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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]
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“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]
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
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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]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“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]
The cited source says what the claim attributes to it.
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]
The cited source says what the claim attributes to it.
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]
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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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The role of scavenger receptor class B type I (SR-BI) in lipid trafficking
Rhainds, D., & Brissette, L. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(03)00173-0 · Cited by 169
Disruption of cholesterol homeostasis by plant sterols
Yang, C., Yu, L., Li, W., Xu, F., Cohen, J. C., & Hobbs, H. H. (2004) · Journal of Clinical Investigation · doi:10.1172/jci22186 · Cited by 171
The Proprotein Convertases, 20 Years Later
Seidah, N. G. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-204-5_3 · Cited by 168
Ecker, J., & Liebisch, G. (2014) · Progress in Lipid Research · doi:10.1016/j.plipres.2014.01.002 · Cited by 167
Cholesterol in health and disease
Tabas, I. A. (2002) · Journal of Clinical Investigation · doi:10.1172/jci16381 · Cited by 167
Valenzuela, R., & Videla, L. A. (2011) · Food & Function · doi:10.1039/c1fo10133a · Cited by 168
LXRβ Is Required for Adipocyte Growth, Glucose Homeostasis, and β Cell Function
Gerin, I., Dolinsky, V. W., Shackman, J. G., Kennedy, R. T., Chiang, S.-H., Burant, C., Steffensen, K. R., Gustafsson, J.-Α., & MacDougald, O. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412564200 · Cited by 167
SREBP-1c and lipogenesis in the liver: an update
Ferré, P., Phan, F., & Foufelle, F. (2021) · Biochemical Journal · doi:10.1042/bcj20210071 · Cited by 183
Control of cholesterol synthesis through regulated ER-associated degradation of HMG CoA reductase
Jo, Y., & DeBose‐Boyd, R. A. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2010.485605 · Cited by 170
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Xu, K. L., Liu, P., & Wei, W. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.10.007 · Cited by 167
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Ma, X., Bi, E., Huang, C., Lu, Y., Xue, G., Guo, X., Wang, A., Yang, M., Qian, J., Dong, C., et al. (2018) · The Journal of Experimental Medicine · doi:10.1084/jem.20171576 · Cited by 167
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Xue, L., Qi, H., Zhang, H., Ding, L., Huang, Q., Zhao, D., Wu, B. J., & Li, X. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.01510 · Cited by 172
Sampath, H., Flowers, M. T., Liu, X., Paton, C. M., Sullivan, R., Chu, K., Zhao, M., & Ntambi, J. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.014225 · Cited by 165
Knebel, B., Haas, J., Hartwig, S., Jacob, S., Köllmer, C., Nitzgen, U., Muller–Wieland, D., & Kotzka, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031812 · Cited by 162
Botolin, D., Wang, Y., Christian, B., & Jump, D. B. (2006) · Journal of Lipid Research · doi:10.1194/jlr.m500365-jlr200 · Cited by 162
Ruiz, R., Jideonwo, V. N., Ahn, M., Surendran, S., Tagliabracci, V. S., Hou, Y., Gamble, A., Kerner, J., Irimia, J. M., Puchowicz, M. A., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.541110 · Cited by 167
Scorletti, E., & Byrne, C. D. (2018) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2018.03.001 · Cited by 168
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Browning, J. D. (2006) · Hepatology · doi:10.1002/hep.21248 · Cited by 164
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Fukuchi, J., Kokontis, J. M., Hiipakka, R. A., Chuu, C., & Liao, S. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-2332 · Cited by 170
