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SREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver
Open accessAbstract
Lipid homeostasis in vertebrate cells is regulated by a family of membrane-bound transcription factors designated sterol regulatory element-binding proteins (SREBPs).SREBPs directly activate the expression of more than 30 genes dedicated to the synthesis and uptake of cholesterol, fatty acids, triglycerides, and phospholipids, as well as the NADPH cofactor required to synthesize these molecules (1-4).In the liver, three SREBPs regulate the production of lipids for export into the plasma as lipoproteins and into the bile as micelles.The complex, interdigitated roles of these three SREBPs have been dissected through the study of ten different lines of gene-manipulated mice.These studies form the subject of this review.
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“By contrast, Srebp-1c is transcribed at extremely high levels in response to insulin (6, 28)”
From miR-33a/b contribute to the regulation of fatty acid metabolism and insulin signaling (2011) · cites this paper as [6]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“As SREBPs contain an SRE in their promoter region, they induce their own expression in a positive feedback mechanism4,18.”
From Haploid genetic screens identify SPRING/C12ORF49 as a determinant of SREBP signaling and cholesterol metabolism (2020) · cites this paper as [4]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“An additional level of regulation of the genes involved in cholesterol uptake and synthesis is provided by SREBP signaling, in which low cellular sterol levels lead to the SCAP-mediated trafficking of SREBP proteins from the ER to the Golgi, where they are cleaved by resident proteases (encoded by MBTPS1 and MBTPS2) to release and activate their transcription factor domains[7,8].”
From Genome-scale CRISPR screening for modifiers of cellular LDL uptake (2021) · cites this paper as [7]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Two transcription factor families with opposing actions – the liver-X receptors (LXRs) and the sterol regulatory element-binding proteins (SREBPs) – are the main orchestrators of this balance (Hong and Tontonoz, 2014; Horton et al., 2002).”
From Inhibition of cholesterol biosynthesis through RNF145-dependent ubiquitination of SCAP (2017) · cites this paper as Horton et al., 2002
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
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“In the liver, SREBP1c is the prominent SREBP1 isoform and primarily controls fatty acid synthesis and mobilization, while SREBP2 controls cholesterol biosynthesis and lipoprotein uptake [12,13].”
From Loss of the E3 ubiquitin ligase MARCHF6 alters hepatic lipid metabolism and drives spontaneous hepatosteatosis (2026) · cites this paper as [12]
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“The intracellular cholesterol economy is largely regulated by the sterol response element binding protein (SREBPs), a group of transcription factors that regulate genes involved in the biosynthesis of cholesterol and fatty acids (13).”
From The Molecular Biology, Biochemistry, and Physiology of Human Steroidogenesis and Its Disorders (2011) · cites this paper as [13]
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“SREBP1a and SREBP1c are responsible for fatty acid metabolism and SREBP2 primarily for cholesterol synthesis through increasing the expression of HMG-CoA reductase (HMGCR) [32].”
From HIV-TAT dysregulates microglial lipid metabolism through SREBP2/miR-124 axis: Implication of lipid droplet accumulation microglia in NeuroHIV (2025) · cites this paper as [32]
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In the citing paper
“However, SREBPs not only activate cholesterol synthesis but also fatty acid and phospholipid synthesis (2).”
From Expression of miR-33 from an SREBP2 Intron Inhibits Cholesterol Export and Fatty Acid Oxidation* (2010) · cites this paper as [2]
The cited source says what the claim attributes to it.
In the citing paper
“Genes involved in its synthesis are coordinately up-regulated by the action of SREBP transcription factors (2).”
From Expression of miR-33 from an SREBP2 Intron Inhibits Cholesterol Export and Fatty Acid Oxidation* (2010) · cites this paper as [2]
The cited source says what the claim attributes to it.
In the citing paper
“SREBP-1c regulates the transcription of genes involved in fatty acid metabolism, such as fatty acid synthase (FASN) (5–7).”
From miR-33a/b contribute to the regulation of fatty acid metabolism and insulin signaling (2011) · cites this paper as [6]
The cited source says what the claim attributes to it.
In the citing paper
“SREBP-2 regulates the transcription of cholesterol-related genes, such as 3-hydroxy-3-methylglutaryl CoA reductase (HMGCR), which catalyzes a rate-limiting step in cholesterol biosynthesis, and the low-density lipoprotein receptor (LDLr), which imports cholesterol from the blood (5–7).”
