The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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
“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
Experimental — accuracy not yet measured
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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]
The cited source says what the claim attributes to it.
In the citing paper
“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]
The cited source says what the claim attributes to it.
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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
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
Cited by
Sorted by citations
Items 801–900 of 1,040
Seo, M. S., Kim, J. H., Kim, H. J., Chang, K. C., & Park, S. W. (2015) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2015.02.020 · Cited by 93
Luteolin Alleviates Alcoholic Liver Disease Induced by Chronic and Binge Ethanol Feeding in Mice
Liu, G., Zhang, Y., Liu, C., Xu, D., Zhang, R., Cheng, Y., Pan, Y., Huang, C., & Chen, Y. (2014) · Journal of Nutrition · doi:10.3945/jn.114.193128 · Cited by 93
Thioacetamide induced liver damage in zebrafish embryo as a disease model for steatohepatitis
Amali, A. A., Rekha, R. D., Lin, C. J., Wang, W.-L., Gong, H., Her, G. M., & Wu, J. (2006) · Journal of Biomedical Science · doi:10.1007/s11373-005-9055-5 · Cited by 93
Regulation of Lipid Homeostasis by the Bifunctional SREBF2-miR33a Locus
Bommer, G. T., & MacDougald, O. A. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.02.004 · Cited by 94
The Roles of Vitamin A in the Regulation of Carbohydrate, Lipid, and Protein Metabolism
Chen, W., & Chen, G. (2014) · Journal of Clinical Medicine · doi:10.3390/jcm3020453 · Cited by 96
Mediterranean diet and nonalcoholic fatty liver disease: molecular mechanisms of protection
Godos, J., Federico, A., Dallio, M., & Scazzina, F. (2016) · International Journal of Food Sciences and Nutrition · doi:10.1080/09637486.2016.1214239 · Cited by 94
Naturally Occurring PCSK9 Inhibitors
Adorni, M. P., Zimetti, F., Lupo, M. G., Ruscica, M., & Ferri, N. (2020) · Nutrients · doi:10.3390/nu12051440 · Cited by 92
Du, X., Malta, C. D., Fang, Z., Shen, T., Niu, X., Chen, M., Jin, B., Yu, H., Lei, L., Gao, W., et al. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.12.012 · Cited by 95
Erlins restrict SREBP activation in the ER and regulate cellular cholesterol homeostasis
Huber, M. D., Vesely, P. W., Datta, K., & Gerace, L. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201305076 · Cited by 91
The Transcription Factor SREBP-1c Is Instrumental in the Development of औ-Cell Dysfunction
Wang, H., Maechler, P., Antinozzi, P. A., Herrero, L., Hagenfeldt-Johansson, K. A., Björklund, A., & Wollheim, C. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212488200 · Cited by 92
SREBP-1 as a Transcriptional Integrator of Circadian and Nutritional Cues in the Liver
Brewer, M., Lange, D., Baler, R., & Anzulovich, A. C. (2005) · Journal of Biological Rhythms · doi:10.1177/0748730405275952 · Cited by 90
Wendel, A. A., Cooper, D. E., Ilkayeva, O., Muoio, D. M., & Coleman, R. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.485219 · Cited by 91
Zaytsoff, S. J. M., Brown, C. L. J., Montina, T., Metz, G. A. S., Abbott, D. W., Uwiera, R. R. E., & Inglis, G. D. (2019) · Scientific Reports · doi:10.1038/s41598-019-52267-6 · Cited by 91
