression of HMG-CoA reductase.	25-hydroxycholesterol	48-69	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	88-105
7713903-10	1995	In contrast to CHO cells, BFA-resistant PtK1 cells displayed normal down-regulation of HMG-CoA reductase and an intact Golgi apparatus in the presence of BFA and 25-hydroxycholesterol.	Brefeldin A	26-29	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	87-104
7616123-8	1995	The F7-7 alpha-methyl-15-ketosterol X lowered the levels of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in CHO-K1 cells with a potency equivalent to that of I. X showed significant hypocholesterolemic action upon oral administration to rats, with a potency far in excess of the 7 alpha-methyl-15-ketosterol IX lacking the F7 substitution.	alpha-methyl-15-ketosterol	9-35	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	60-107
1486662-1	1992	Chemical syntheses and spectral properties of 26-oxygenated derivatives of 3 beta-hydroxy-5 alpha-cholest-8(14)-en-15-one and their effects on 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in CHO-K1 cells.	cholest-8(14)-en-3-ol-15-one	75-121	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	143-190
7820900-1	1994	Synthesis and spectral properties of 3 beta-hydroxy-5 alpha-cholestan-15-one and its 17 beta-epimer and their effects on 3-hydroxy-3-methylglutaryl coenzyme A reductase activity.	3 beta-hydroxy-5 alpha-cholestan-15-one	37-76	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	121-168
7844177-1	1994	The rate-limiting enzyme in cholesterol biosynthesis, 3-hydroxy-3-methylglutaryl-coenzyme A (HMG CoA) reductase, is regulated at a number of levels.	Cholesterol	28-39	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	54-111
7844177-11	1994	CHO cells transfected with DNA encoding HM-Gal were exposed to mevalonic acid, which enhances the rate of HMG CoA reductase degradation several fold, and leads to the reduction of the steady state levels of HM-Gal by 80-90%.	Mevalonic Acid	63-77	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	106-123
7844177-11	1994	CHO cells transfected with DNA encoding HM-Gal were exposed to mevalonic acid, which enhances the rate of HMG CoA reductase degradation several fold, and leads to the reduction of the steady state levels of HM-Gal by 80-90%.	cyclohexenoesculetin-beta-galactoside	42-46	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	106-123
8102788-1	1993	Cholesterol biosynthesis and uptake are controlled by a classic end product-feedback mechanism whereby elevated cellular sterol levels suppress transcription of the genes encoding 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) synthase, HMG-CoA reductase, and the low-density lipoprotein receptor.	Cholesterol	0-11	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	238-255
8102788-1	1993	Cholesterol biosynthesis and uptake are controlled by a classic end product-feedback mechanism whereby elevated cellular sterol levels suppress transcription of the genes encoding 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) synthase, HMG-CoA reductase, and the low-density lipoprotein receptor.	Sterols	5-11	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	238-255
8073444-7	1994	The 25-hydroxysterol IV and the 25-fluorosterol III differed markedly in their effects on the levels of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in CHO-K1 cells.	25-hydroxysterol	4-20	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	104-151
8073444-7	1994	The 25-hydroxysterol IV and the 25-fluorosterol III differed markedly in their effects on the levels of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in CHO-K1 cells.	25-fluorosterol	32-47	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	104-151
8270199-0	1993	Pleurotus fungi produce mevinolin, an inhibitor of HMG CoA reductase.	Lovastatin	24-33	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	51-68
8270199-1	1993	Fungi of the genus Pleurotus were shown to produce the 3-hydroxy-3-methylglutaryl-CoA reductase inhibitor mevinolin.	Lovastatin	106-115	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	55-95
7693673-0	1993	Modulation of 3-hydroxy-3-methylglutaryl-CoA reductase by 15 alpha-fluorolanost-7-en-3 beta-ol.	alpha-fluorolanost-7-en-3 beta-ol	61-94	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	14-54
7693673-5	1993	When cultured cells are treated with the fluorinated lanosterol analogue, a decrease in 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase activity and immunoreactive protein was observed.	Lanosterol	53-63	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	88-134
1486662-9	1992	The 3,15-diketone VII was found to be highly active in lowering the levels of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in CHO-K1 cells, with a potency comparable to that of I.	3,15-diketone	4-17	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	78-125
1618856-1	1992	We have studied the regulated degradation of the enzyme 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase within the endoplasmic reticulum in cells permeabilized with digitonin.	Digitonin	175-184	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	56-113