From miR-33a/b contribute to the regulation of fatty acid metabolism and insulin signaling (2011) · cites this paper as [6]
The cited source says what the claim attributes to it.
In the citing paper
“The sterol-regulatory element binding proteins (SREBP) are central transcriptional regulators of lipid metabolism.”
From Haploid genetic screens identify SPRING/C12ORF49 as a determinant of SREBP signaling and cholesterol metabolism (2020) · cites this paper as [4]
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In the citing paper
“The SREBP pathway is activated when cellular cholesterol levels decline as a means to increase cholesterol synthesis and uptake (4).”
From A MARCH6 and IDOL E3 Ubiquitin Ligase Circuit Uncouples Cholesterol Synthesis from Lipoprotein Uptake in Hepatocytes (2016) · cites this paper as [4]
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In the citing paper
“The released N-terminal SREBP-1 and −2 transcriptional domains translocate to the nucleus to activate transcriptional programs that promote fatty acid and cholesterol biosynthesis, respectively8.”
From Hepatic SREBP signaling requires SPRING to govern systemic lipid metabolism in mice and humans (2023) · cites this paper as [8]
In the citing paper
“The cellular signal driving this increased hepatic de novo lipogenesis can most likely be attributed to hyperinsulinemia promoting increased expression of the sterol regulatory element binding protein-1c in the liver, which coordinately regulates transcription of all of the key enzymes involved in lipogenesis (24).”
From The role of skeletal muscle insulin resistance in the pathogenesis of the metabolic syndrome (2007) · cites this paper as [24]
In the citing paper
“Recently, 2 additional transcription factors, X-box binding protein 1 (XBP1) and CHO response element-binding protein (ChREBP), have been identified as inducers of hepatic lipogenesis in response to ingested CHOs (eg, fructose and glucose) that is independent of insulin.431,432”
From Triglycerides and Cardiovascular Disease: A Scientific Statement From the American Heart Association (2011) · cites this paper as [431]
In the citing paper
“likely due to overlapping functions allowing one gene to compensate for loss of the other[7]”
From Genome-scale CRISPR screening for modifiers of cellular LDL uptake (2021) · cites this paper as [7]
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Cites
Role of AMP-Activated Protein Kinase in Mechanism of Metformin Action
Zhou, G., Myers, R., Li, Y., Chen, Y., Shen, X., Fenyk-Melody, J., Wu, M., Ventre, J., Doebber, T., Fujii, N., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13505 · Cited by 5,652
Brown, M. S., & Goldstein, J. L. (1997) · Cell · doi:10.1016/s0092-8674(00)80213-5 · Cited by 3,834
Self-citationNonalcoholic Fatty Liver Disease
Marchesini, G., Brizi, M., Bianchi, G., Tomassetti, S., Bugianesi, E., Lenzi, M., McCullough, A. J., Natale, S., Forlani, G., & Melchionda, N. (2001) · Diabetes · doi:10.2337/diabetes.50.8.1844 · Cited by 2,581
Repa, J. J., Liang, G., Ou, J., Bashmakov, Y. K., Lobaccaro, J. A., Shimomura, I., Shan, B., Brown, M. S., Goldstein, J. L., & Mangelsdorf, D. J. (2000) · Genes & Development · doi:10.1101/gad.844900 · Cited by 1,724
Self-citationLeptin reverses insulin resistance and diabetes mellitus in mice with congenital lipodystrophy
Shimomura, I., Hammer, R. E., Ikemoto, S., Brown, M. S., & Goldstein, J. L. (1999) · Nature · doi:10.1038/43448 · Cited by 1,038
Self-citationStructural requirements of ligands for the oxysterol liver X receptors LXRα and LXRβ
Janowski, B. A., Grogan, M. J., Jones, S. A., Wisely, G. B., Kliewer, S. A., Corey, E. J., & Mangelsdorf, D. J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.1.266 · Cited by 946
Shimomura, I., Matsuda, M., Hammer, R. E., Bashmakov, Y. K., Brown, M. S., & Goldstein, J. L. (2000) · Molecular Cell · doi:10.1016/s1097-2765(05)00010-9 · Cited by 860
Self-citationShimano, H., Horton, J. D., Hammer, R. E., Shimomura, I., Brown, M. S., & Goldstein, J. L. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118951 · Cited by 817
Self-citationJoseph, S. B., Laffitte, B. A., Patel, P. H., Watson, M. A., Matsukuma, K. E., Walczak, R., Collins, J. L., Osborne, T. F., & Tontonoz, P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111041200 · Cited by 795
Kim, J. B., Sarraf, P., Wright, M., Yao, K., Mueller, E., Solanes, G., Lowell, B. B., & Spiegelman, B. M. (1998) · Journal of Clinical Investigation · doi:10.1172/jci1411 · Cited by 792
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Kunkel, S. D., Elmore, C., Bongers, K. S., Ebert, S. M., Fox, D. K., Dyle, M. C., Bullard, S. A., & Adams, C. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039332 · Cited by 225
Cholesterol transport system: An integrated cholesterol transport model involved in atherosclerosis
Yu, X.-H., Zhang, D., Zheng, X., & Tang, C. (2018) · Progress in Lipid Research · doi:10.1016/j.plipres.2018.12.002 · Cited by 222
Even Cancer Cells Watch Their Cholesterol!