Jeong, D., Park, J., Kim, K.-S., Kim, J., Huh, J., Seo, J., Kim, Y., Cho, J., Lee, K., Fukuda, J., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42170-0 · Cited by 91
PAQR3 modulates cholesterol homeostasis by anchoring Scap/SREBP complex to the Golgi apparatus
Xu, D., Wang, Z., Zhang, Y., Jiang, W., Pan, Y., Song, B.-L., & Chen, Y. (2015) · Nature Communications · doi:10.1038/ncomms9100 · Cited by 89
Ubiquitin-proteasome-dependent degradation of mammalian ER stearoyl-CoA desaturase
Kato, H., Sakaki, K., & Mihara, K. (2006) · Journal of Cell Science · doi:10.1242/jcs.02951 · Cited by 93
Lu, C., Zhang, F., Xu, W., Wu, X., Lian, N., Jin, H., Chen, Q., Chen, L., Shao, J., Wu, L., et al. (2015) · IUBMB Life · doi:10.1002/iub.1409 · Cited by 91
Kortner, T. M., Björkhem, I., Krasnov, A., Timmerhaus, G., & Krogdahl, Å. (2014) · British Journal Of Nutrition · doi:10.1017/s0007114514000373 · Cited by 95
Intracoronary Imaging, Cholesterol Efflux, and Transcriptomes After Intensive Statin Treatment
Kini, A. S., Vengrenyuk, Y., Shameer, K., Maehara, A., Meerarani, P., Yoshimura, T., Matsumura, M., Aquino, M. B., Haider, N., Johnson, K. W., et al. (2016) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2016.10.029 · Cited by 92
An Atomic-Level Perspective of HMG-CoA-Reductase: The Target Enzyme to Treat Hypercholesterolemia
Gesto, D., Pereira, C. M. S. B., Cerqueira, N. M. F. S. A., & Sousa, S. F. (2020) · Molecules · doi:10.3390/molecules25173891 · Cited by 100
Fukunishi, S., Sujishi, T., Takeshita, A., Ohama, H., Tsuchimoto, Y., Asai, A., Tsuda, Y., & Higuchi, K. (2013) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.13-49 · Cited by 90
Hepatic farnesyl diphosphate synthase expression is suppressed by polyunsaturated fatty acids
Jossic-Corcos, C. L., Gonthier‐Guéret, C., Zaghini, I., Logette, E., Shechter, I., & Bournot, P. (2005) · Biochemical Journal · doi:10.1042/bj20040933 · Cited by 90
Steneberg, P., Sykaras, A. G., Backlund, F., Straseviçiene, J., Söderström, I., & Edlund, H. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.640292 · Cited by 88
Zhao, Y., Li, H., Zhang, Y., Li, L., Fang, R., Li, Y., Liu, Q., Zhang, W., Qiu, L., Liu, F., et al. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-1734 · Cited by 89
PRMT5 in gene regulation and hematologic malignancies
Zhu, F., & Rui, L. (2019) · Genes & Diseases · doi:10.1016/j.gendis.2019.06.002 · Cited by 93
Kaymak, I., Maier, C. R., Schmitz, W., Campbell, A. D., Dankworth, B., Ade, C. P., Walz, S., Paauwe, M., Kalogirou, C., Marouf, H., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-0650 · Cited by 90
Fernø, J., Skrede, S., Vik‐Mo, A. O., Håvik, B., & Steen, V. M. (2006) · BMC Neuroscience · doi:10.1186/1471-2202-7-69 · Cited by 91
Wang, X. X., Jiang, T., Shen, Y., Santamaria, H., Solis, N., ARBEENY, C. M., & Levi, M. (2011) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00338.2010 · Cited by 90
Pandey, P. R., Xing, F., Sharma, S., Watabe, M., Pai, S., Iiizumi, M., Fukuda, K., Hirota, S., Mo, Y.-Y., & Watabe, K. (2012) · Oncogene · doi:10.1038/onc.2012.519 · Cited by 89
Rowe, A. H., Argmann, C., Edwards, J. Y., Sawyez, C. G., Morand, O. H., Hegele, R. A., & Huff, M. W. (2003) · Circulation Research · doi:10.1161/01.res.0000097606.43659.f4 · Cited by 89
Transgenic Mice Overexpressing Nuclear SREBP-1c in Pancreatic β-Cells