Jackel‐Cram, C., Babiuk, L. A., & Liu, Q. (2006) · Journal of Hepatology · doi:10.1016/j.jhep.2006.10.019 · Cited by 160
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Guerra, B., Recio, C., Aranda-Tavío, H., Guerra-Rodríguez, M., García-Castellano, J. M., & Fernández‐Pérez, L. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.626971 · Cited by 177
Wang, H. H., Liu, M., Clegg, D. J., Portincasa, P., & Wang, D. Q. ‐. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2009.06.006 · Cited by 160
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Wang, G., Kim, W. K., Cline, M. A., & Gilbert, E. R. (2017) · Poultry Science · doi:10.3382/ps/pex184 · Cited by 166
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Soy protein reduces hepatic lipotoxicity in hyperinsulinemic obese Zucker fa/fa rats
Tovar, A. R., Torre-Villalvazo, I., Ochoa, M., Elías, A. L., Ortíz-Ortega, V. M., Aguilar-Salinas, C. A., & Torres, N. (2005) · Journal of Lipid Research · doi:10.1194/jlr.m500067-jlr200 · Cited by 160
Li, T., Ferrell, J. M., Boehme, S., & Chiang, J. Y. L. (2013) · Hepatology · doi:10.1002/hep.26427 · Cited by 163
Hwang, Y. P., Choi, J. H., Han, E. H., Kim, H. G., Wee, J., Jung, K. O., Jung, K. H., Kwon, K., Jeong, T. C., Chung, Y., et al. (2011) · Nutrition Research · doi:10.1016/j.nutres.2011.09.026 · Cited by 160
Sevastianova, K., Kotronen, A., Gastaldelli, A., Perttilä, J., Hakkarainen, A., Lundbom, J., Suojanen, L.-U., Orho‐Melander, M., Lundbom, N. M. I., Ferrannini, E., et al. (2011) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.111.012369 · Cited by 158
n-3 Polyunsaturated fatty acids for the management of alcoholic liver disease: A critical review
Wang, M., Ma, L., Yang, Y., Xiao, Z., & Wan, J. (2018) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2018.1544542 · Cited by 163
Chan, D. C., Watts, G. F., Gan, S. K., Ooi, E. M. M., & Barrett, P. H. R. (2010) · Diabetes Care · doi:10.2337/dc09-1765 · Cited by 159
Li, J., Bosch‐Marcé, M., Nanayakkara, A., Savransky, V., Fried, S. K., Semenza, G. L., & Polotsky, V. Y. (2006) · Physiological Genomics · doi:10.1152/physiolgenomics.00293.2005 · Cited by 168
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Stevenson, J., Huang, E. Y., & Olzmann, J. A. (2016) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071715-051030 · Cited by 158
Oakes, S. R., Hilton, H. N., & Ormandy, C. J. (2006) · Breast Cancer Research · doi:10.1186/bcr1411 · Cited by 159
High-flux mitochondrial cholesterol trafficking, a specialized function of the adrenal cortex
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Guan, H., Arany, E. J., van Beek, J. P., Chamson-Reig, A., Thyssen, S. M., Hill, D. J., & Yang, K. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00461.2004 · Cited by 154
Kusnadi, A., Park, S. H., Yuan, R., Pannellini, T., Giannopoulou, E., Oliver, D., Lu, T., Park-Min, K.-H., & Ivashkiv, L. B. (2019) · Immunity · doi:10.1016/j.immuni.2019.06.005 · Cited by 157
Plebanek, M. P., Xue, Y., Nguyen, Y.-V., DeVito, N. C., Wang, X., Holtzhausen, A., Beasley, G. M., Theivanthiran, B., & Hanks, B. A. (2024) · Science Immunology · doi:10.1126/sciimmunol.adi4191 · Cited by 164
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Quan, H. Y., Kim, D. Y., Kim, S. J., Jo, H. K., Kim, G. W., & Chung, S. H. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.02.007 · Cited by 156
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Meissner, E. G., Lee, Y., Osinusi, A. O., Sims, Z., Qin, J., Sturdevant, D. E., McHutchison, J. G., Subramanian, M. G., Sampson, M. L., Naggie, S., et al. (2014) · Hepatology · doi:10.1002/hep.27424 · Cited by 153
Simonen, P. P., Kotronen, A., Hallikainen, M., Sevastianova, K., Makkonen, J., Hakkarainen, A., Lundbom, N. M. I., Miettinen, T. A., Gylling, H. K., & Yki‐Järvinen, H. (2010) · Journal of Hepatology · doi:10.1016/j.jhep.2010.05.037 · Cited by 157
Savransky, V., Jun, J. C., Li, J., Nanayakkara, A., Bevans‐Fonti, S., Moser, A. B., Steele, K., Schweitzer, M., Patil, S. P., Bhanot, S., et al. (2008) · Circulation Research · doi:10.1161/circresaha.108.178533 · Cited by 159