Riscal, R., Skuli, N., & Simon, M. C. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.09.008 · Cited by 223
Txnip balances metabolic and growth signaling via PTEN disulfide reduction
Hui, S. T. Y., Andres, A. M., Miller, A. K., Spann, N. J., Potter, D. W., Post, N. M., Chen, A. Z., Sachithanantham, S., Jung, D. Y., Kim, J. K., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800293105 · Cited by 214
Chakravarty, K., Cassuto, H., Reshef, L., & Hanson, R. W. (2005) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230590935479 · Cited by 223
Feedback modulation of cholesterol metabolism by the lipid-responsive non-coding RNA LeXis
Sallam, T., Jones, M. C., Gilliland, T., Zhang, L., Wu, X., Eskin, A., Sandhu, J., Casero, D., Vallim, T. Q. D. A., Hong, C., et al. (2016) · Nature · doi:10.1038/nature17674 · Cited by 212
Body Mass Index and Metastatic Renal Cell Carcinoma: Clinical and Biological Correlations
Albiges, L. K., Hakimi, A. A., Xie, W., McKay, R. R., Simantov, R., Lin, X., Lee, J., Rini, B. I., Srinivas, S., Bjarnason, G. A., et al. (2016) · Journal of Clinical Oncology · doi:10.1200/jco.2016.66.7311 · Cited by 217
Green, C. B., Douris, N., Kojima, S., Strayer, C. A., Fogerty, J., Lourim, D., Keller, S. R., & Besharse, J. C. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702448104 · Cited by 220
Regulation of cholesterol homeostasis
Goedeke, L., & Fernandez-Hernando, C. F. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0857-5 · Cited by 232
Wang, Q. A., Jiang, L., Wang, J., Li, S., Yu, Y., You, J., Zeng, R., Gao, X., Rui, L., Li, W., et al. (2008) · Hepatology · doi:10.1002/hep.22774 · Cited by 215
Miller, W. L. (2006) · Molecular Endocrinology · doi:10.1210/me.2006-0303 · Cited by 212
Involvement of mammalian sirtuin 1 in the action of ethanol in the liver
You, M., Liang, X., Ajmo, J. M., & Ness, G. C. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00575.2007 · Cited by 216
Mechanisms of regulation of gene expression by fatty acids
Nakamura, M., Cheon, Y., Li, Y., & Nara, T. (2004) · Lipids · doi:10.1007/s11745-004-1333-0 · Cited by 221
Identification of Two Mammalian Reductases Involved in the Two-carbon Fatty Acyl Elongation Cascade
Moon, Y.-A., & Horton, J. D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211684200 · Cited by 214
Self-citationAdlakha, Y. K., & Saini, N. (2014) · Molecular Cancer · doi:10.1186/1476-4598-13-33 · Cited by 213
Nakagawa, Y., Shimano, H., Yoshikawa, T., Ide, T., Tamura, M., Furusawa, M., Yamamoto, T., Inoue, N., Matsuzaka, T., Takahashi, A., et al. (2005) · Nature Medicine · doi:10.1038/nm1334 · Cited by 212
Park, J., Rho, H. K., Kim, K. H., Choe, S. S., Lee, Y. S., & Kim, J. B. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.12.5146-5157.2005 · Cited by 212
Kondo, A., Yamamoto, S., Nakaki, R., Shimamura, T., Hamakubo, T., Sakai, J., Kodama, T., Yoshida, T., Aburatani, H., & Osawa, T. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.02.006 · Cited by 205
Regulation of gene expression by glycolytic and gluconeogenic enzymes
Bian, X., Jiang, H., Meng, Y., Li, Y.-P., Fang, J., & Lu, Z. (2022) · Trends in Cell Biology · doi:10.1016/j.tcb.2022.02.003 · Cited by 211
Nutrigenomics: exploiting systems biology in the nutrition and health arena
van Ommen, B., & Stierum, R. H. (2002) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(02)00349-x · Cited by 209
Hegarty, B. D., Bobard, A., Hainault, I., Ferré, P., Bossard, P., & Foufelle, F. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405067102 · Cited by 208
Chronic intermittent hypoxia upregulates genes of lipid biosynthesis in obese mice
Li, J., Grigoryev, D. N., Ye, S. Q., Thorne, L. N., Schwartz, A. R., Smith, P. L., O'Donnell, C. P., & Polotsky, V. Y. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00522.2005 · Cited by 214
Reed, B. D., Charos, A. E., Szekely, A. M., Weissman, S. M., & Snyder, M. P. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000133 · Cited by 214
Do oxysterols control cholesterol homeostasis?