Takahashi, A., Motomura, K., Kato, T., Yoshikawa, T., Nakagawa, Y., Yahagi, N., Sone, H., Suzuki, H., Toyoshima, H., Yamada, N., et al. (2005) · Diabetes · doi:10.2337/diabetes.54.2.492 · Cited by 90
Quinn, C. M., Jessup, W., Wong, J., Kritharides, L., & Brown, A. J. (2005) · Biochemical Journal · doi:10.1042/bj20041776 · Cited by 93
Rab1 in cell signaling, cancer and other diseases
Yang, X.-Z., Li, X., Zhang, Y.-J., Rodríguez‐Rodríguez, L., Xiang, M.-Q., Wang, H.-Y., & Zheng, X. F. S. (2016) · Oncogene · doi:10.1038/onc.2016.81 · Cited by 91
Selective targeting of mutant adenomatous polyposis coli ( APC ) in colorectal cancer
Zhang, L., Theodoropoulos, P. C., Eskiocak, U., Wang, W., Moon, Y.-A., Posner, B., Williams, N. S., Wright, W. E., Kim, S. B., Nijhawan, D., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf8127 · Cited by 88
Bort, A., Sánchez, B. G., Mateos‐Gómez, P. A., Díaz‐Laviada, I., & Rodríguez‐Henche, N. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20071660 · Cited by 92
Subedi, A., Liu, Q., Ayyathan, D. M., Sharon, D. M., Cathelin, S., Hosseini, M., Xu, C., Voisin, V., Bader, G. D., D’Alessandro, A., et al. (2020) · Cell stem cell · doi:10.1016/j.stem.2021.06.004 · Cited by 86
Hepatic iron loading in mice increases cholesterol biosynthesis†
Graham, R. M., Chua, A. C. G., Carter, K. W., Delima, R. D., Johnstone, D. M., Herbison, C. E., Firth, M. J., O’Leary, R., Milward, E. A., Olynyk, J. K., et al. (2010) · Hepatology · doi:10.1002/hep.23712 · Cited by 92
Steele, M. A., Dionissopoulos, L., AlZahal, O., Doelman, J., & McBride, B. W. (2011) · Journal of Dairy Science · doi:10.3168/jds.2011-4465 · Cited by 90
Tang, C.-C., Huang, H., Lee, Y., Tang, Y.-H., & Wang, C. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.10.011 · Cited by 88
Nasheri, N., Joyce, M., Rouleau, Y., Yang, P., Yao, S. Q., Tyrrell, D. L., & Pezacki, J. P. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.03.014 · Cited by 88
Cholesterol imbalance in adipocytes: a possible mechanism of adipocytes dysfunction in obesity
Yu, B. ‐., Zhao, S., & Hu, J. (2009) · Obesity Reviews · doi:10.1111/j.1467-789x.2009.00699.x · Cited by 87
Peroxisome proliferator-activated receptor δ
Bojic, L. A., & Huff, M. W. (2013) · Current Opinion in Lipidology · doi:10.1097/mol.0b013e32835cc949 · Cited by 89
HYPOCHOLESTEROLEMIA IN CLINICALLY SERIOUS CONDITIONS - REVIEW
Vyroubal, P., Chiarla, C., Giovannini, I., Hyšpler, R., Tichá, A., Hrnčiariková, D., & Zadák, Z. (2008) · Biomedical Papers · doi:10.5507/bp.2008.029 · Cited by 87
Posttranscriptional regulation of de novo lipogenesis by glucose-induced O-GlcNAcylation
Tan, W. H., Jiang, P., Zhang, W., Hu, Z., Lin, S., Chen, L., Li, Y., Peng, C., Li, Z., Sun, A., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.02.009 · Cited by 86
Lipid scavenging macrophages and inflammation
Vogel, A., Brunner, J. S., Hajto, A., Sharif, O., & Schabbauer, G. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2021.159066 · Cited by 92
The Role of SCAP/SREBP as Central Regulators of Lipid Metabolism in Hepatic Steatosis
Chandrasekaran, P., & Weiskirchen, R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25021109 · Cited by 95
Yang, D., Chang, Y., Hsu, C., Liu, C., Lin, Y., Lin, Y., Liu, K., & Chen, Y. (2010) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf903355q · Cited by 87