1423803-1	1992	Chemical synthesis of 7 alpha-ethyl and 16 alpha-ethyl derivatives of delta 8(14)-15-oxygenated sterols and their effects on 3-hydroxy-3-methylglutaryl coenzyme A reductase in CHO-K1 cells.	Sterols	96-103	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	125-172
1606178-8	1992	In agreement with an increased synthesis of cholesterol, a 2-3-fold higher 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) reductase activity was measured in both mutant cell lines.	Cholesterol	44-55	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	75-125
1813179-8	1991	The 25-aza analog (VII) of the 15-ketosterol (I), at a concentration of 1.0 microM, caused a 47% lowering of the level of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in Chinese hamster ovary cells.	25-aza	4-10	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	122-169
1533625-1	1992	3-Hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase) is located in the endoplasmic reticulum (ER) and responds to rapid degradation which is regulated by mevalonate or sterols.	Mevalonic Acid	169-179	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	0-66
1533625-1	1992	3-Hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase) is located in the endoplasmic reticulum (ER) and responds to rapid degradation which is regulated by mevalonate or sterols.	Sterols	183-190	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	0-66
1525963-1	1992	Chemical synthesis and spectral properties of (25R)-5 alpha-cholest-8(14)-ene-3 beta,15 beta,26-triol, a potential metabolite of 3 beta-hydroxy-5 alpha-cholest-8(14)-en-15-one and its effects on 3-hydroxy-3-methylglutaryl-coenzyme A reductase in CHO-K1 cells.	(25r)-5 alpha-cholest-8(14)-ene-3 beta,15 beta,26-triol	46-101	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	195-242
1525963-5	1992	The triol was found to be very potent in lowering the levels of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in Chinese hamster ovary cells.	Calcitriol	4-9	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	64-111
1813179-8	1991	The 25-aza analog (VII) of the 15-ketosterol (I), at a concentration of 1.0 microM, caused a 47% lowering of the level of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in Chinese hamster ovary cells.	COLESTOLONE	31-44	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	122-169
1856223-1	1991	Sterol-dependent regulation of the 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase promoter was previously localized to a 42-base pair region containing an octamer sequence, referred to as the sterol regulatory element (SRE-1).	Sterols	0-6	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	35-92
1856223-1	1991	Sterol-dependent regulation of the 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase promoter was previously localized to a 42-base pair region containing an octamer sequence, referred to as the sterol regulatory element (SRE-1).	Sterols	203-209	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	35-92
1673968-1	1991	Sterols reduce the activity of 3-hydroxy-3-methyl-glutaryl-coenzyme A reductase (HMG-CoA reductase) transcriptionally by inhibiting the synthesis of reductase mRNA and posttranscriptionally by accelerating degradation of the enzyme.	Sterols	0-7	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	81-98
1940644-1	1991	Characterization of beta,gamma-unsaturated analogs of 3 beta-hydroxy-5 alpha-cholest-8(14)-en-15-one and their effects on 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in CHO-K1 cells.	beta,gamma-unsaturated	20-42	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	122-169
1940644-1	1991	Characterization of beta,gamma-unsaturated analogs of 3 beta-hydroxy-5 alpha-cholest-8(14)-en-15-one and their effects on 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in CHO-K1 cells.	cholest-8(14)-en-3-ol-15-one	54-100	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	122-169
1906466-1	1991	3-Hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase is a key regulatory enzyme of cholesterol biosynthesis and is located in the endoplasmic reticulum (ER).	Cholesterol	88-99	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	0-57
1673968-3	1991	In the current studies, we show that one line of sterol-resistant mutant cells (SRD-3 cells) retains the ability to slow the degradation of HMG-CoA reductase by 7-fold in response to treatment with compactin, an inhibitor of reductase that blocks sterol synthesis.	Sterols	49-55	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	140-157
1673968-3	1991	In the current studies, we show that one line of sterol-resistant mutant cells (SRD-3 cells) retains the ability to slow the degradation of HMG-CoA reductase by 7-fold in response to treatment with compactin, an inhibitor of reductase that blocks sterol synthesis.	mevastatin	198-207	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	140-157
2117604-9	1990	25-Hydroxycholesterol is a poor regulator of the synthesis and degradation of the rate-limiting enzyme, 3-hydroxy-3-methylglutaryl-coenzyme A reductase in crB in comparison to the wild-type Chinese hamster ovary K1 cells.	25-hydroxycholesterol	0-21	3-hydroxy-3-methylglutaryl-coenzyme A reductase	Cricetulus griseus	104-151