Björkhem, I. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0216388 · Cited by 207
Wu, H., Ng, R., Chen, X., Steer, C. J., & Song, G. (2015) · Gut · doi:10.1136/gutjnl-2014-308430 · Cited by 212
Nakatani, T., Kim, H.-J., Kaburagi, Y., Yasuda, K., & Ezaki, O. (2003) · Journal of Lipid Research · doi:10.1194/jlr.m200289-jlr200 · Cited by 203
Rudolph, M. C., McManaman, J. L., Hunter, L., Phang, T., & Neville, M. C. (2003) · Journal of Mammary Gland Biology and Neoplasia · doi:10.1023/b:jomg.0000010030.73983.57 · Cited by 204
Regulation of cholesterol homeostasis
van der Wulp, M. Y. M., Verkade, H. J., & Groen, A. K. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.06.007 · Cited by 210
Lowering LDL—not only how low, but how long?
Brown, M. S., & Goldstein, J. L. (2006) · Science · doi:10.1126/science.1125884 · Cited by 204
Self-citationInhibition of Notch signaling ameliorates insulin resistance in a FoxO1-dependent manner
Pajvani, U. B., Shawber, C. J., Samuel, V. T., Birkenfeld, A. L., Shulman, G. I., Kitajewski, J., & Accili, D. (2011) · Nature Medicine · doi:10.1038/nm.2378 · Cited by 193
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Plasma PCSK9 preferentially reduces liver LDL receptors in mice
Grefhorst, A., McNutt, M. C., Lagace, T. A., & Horton, J. D. (2008) · Journal of Lipid Research · doi:10.1194/jlr.m800027-jlr200 · Cited by 183
Self-citationMicroRNAs and lipid metabolism
Aryal, B., Singh, A. K., Rotllan, N., Price, N., & Fernández-Hernando, C. (2017) · Current Opinion in Lipidology · doi:10.1097/mol.0000000000000420 · Cited by 191
Lee, J. H., Giannikopoulos, P., Duncan, S. A., Wang, J., Johansen, C. T., Brown, J. D., Plutzky, J., Hegele, R. A., Glimcher, L. H., & Lee, A. (2011) · Nature Medicine · doi:10.1038/nm.2347 · Cited by 202
Mulvihill, E. E., Assini, J. M., Lee, J. K., Allister, E. M., Sutherland, B. G., Koppes, J. B., Sawyez, C. G., Edwards, J. Y., Telford, D. E., Charbonneau, A., et al. (2011) · Diabetes · doi:10.2337/db10-0589 · Cited by 202
Lipid metabolism emerges as a promising target for malignant glioma therapy
Guo, D., Bell, E. H., & Chakravarti, A. (2013) · CNS Oncology · doi:10.2217/cns.13.20 · Cited by 203
Pihlajamäki, J., Gylling, H. K., Miettinen, T. A., & Laakso, M. (2004) · Journal of Lipid Research · doi:10.1194/jlr.m300368-jlr200 · Cited by 202
Gouw, A. M., Margulis, K., Liu, N. S., Raman, S. J., Mancuso, A., Toal, G. G., Tong, L., Mosley, A. R., Hsieh, A. L., Sullivan, D. K., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.07.012 · Cited by 195
Ohgami, N., Ko, D. C., Thomas, M., Scott, M. P., Chang, C. C. Y., & Chang, T. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405255101 · Cited by 193
An Essential Requirement for the SCAP/SREBP Signaling Axis to Protect Cancer Cells from Lipotoxicity
Williams, K. J., Argus, J. P., Zhu, Y., Wilks, M. Q., Marbois, B. N., York, A. G., Kidani, Y., Pourzia, A. L., Akhavan, D., Lisiero, D. N., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-0382-t · Cited by 197
Matsuzaka, T., Shimano, H., Yahagi, N., Amemiya-Kudo, M., Okazaki, H., Tamura, Y., Iizuka, Y., Ohashi, K., Tomita, S., Sekiya, M., et al. (2004) · Diabetes · doi:10.2337/diabetes.53.3.560 · Cited by 196
Maetzel, D., Sarkar, S., Wang, H., Abi-Mosleh, L., Xu, P., Cheng, A. W., Gao, Q., Mitalipova, M., & Jaenisch, R. (2014) · Stem Cell Reports · doi:10.1016/j.stemcr.2014.03.014 · Cited by 195
Resveratrol as a calorie restriction mimetic: therapeutic implications