Lam, P., Cheung, F., Tan, H., Wang, N., Yuen, M., & Feng, Y. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17040465 · Cited by 156
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Fernø, J., Raeder, M. B., Vik‐Mo, A. O., Skrede, S., Glambek, M., Tronstad, K. J., Breilid, H., Løvlie, R., Berge, R. K., Stansberg, C. T., et al. (2005) · The Pharmacogenomics Journal · doi:10.1038/sj.tpj.6500323 · Cited by 152
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Role of Nrf2 in preventing ethanol-induced oxidative stress and lipid accumulation
Wu, K. C., Liu, J., & Klaassen, C. D. (2012) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2012.05.010 · Cited by 150
Sun, X.-M., Eden, E. R., Tosi, I., Neuwirth, C. K. Y., Wile, D. B., Naoumova, R. P., & Soutar, A. K. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi128 · Cited by 155
Taniguchi, C. M., Finger, E. C., Krieg, A. J., Wu, C., Diep, A. N., LaGory, E. L., Wei, K., McGinnis, L. M., Yuan, J., Kuo, C. J., et al. (2013) · Nature Medicine · doi:10.1038/nm.3294 · Cited by 150
Docosahexaenoic acid (DHA) and hepatic gene transcription
Jump, D. Β., Botolin, D., Wang, Y., Xu, J., Demeure, O., & Christian, B. (2008) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2008.02.007 · Cited by 152
Prolactin Regulation of Mammary Gland Development
Oakes, S. R., Rogers, R. L., Naylor, M. J., & Ormandy, C. J. (2008) · Journal of Mammary Gland Biology and Neoplasia · doi:10.1007/s10911-008-9069-5 · Cited by 155
Liong, M., Dunshea, F. R., & Shah, N. P. (2007) · British Journal Of Nutrition · doi:10.1017/s0007114507747803 · Cited by 149
Desai, R., Frazier, A. E., Durigon, R., Patel, H., Jones, A. W. E., Rosa, I. D., Lake, N. J., Compton, A. G., Mountford, H. S., Tucker, E. J., et al. (2017) · Brain · doi:10.1093/brain/awx094 · Cited by 150
Single-cell dissection of the human motor and prefrontal cortices in ALS and FTLD
Pineda, S. S., Lee, H., Fitzwalter, B. E., Mohammadi, S., Pregent, L., Gardashli, M., Mantero, J. C., Engelberg-Cook, E., DeJesus‐Hernandez, M., van Blitterswijk, M., et al. (2024) · Cell · doi:10.1016/j.cell.2024.02.031 · Cited by 158
Flowers, J. B., Rabaglia, M. E., Schueler, K. L., Flowers, M. T., Hong, L., Keller, M. P., Ntambi, J. M., & Attie, A. (2007) · Diabetes · doi:10.2337/db06-1142 · Cited by 148
Shi, M. Y., Loftus, H., McAinch, A. J., & Su, X. Q. (2017) · Journal of Functional Foods · doi:10.1016/j.jff.2016.12.036 · Cited by 153
ATF6α downregulation of PPARα promotes lipotoxicity-induced tubulointerstitial fibrosis
Jao, T., Nangaku, M., Wu, C.-H., Sugahara, M., Saito, H., Maekawa, H., Ishimoto, Y., Aoe, M., Inoue, T., Tanaka, T., et al. (2019) · Kidney International · doi:10.1016/j.kint.2018.09.023 · Cited by 148
Lund, E. G., Peterson, L. B., Adams, A. D., Lam, M.-H. N., Burton, C. A., Chin, J., Guo, Q., Huang, S., Latham, M., Lopez, J. C., et al. (2005) · Biochemical Pharmacology · doi:10.1016/j.bcp.2005.11.004 · Cited by 148
Additive regulation of hepatic gene expression by dwarfism and caloric restriction
Tsuchiya, T., Dhahbi, J. M., Cui, X., Mote, P. L., Bartke, A., & Spindler, S. R. (2004) · Physiological Genomics · doi:10.1152/physiolgenomics.00039.2004 · Cited by 149
Deng, X., Zhang, W., O‐Sullivan, I., Williams, J. B., Dong, Q., Park, E. A., Raghow, R., Unterman, T. G., & Elam, M. B. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.347211 · Cited by 150
Pharmacologic ER stress induces non-alcoholic steatohepatitis in an animal model
Lee, J.-S., Zheng, Z., Méndez, R., Ha, S.-W., Xie, Y., & Zhang, K. (2012) · Toxicology Letters · doi:10.1016/j.toxlet.2012.02.017 · Cited by 147
Bile acids and sphingosine-1-phosphate receptor 2 in hepatic lipid metabolism
Kwong, E. K., Li, Y., Hylemon, P. B., & Zhou, H. (2015) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2014.12.009 · Cited by 152
Thyrotropin increases hepatic triglyceride content through upregulation of SREBP-1c activity
Yan, F., Wang, Q., Lu, M. H., Chen, W., Song, Y., Jing, F., Guan, Y., Wang, L., Lin, Y., Bo, T., et al. (2014) · Journal of Hepatology · doi:10.1016/j.jhep.2014.06.037 · Cited by 147
