Academic literature on the topic '3-Hydroxy-3-methylglutaryl coenzyme A reductase'

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Journal articles on the topic "3-Hydroxy-3-methylglutaryl coenzyme A reductase"

1

Ness, G. C., C. E. Sample, M. Smith, L. C. Pendleton, and D. C. Eichler. "Characteristics of rat liver microsomal 3-hydroxy-3-methylglutaryl-coenzyme A reductase." Biochemical Journal 233, no. 1 (1986): 167–72. http://dx.doi.org/10.1042/bj2330167.

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A procedure for the preparation of rat liver microsomal fractions essentially devoid of contaminating lysosomes is described. When this preparation was examined by immunoblotting with a rabbit antiserum to rat 3-hydroxy-3-methylglutaryl-CoA reductase, a single band corresponding to an Mr of 100000 was observed. No evidence was found for glycosylation of rat liver-3-hydroxy-3-methylglutaryl-CoA reductase. Native rat liver microsomal 3-hydroxy-3-methylglutaryl-CoA reductase differs from the purified proteolytically modified species in that it displays allosteric kinetics towards NADPH.
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2

Chin, D. J., G. Gil, J. R. Faust, J. L. Goldstein, M. S. Brown, and K. L. Luskey. "Sterols accelerate degradation of hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase encoded by a constitutively expressed cDNA." Molecular and Cellular Biology 5, no. 4 (1985): 634–41. http://dx.doi.org/10.1128/mcb.5.4.634.

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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. We selected a line of permanently transfected cells, designated TR-36 cells, that expressed high levels of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity and thus grew in the absence of low density lipoprotein a
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3

Chin, D. J., G. Gil, J. R. Faust, J. L. Goldstein, M. S. Brown, and K. L. Luskey. "Sterols accelerate degradation of hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase encoded by a constitutively expressed cDNA." Molecular and Cellular Biology 5, no. 4 (1985): 634–41. http://dx.doi.org/10.1128/mcb.5.4.634-641.1985.

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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. We selected a line of permanently transfected cells, designated TR-36 cells, that expressed high levels of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity and thus grew in the absence of low density lipoprotein a
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4

Jones, Peter H. "Tachyphylaxis in 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors." American Journal of Cardiology 87, no. 8 (2001): 1032. http://dx.doi.org/10.1016/s0002-9149(01)01543-0.

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5

Pasco, J. A. "Falls and 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase Inhibitors." Archives of Internal Medicine 162, no. 20 (2002): 2381. http://dx.doi.org/10.1001/archinte.162.20.2381.

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6

Heise, Norton, and Fred R. Opperdoes. "Localisation of a 3-Hydroxy-3-methylglutaryl-Coenzyme A Reductase in the Mitochondrial Matrix of Trypanosoma brucei Procyclics." Zeitschrift für Naturforschung C 55, no. 5-6 (2000): 473–77. http://dx.doi.org/10.1515/znc-2000-5-626.

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Contrary to Leishmania spp. and Trypanosoma cruzi, Trypanosoma brucei bloodstream forms do not synthesise their own sterols but take these compounds in the form of cholesterol directly from the mammalian host. However, procyclic insect stages synthesise ergosterol rather than cholesterol. Here the sub-cellular localisation of the first committed enzyme of this pathway of isoprenoid synthesis 3-hydroxy-3-methylglutaryl-coenzyme A reductase in T. brucei procyclics (0.9 nmol. min-1 . mg-1 protein) was carried out using both cell-fractionation by isopycnic centrifugation and digitonin-titration ex
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7

Desager, Jean-Pierre, and Yves Horsmans. "Clinical Pharmacokinetics of 3-Hydroxy-3-Methylglutaryl-Coenzyme A Reductase Inhibitors." Clinical Pharmacokinetics 31, no. 5 (1996): 348–71. http://dx.doi.org/10.2165/00003088-199631050-00003.

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8

Dreyer, Geoffrey B., Clare T. Garvie§, Brian W. Metcalf, Thomas D. Meek, and Ruth J. Mayer. "Phosphinic acid inhibitors of 3-hydroxy-3-methylglutaryl-coenzyme a reductase." Bioorganic & Medicinal Chemistry Letters 1, no. 3 (1991): 151–54. http://dx.doi.org/10.1016/s0960-894x(01)80788-5.

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9

Wu, Yan, Fang-Jun Xiong, and Fen-Er Chen. "Stereoselective synthesis of 3-hydroxy-3-methylglutaryl–coenzyme A reductase inhibitors." Tetrahedron 71, no. 45 (2015): 8487–510. http://dx.doi.org/10.1016/j.tet.2015.07.059.

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10

Moghadasian, Mohammed H. "Clinical pharmacology of 3-hydroxy-3-methylglutaryl coenzyme a reductase inhibitors." Life Sciences 65, no. 13 (1999): 1329–37. http://dx.doi.org/10.1016/s0024-3205(99)00199-x.

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