Chung, J. H., Manganiello, V., & Dyck, J. R. B. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.07.004 · Cited by 192
Cholesterol as a causative factor in Alzheimer's disease: a debatable hypothesis
Wood, W. G., Li, L., Müller, W. E., & Eckert, G. P. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12637 · Cited by 194
An integrated functional genomics screening program reveals a role for BMP-9 in glucose homeostasis
Chen, C., Grzegorzewski, K. J., Barash, S., Zhao, Q., Schneider, H., Wang, Q., Singh, M., Pukac, L., Bell, A. C., Duan, R., et al. (2003) · Nature Biotechnology · doi:10.1038/nbt795 · Cited by 199
Nuclear Factor-Eythroid 2–Related Factor 2 Prevents Alcohol-Induced Fulminant Liver Injury
Lamlé, J., Marhenke, S., Borlak, J. T., von Wasielewski, R., Eriksson, C. J. P., Geffers, R., Manns, M. P., Yamamoto, M. P., & Vogel, A. (2008) · Gastroenterology · doi:10.1053/j.gastro.2008.01.011 · Cited by 193
Breitkopf, S. B., Ricoult, S. J. H., Yuan, M., Xu, Y., Peake, D. A., Manning, B. D., & Asara, J. M. (2017) · Metabolomics · doi:10.1007/s11306-016-1157-8 · Cited by 193
Endoplasmic reticulum stress causes the activation of sterol regulatory element binding protein-2
Colgan, S. M., Tang, D., Werstuck, G. H., & Austin, R. C. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.05.002 · Cited by 193
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Bhalla, K., Hwang, B. J., Dewi, R. E., Ou, L., Twaddel, W., Fang, H., Vafai, S. B., Vazquez, F., Puigserver, P., Boros, L. G., et al. (2011) · Cancer Research · doi:10.1158/0008-5472.can-11-1011 · Cited by 195
Schreuder, T. C. M. A., Verwer, B. J., van Nieuwkerk, C. M., & Mulder, C. J. J. (2008) · World Journal of Gastroenterology · doi:10.3748/wjg.14.2474 · Cited by 197
Thyroid hormone signaling and the liver
Ritter, M. J., Amano, I., Hollenberg, A. N., et al. (2020) · Hepatology · doi:10.1002/hep.31296 · Cited by 188
Regulation of lipid metabolism by the unfolded protein response
Moncan, M., Mnich, K., Blomme, A., Almanza, A., Samali, A., & Gorman, A. M. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16255 · Cited by 191
Cholesterol in health and disease
Tabas, I. A. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0216381 · Cited by 190
Li, J. Z., Ye, J., Xue, B., Qi, J., Zhang, J., Zhou, Z., Li, Q., Wen, Z., & Li, P. (2007) · Diabetes · doi:10.2337/db07-0040 · Cited by 189
Toward a unifying hypothesis of metabolic syndrome
Bremer, A. A., Mietus-Snyder, M., & Lustig, R. H. (2012) · PEDIATRICS · doi:10.1542/peds.2011-2912 · Cited by 186
A role for PPARα in the control of SREBP activity and lipid synthesis in the liver
Knight, B. L., Hebbachi, A., Hauton, D., Brown, A.-M., Wiggins, D. K., Patel, D. D., & Gibbons, G. F. (2005) · Biochemical Journal · doi:10.1042/bj20041896 · Cited by 193
Lipidomics: a new window to biomedical frontiers
Orešič, M., Hänninen, V. A., & Vidal‐Puig, A. (2008) · Trends in biotechnology · doi:10.1016/j.tibtech.2008.09.001 · Cited by 189
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Ali, A., Levantini, E., Teo, J. T., Goggi, J., Clohessy, J. G., Wu, C., Chen, L., Yang, H. H., Krishnan, I., Kocher, O. N., et al. (2018) · EMBO Molecular Medicine · doi:10.15252/emmm.201708313 · Cited by 187
Fragki, S., Dirven, H. A. A. M., Fletcher, T., Grasl‐Kraupp, B., Gützkow, K. B., Hoogenboom, L. A. P., Kersten, S., Lindeman, B., Louisse, J., Peijnenburg, A., et al. (2021) · Critical Reviews in Toxicology · doi:10.1080/10408444.2021.1888073 · Cited by 196