The Role of Liver X Receptor-α in the Fatty Acid Regulation of Hepatic Gene Expression
Pawar, A., Botolin, D., Mangelsdorf, D. J., & Jump, D. Β. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307973200 · Cited by 149
Goedeke, L., Salerno, A., Ramírez, C. M., Guo, L., Allen, R. M., Yin, X., Langley, S. R., Esau, C., Wanschel, A., Fisher, E. A., et al. (2014) · EMBO Molecular Medicine · doi:10.15252/emmm.201404046 · Cited by 145
Lipid Metabolism in Metabolic-Associated Steatotic Liver Disease (MASLD)
Syed‐Abdul, M. M. (2023) · Metabolites · doi:10.3390/metabo14010012 · Cited by 166
Hypothalamic fatty acid metabolism: A housekeeping pathway that regulates food intake
López, M., Lelliott, C. J., & Vidal‐Puig, A. (2007) · BioEssays · doi:10.1002/bies.20539 · Cited by 150
Park, C., Jun, H.-J., Wakita, T., Cheong, J. H., & Hwang, S. B. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808773200 · Cited by 144
A Phosphorylation Cascade Controls the Degradation of Active SREBP1
Bengoechea-Alonso, M. T., & Ericsson, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m807906200 · Cited by 149
Fuller, S. E., & Stephens, J. M. (2015) · Advances in Nutrition · doi:10.3945/an.114.007807 · Cited by 147
Fougerat, A., Montagner, A., Loiseau, N., Guillou, H., & Wahli, W. (2020) · Cells · doi:10.3390/cells9071638 · Cited by 150
Yamamoto, T., Shimano, H., Nakagawa, Y., Ide, T., Yahagi, N., Matsuzaka, T., Nakakuki, M., Takahashi, A., Suzuki, H., Sone, H., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310333200 · Cited by 143
Combined Expression Trait Correlations and Expression Quantitative Trait Locus Mapping
Hong, L., Chen, M., Flowers, J. B., Yandell, B. S., Stapleton, D. S., Mata, C., Mui, E. T.-K., Flowers, M. T., Schueler, K. L., Manly, K. F., et al. (2006) · PLoS Genetics · doi:10.1371/journal.pgen.0020006 · Cited by 143
The unfolded protein response and hepatic lipid metabolism in non alcoholic fatty liver disease
Song, M. J., & Malhi, H. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.107401 · Cited by 146
Regulation of Cholesterologenesis by the Oxysterol Receptor, LXRα
Wang, Y., Rogers, P. M., Chen, S., Varga, G., Stayrook, K. R., & Burris, T. P. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804808200 · Cited by 162
Special relationship between sterols and oxygen: Were sterols an adaptation to aerobic life?
Galea, A. M., & Brown, A. J. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.06.027 · Cited by 142
Torre-Villalvazo, I., Tovar, A. R., Ramos-Barragán, V. E., Cerbón-Cervantes, M. A., & Torres, N. (2008) · Journal of Nutrition · doi:10.1093/jn/138.3.462 · Cited by 141
Solsona‐Vilarrasa, E., Fucho, R., Torres, S., Núñez, S., Nuño‐Lámbarri, N., Enrich, C., García‐Ruiz, C., & Fernández-Checa, J. C. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101214 · Cited by 149
High-flux mitochondrial cholesterol trafficking, a specialized function of the adrenal cortex
Jefcoate, C. R. E. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0216771 · Cited by 141
A Regulatory Role for MicroRNA 33* in Controlling Lipid Metabolism Gene Expression
Goedeke, L., Vales-Lara, F. M., Fenstermaker, M., Cirera-Salinas, D., Chamorro-Jorganes, A., Ramírez, C. M., Mattison, J. A., de Cabo, R., Suárez, Y., & Fernández-Hernando, C. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01714-12 · Cited by 140
Herbal medicines for the prevention of alcoholic liver disease: A review
Ding, R., Tian, K., huang, L.-L., He, C., Jiang, Y., Wang, Y., & Wan, J. (2012) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2012.09.044 · Cited by 140
Xiong, X., Wang, X., Lu, Y., Wang, E., Zhang, Z., Yang, J., Zhang, H., & Li, X. (2013) · Journal of Hepatology · doi:10.1016/j.jhep.2013.12.003 · Cited by 142
Kotani, K., Peroni, O. D., Minokoshi, Y., Boss, O., & Kahn, B. B. (2004) · Journal of Clinical Investigation · doi:10.1172/jci21341 · Cited by 143
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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