Olsen, B. N., Schlesinger, P. H., & Baker, N. (2009) · Journal of the American Chemical Society · doi:10.1021/ja8095224 · Cited by 87
Li, G., Mobbs, C. V., & Scarpace, P. J. (2003) · Diabetes · doi:10.2337/diabetes.52.8.1951 · Cited by 88
PPAR? in the pathogenesis of fatty liver disease
Rao, M. S., & Reddy, J. K. (2004) · Hepatology · doi:10.1002/hep.20453 · Cited by 87
Flock, M. R., Green, M. H., & Kris-Etherton, P. M. (2011) · Advances in Nutrition · doi:10.3945/an.111.000422 · Cited by 82
Moya, M., Gómez-Lechón, M. J., Castell, J. V., & Jover, R. (2010) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2010.01.008 · Cited by 86
Endoplasmic reticulum stress related molecular mechanisms in nonalcoholic steatohepatitis
Bozaykut, P., Şahin, A., Karademir-Yilmaz, B., & Özer, N. K. (2016) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.07.001 · Cited by 88
Targeting extracellular nutrient dependencies of cancer cells
García‐Bermúdez, J., Williams, R. T., Guarecuco, R., & Birsoy, K. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.11.011 · Cited by 93
Wan, M., Pan, S., Shan, B., Diao, H., Jin, H., Wang, Z., Wang, W., Han, S., Liu, W., He, J., et al. (2025) · Molecular Cancer · doi:10.1186/s12943-025-02258-1 · Cited by 102
Lee, P., Leong, W., Tan, T., Lim, M., Han, W., & Radda, G. K. (2012) · Hepatology · doi:10.1002/hep.26028 · Cited by 87
The miRNA Interactome in Metabolic Homeostasis
Hartig, S. M., Hamilton, M. P., Bader, D. A., & McGuire, S. E. (2015) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.09.006 · Cited by 87
Lee, S., Lee, M.-S., Kim, C., Kim, I.-H., & Kim, Y. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13055729 · Cited by 85
Ouimet, M. I. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.03.007 · Cited by 86
Wu, K., Luo, Z., Högstrand, C., Chen, G., Wei, C., & Li, D. (2018) · Environmental Science & Technology · doi:10.1021/acs.est.8b02967 · Cited by 83
Tao, W., Sun, W., Liu, L., Wang, G., Xiao, Z., Pei, X., & Wang, M. (2019) · Marine Drugs · doi:10.3390/md17110645 · Cited by 85
Insulin Regulation of Cholesterol 7α-Hydroxylase Expression in Human Hepatocytes
Li, T., Kong, X., Owsley, E., Ellis, E. C. S., Strom, S. C., & Chiang, J. Y. L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605815200 · Cited by 87
Zhou, Z., Wang, F., Ren, X., Wang, Y., & BLANCHARD, C. L. (2015) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2015.01.052 · Cited by 85
Qiao, A., Liang, J., Ke, Y., Li, C., Cui, Y., Shen, L., Zhang, H., Cui, A., Liu, X., Liu, C., et al. (2011) · Hepatology · doi:10.1002/hep.24402 · Cited by 85
Parks, E. J., & Hellerstein, M. K. (2006) · Journal of Lipid Research · doi:10.1194/jlr.r600018-jlr200 · Cited by 85
Genetic, anatomic, and clinical determinants of human serum sterol and vitamin D levels
Stiles, A. R., Kozlitina, J., Thompson, B. M., McDonald, J. G., King, K. S., & Russell, D. W. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1413561111 · Cited by 87
Alvi, S. S., Ansari, I. A., Khan, I., Iqbal, J., & Khan, M. S. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.04.012 · Cited by 89
mTORC1 signaling activates NRF1 to increase cellular proteasome levels
Zhang, Y., & Manning, B. D. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1044188 · Cited by 85
Yang, M., Bose, S., Lim, S.-K., Seo, J., Shin, J., Lee, D., Chung, W., Song, E., Nam, Y., & Kim, H. (2020) · Microorganisms · doi:10.3390/microorganisms8091413 · Cited by 89