Alves, F. M., Lane, D. J. R., Nguyen, T. P. M., Bush, A. I., & Ayton, S. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02088-5 · Cited by 212
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Suzuki, R., Lee, K., Jing, E., Biddinger, S. B., McDonald, J. G., Montine, T. J., Craft, S., & Kahn, C. R. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.006 · Cited by 169
Li, Q., Pène, V., Krishnamurthy, S. R., Cha, H., & Liang, T. J. (2013) · Nature Medicine · doi:10.1038/nm.3190 · Cited by 193
Lipotoxicity, an imbalance between lipogenesis de novo and fatty acid oxidation
Lelliott, C. J., & Vidal‐Puig, A. (2004) · International Journal of Obesity · doi:10.1038/sj.ijo.0802854 · Cited by 187
Iron Chaperone Poly rC Binding Protein 1 Protects Mouse Liver From Lipid Peroxidation and Steatosis
Protchenko, O. V., Baratz, E., Jadhav, S., Li, F., Shakoury‐Elizeh, M., Gavrilova, O., Ghosh, M. C., Cox, J. E., Maschek, J. A., Tyurin, V. A., et al. (2020) · Hepatology · doi:10.1002/hep.31328 · Cited by 182
Severe Hypercholesterolemia in Four British Families With the D374Y Mutation in the PCSK9 Gene
Naoumova, R. P., Tosi, I., Patel, D., Neuwirth, C. K. Y., Horswell, S. D., Marais, A. D., van Heyningen, C., & Soutar, A. K. (2005) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000190668.94752.ab · Cited by 185
Farrell, G. C., Haczeyni, F., & Chitturi, S. (2018) · Advances in Experimental Medicine and Biology · doi:10.1007/978-981-10-8684-7_3 · Cited by 178
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Moslehi, A., & Hamidizad, Z. (2018) · Journal of Clinical and Translational Hepatology · doi:10.14218/jcth.2017.00061 · Cited by 185
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Aguilar, P. S., & de Mendoza, D. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05484.x · Cited by 180
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Larter, C. Z., Chitturi, S., Heydet, D., & Farrell, G. C. (2010) · Journal of Gastroenterology and Hepatology · doi:10.1111/j.1440-1746.2010.06253.x · Cited by 187
Masterton, G., Plevris, J. N., & Hayes, P. C. (2009) · Alimentary Pharmacology & Therapeutics · doi:10.1111/j.1365-2036.2010.04230.x · Cited by 210
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Sun, Y., Yao, J., Kim, T.-W., & Tall, A. R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300760200 · Cited by 179
Matsumoto, M., Ogawa, W., Akimoto, K., Inoue, H., Miyake, K., Furukawa, K., Hayashi, Y., Iguchi, H., Matsuki, Y., Hiramatsu, R., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci18816 · Cited by 176
Horiguchi, N., Wang, L., Mukhopadhyay, P., Park, O., Jeong, W. I., Lafdil, F., Osei‐Hyiaman, D., Moh, A., Fu, X. Y., Pacher, P., et al. (2008) · Gastroenterology · doi:10.1053/j.gastro.2008.01.016 · Cited by 180
Mukherji, A., Kobiita, A., Damara, M., Misra, N., Méziane, H., Champy, M., & Chambon, P. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1519807112 · Cited by 185
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Bedi, O., Dhawan, V., Sharma, P. L., & Kumar, P. (2016) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-016-1252-4 · Cited by 186
Liu, Y., Wu, F.-Y., Tian, R.-Y., Shi, Y., Xu, Z.-Q., Liu, J.-Y., Huang, J., Xue, F.-F., Liu, B.-Y., & Liu, G. (2023) · Communications Biology · doi:10.1038/s42003-022-04154-6 · Cited by 178
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Howell, J. J., Ricoult, S. J. H., Ben‐Sahra, I., & Manning, B. D. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130041 · Cited by 185
