Role for sterol regulatory element binding protein in the regulation of farnesyl diphosphate synthase and in the control of cellular levels of cholesterol and triglyceride: evidence from sterol regulation-defective cells.
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[1] P. Edwards,et al. Sterol regulatory element binding protein binds to a cis element in the promoter of the farnesyl diphosphate synthase gene. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[2] Mary K. Bennett,et al. Sterol Regulation of Fatty Acid Synthase Promoter , 1995, The Journal of Biological Chemistry.
[3] P. Edwards,et al. NF-Y Has a Novel Role in Sterol-dependent Transcription of Two Cholesterogenic Genes (*) , 1995, The Journal of Biological Chemistry.
[4] I. Shechter,et al. Molecular Cloning and Functional Analysis of the Promoter of the Human Squalene Synthase Gene (*) , 1995, The Journal of Biological Chemistry.
[5] Jasmine Chen,et al. Identification of a nuclear receptor that is activated by farnesol metabolites , 1995, Cell.
[6] B. Bloom,et al. Natural and synthetic non-peptide antigens recognized by human γδ T cells , 1995, Nature.
[7] P. Edwards,et al. Identification of a 6-base pair element involved in the sterol-mediated transcriptional regulation of farnesyl diphosphate synthase. , 1994, The Journal of biological chemistry.
[8] P. Edwards,et al. Identification of farnesol as the non-sterol derivative of mevalonic acid required for the accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase. , 1994, The Journal of biological chemistry.
[9] X. Hua,et al. SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis , 1994, Cell.
[10] R. D. Simoni,et al. Non-sterol compounds that regulate cholesterogenesis. Analogues of farnesyl pyrophosphate reduce 3-hydroxy-3-methylglutaryl-coenzyme A reductase levels. , 1994, The Journal of biological chemistry.
[11] T. Osborne,et al. Two separate sites contribute to AP-1 activation of the promoter for 3-hydroxy-3-methylglutaryl coenzyme A synthase. , 1994, Nucleic acids research.
[12] M. Brown,et al. SREBP-2, a second basic-helix-loop-helix-leucine zipper protein that stimulates transcription by binding to a sterol regulatory element. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[13] M. Evans,et al. Loss of transcriptional activation of three sterol-regulated genes in mutant hamster cells , 1993, Molecular and cellular biology.
[14] ADD1: a novel helix-loop-helix transcription factor associated with adipocyte determination and differentiation. , 1993, Molecular and cellular biology.
[15] X. Wang,et al. Nuclear protein that binds sterol regulatory element of low density lipoprotein receptor promoter. II. Purification and characterization. , 1993, The Journal of biological chemistry.
[16] J. Ericsson,et al. Biosynthesis of trans,trans,trans-geranylgeranyl diphosphate by the cytosolic fraction from rat tissues. , 1992, Biochemical and biophysical research communications.
[17] P. Edwards,et al. Molecular cloning and promoter analysis of the rat liver farnesyl diphosphate synthase gene. , 1992, The Journal of biological chemistry.
[18] J. Ericsson,et al. Characterization and distribution of cis-prenyl transferase participating in liver microsomal polyisoprenoid biosynthesis. , 1991, European journal of biochemistry.
[19] P. Dawson,et al. Genetic distinction between sterol-mediated transcriptional and posttranscriptional control of 3-hydroxy-3-methylglutaryl-coenzyme A reductase. , 1991, The Journal of biological chemistry.
[20] W. Maltese. Posttranslational modification of proteins by isoprenoids in mammalian cells , 1990, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[21] J. Goldstein,et al. Regulation of the mevalonate pathway , 1990, Nature.
[22] M. Brown,et al. Loss of transcriptional repression of three sterol-regulated genes in mutant hamster cells. , 1989, The Journal of biological chemistry.
[23] K. Svenson,et al. Molecular Cloning and Sequence of a Cholesterol-Repressible Enzyme Related to Prenyltransferase in the Isoprene Biosynthetic Pathway , 1987, Molecular and cellular biology.
[24] Warnick Gr. Enzymatic methods for quantification of lipoprotein lipids. , 1986 .
[25] J. Sambrook,et al. Molecular Cloning: A Laboratory Manual , 2001 .
[26] M. M. Bradford. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.