Lawrence, G. D. (2021) · Advances in Nutrition · doi:10.1093/advances/nmab013 · Cited by 88
Hu, X., Wang, Y., Wang, J., Xue, Y., Li, Z., Nagao, K., Yanagita, T., & Xue, C. (2010) · Lipids in Health and Disease · doi:10.1186/1476-511x-9-25 · Cited by 85
Wang, Y., Torres‐Gonzalez, M., Tripathy, S., Botolin, D., Christian, B., & Jump, D. Β. (2008) · Journal of Lipid Research · doi:10.1194/jlr.m800123-jlr200 · Cited by 87
Oxysterol Binding Protein Induces Upregulation of SREBP-1c and Enhances Hepatic Lipogenesis
Yan, D., Lehto, M. J., Rasilainen, L., Metso, J., Ehnholm, C., Ylä‐Herttuala, S., Jauhiainen, M., & Olkkonen, V. M. (2007) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.106.138545 · Cited by 84
Dávalos, A., Fernandez-Hernando, C. F., Cerrato, F., Martı́nez-Botas, J., Gómez‐Coronado, D., Gómez‐Cordovés, C., & Lasunción, M. A. (2006) · Journal of Nutrition · doi:10.1093/jn/136.7.1766 · Cited by 85
Differential expression and function of ABCG1 and ABCG4 during development and aging
Bojanic, D. D., Tarr, P. T., Gale, G. D., Smith, D. J., Bok, D., Chen, B., Nusinowitz, S., Lövgren‐Sandblom, A., Björkhem, I., & Edwards, P. A. (2009) · Journal of Lipid Research · doi:10.1194/jlr.m900250-jlr200 · Cited by 84
The beneficial effects of taurine in preventing metabolic syndrome
Chen, W., Guo, J., Zhang, Y., & Zhang, J. (2016) · Food & Function · doi:10.1039/c5fo01295c · Cited by 84
Röhrl, C., & Stangl, H. (2018) · Wiener Medizinische Wochenschrift · doi:10.1007/s10354-018-0626-2 · Cited by 83
Progress and prospects of long noncoding RNAs in lipid homeostasis
Chen, Z. (2015) · Molecular Metabolism · doi:10.1016/j.molmet.2015.12.003 · Cited by 83
Rincón‐Cervera, M. Á., Valenzuela, R., Hernández‐Rodas, M. C., Marambio, M., Espinosa, A., Mayer, S., Romero, N., Barrera, C. R., Valenzuela, A., & Videla, L. A. (2016) · Nutrition · doi:10.1016/j.nut.2016.04.006 · Cited by 87
Sud, N., Zhang, H., Pan, K., Cheng, X., Cui, J., & Su, Q. (2017) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2017.02.003 · Cited by 82
PI3K signaling-regulated metabolic reprogramming: From mechanism to application
Su, W. Y., Tian, L. Y., Guo, L. P., Huang, L., & Gao, W. (2023) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2023.188952 · Cited by 88
Han, S., Komatsu, Y., Murayama, A., Steffensen, K. R., Nakagawa, Y., Nakajima, Y., Suzuki, M., Oie, S., Parini, P., Vedin, L., et al. (2013) · Hepatology · doi:10.1002/hep.26951 · Cited by 88
Ablation of ARNT/HIF1β in Liver Alters Gluconeogenesis, Lipogenic Gene Expression, and Serum Ketones
Wang, X. L., Suzuki, R., Lee, K., Tran, T. T., Gunton, J. E., Saha, A. K., Patti, M., Goldfine, A. B., Ruderman, N. B., Gonzalez, F. J., et al. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.04.001 · Cited by 86
Chen, Q.-L., Luo, Z., Pan, Y., Zheng, J., Zhu, Q., Sun, L., Zhuo, M.-Q., & Hu, W. (2013) · Aquatic Toxicology · doi:10.1016/j.aquatox.2013.04.003 · Cited by 85
Microarray analysis of differential gene expression in the liver of lean and fat chickens
Bourneuf, E., Herault, F., Chicault, C., Carré, W., Assaf, S., Monnier, A., Mottier, S., Lagarrigue, S., Douaire, M., Mosser, J., et al. (2006) · Gene · doi:10.1016/j.gene.2005.12.028 · Cited by 88
Nuclear bile acid receptor FXR as pharmacological target: Are we there yet?