Vagner, M., & Santigosa, E. (2010) · Aquaculture · doi:10.1016/j.aquaculture.2010.11.031 · Cited by 175
Yamashita, T., Honda, M., Takatori, H., Nishino, R., Minato, H., Takamura, H., Ohta, T., & Kaneko, S. (2008) · Journal of Hepatology · doi:10.1016/j.jhep.2008.07.036 · Cited by 178
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Lee, Y., Park, J. E., Lee, M., & Hardwick, J. P. (2018) · Liver Research · doi:10.1016/j.livres.2018.12.001 · Cited by 185
Kirchgessner, T. G., Sleph, P., Ostrowski, J., Lupisella, J., Ryan, C. S., Liu, X., Fernando, G., Grimm, D., Shipkova, P., Zhang, R., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.07.016 · Cited by 172
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Espenshade, P. J. (2006) · Journal of Cell Science · doi:10.1242/jcs.02866 · Cited by 174
Regulatory network of lipid-sensing nuclear receptors: roles for CAR, PXR, LXR, and FXR
Handschin, C., & Meyer, U. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.08.030 · Cited by 173
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Seo, Y., Jeon, T.-I., Chong, H. K., Biesinger, J., Xie, X. S., & Osborne, T. F. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.005 · Cited by 177
Thyfault, J. P., Rector, R. S., Uptergrove, G. M., Borengasser, S. J., Morris, E. M., Wei, Y., Laye, M. J., Burant, C., Qi, N., Ridenhour, S. E., et al. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2009.169060 · Cited by 175
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Thapa, B., & Lee, K. (2019) · BMB Reports · doi:10.5483/bmbrep.2019.52.6.140 · Cited by 176
Todd, B. L., Stewart, E. V., Burg, J. S., Hughes, A. L., & Espenshade, P. J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.7.2817-2831.2006 · Cited by 172
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Weber, L. W. D. (2004) · World Journal of Gastroenterology · doi:10.3748/wjg.v10.i21.3081 · Cited by 172
Erhuma, A. M., Salter, A. M., Sculley, D., Langley‐Evans, S. C., & Bennett, A. J. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00605.2006 · Cited by 171
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Han, J., & Wang, Y. (2017) · Protein & Cell · doi:10.1007/s13238-017-0409-3 · Cited by 172
Guo, W., Deng, J., Pan, Y., Xu, J., Hong, J., Shi, F., Liu, G.-L., Qian, M., Bai, W., Zhang, W., et al. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.10.253 · Cited by 170
Metadata
- Authors
- Horton, J. D., Goldstein, J. L., & Brown, M. S.
- Affiliations
- The University of Texas Southwestern Medical Center (US)
- Corresponding author
- Horton, Jay D.
- Venue
- Journal of Clinical Investigation
- Published
- 2002-05-01
- Volume
- 109
- Issue
- 9
- Pages
- 1125-1131
- ISSN
- 0021-9738 (ISSN-L)
- OpenAlex
- W4252021281
- Cited by
- 4,092
- References
- 47
- Citations by year
- 2026: 149 · 2025: 178 · 2024: 191 · 2023: 215 · 2022: 211 · 2021: 210 · 2020: 263 · 2019: 217 · 2018: 212 · 2017: 206 · 2016: 199 · 2015: 180 · 2014: 184 · 2013: 180 · 2012: 142
- FWCI
- 104.78
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- Funders
- W. M. Keck Foundation
- American Heart Association
- National Institutes of Health (HL20948)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
- Keywords
- SREBP, cholesterol biosynthesis, fatty acid synthesis, lipid homeostasis, liver, transcription factors, NADPH, triglyceride synthesis, phospholipid synthesis, bile micelles, knockout mice
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