PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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 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 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 6643457-7 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 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 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 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 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 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 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 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 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 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 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 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