Modica, S., & Moschetta, A. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.07.082 · Cited by 83
Fukuchi, J., Hiipakka, R. A., Kokontis, J. M., Hsu, S., Ko, A. L., Fitzgerald, M. L., & Liao, S. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-2647 · Cited by 83
Moon, Y.-A., Ochoa, C. R., Mitsche, M. A., Hammer, R. E., & Horton, J. D. (2014) · Journal of Lipid Research · doi:10.1194/jlr.m054353 · Cited by 86
Self-citationCancer cells depend on environmental lipids for proliferation when electron acceptors are limited
Li, Z., Ji, B. W., Dixit, P. D., Tchourine, K., Lien, E. C., Hosios, A. M., Abbott, K. L., Rutter, J. C., Westermark, A. M., Gorodetsky, E. F., et al. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00588-8 · Cited by 81
Williams, K. J., & Wu, X. (2016) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2016.02.004 · Cited by 83
Jiang, L.-Y., Jiang, W., Tian, N., Xiong, Y.-N., Liu, J., Wei, J. N., Wu, K., Luo, J., Shi, X.-J., & Song, B. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.001260 · Cited by 81
Lipid Droplets in Brown Adipose Tissue Are Dispensable for Cold-Induced Thermogenesis
Chitraju, C., Fischer, A. W., Farese, R. V., & Walther, T. C. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108348 · Cited by 85
Tsuboyama-Kasaoka, N., Miyazaki, H., Ezaki, O., & Kasaoka, S. (2003) · Journal of Nutrition · doi:10.1093/jn/133.6.1793 · Cited by 82
Systems biology strategies to study lipidomes in health and disease
Hyötyläinen, T., & Orešič, M. (2014) · Progress in Lipid Research · doi:10.1016/j.plipres.2014.06.001 · Cited by 83
Choi, W., Jeon, B.-N., Park, H., Yoo, J., Ys, K., Koh, D.-I., Kim, M. H., Kim, Y.-R., Lee, C.-E., Kim, K., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802477200 · Cited by 80
Yang, J., MacDougall, M. L., McDowell, M. T., Xi, L., Wei, R., Zavadoski, W. J., Molloy, M. P., Baker, J. D., Kühn, M., Cabrera, O., et al. (2011) · BMC Genomics · doi:10.1186/1471-2164-12-281 · Cited by 82
Regulation of hepatic gene expression by saturated fatty acids
Vallim, T., & Salter, A. M. (2010) · Prostaglandins Leukotrienes and Essential Fatty Acids · doi:10.1016/j.plefa.2010.02.016 · Cited by 83
Shimizu, S., Ugi, S., Maegawa, H., Egawa, K., Nishio, Y., Yoshizaki, T., Shi, K., Nagai, Y., Morino, K., Nemoto, K.-I., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306880200 · Cited by 82
(-)-Epicatechin regulates blood lipids and attenuates hepatic steatosis in rats fed high-fat diet
Cheng, H., Xu, N., Zhao, W., Su, J., Liang, M., Xie, Z., Wu, X., & Li, Q. (2017) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201700303 · Cited by 81
MicroRNA Modulation of Cholesterol Homeostasis
Fernández-Hernando, C., & Moore, K. J. (2011) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.111.226688 · Cited by 89
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review