The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
PPARs and the complex journey to obesity
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.
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
Positional cloning of the mouse obese gene and its human homologue
Zhang, Y., Proenca, R., Maffei, M., Barone, M., Leopold, L., & Friedman, J. M. (1994) · Nature · doi:10.1038/372425a0 · Cited by 13,419
Yamauchi, T., Kamon, J., Minokoshi, Y., Ito, Y., Waki, H., Uchida, S., Yamashita, S., Noda, M., Kita, S., Ueki, K., et al. (2002) · Nature Medicine · doi:10.1038/nm788 · Cited by 4,238
Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators
Issemann, I., & Green, S. (1990) · Nature · doi:10.1038/347645a0 · Cited by 3,519
A role for ghrelin in the central regulation of feeding
Nakazato, M., Murakami, N., Date, Y., Kojima, M., Matsuo, H., Kangawa, K., & Matsukura, S. (2001) · Nature · doi:10.1038/35051587 · Cited by 3,443
Cloning of adiponectin receptors that mediate antidiabetic metabolic effects
Yamauchi, T., Kamon, J., Ito, Y., Tsuchida, A., Yokomizo, T., Kita, S., Sugiyama, T., Miyagishi, M., Hara, K., Tsunoda, M., et al. (2003) · Nature · doi:10.1038/nature01705 · Cited by 3,176
Cellular mechanisms of insulin resistance
Shulman, G. I. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10583 · Cited by 2,714
Transcriptional co-activator PGC-1α drives the formation of slow-twitch muscle fibres
Lin, J., Wu, H., Tarr, P. T., Zhang, C.-Y., Wu, Z., Boss, O., Michael, L. F., Puigserver, P., Isotani, E., Olson, E. N., et al. (2002) · Nature · doi:10.1038/nature00904 · Cited by 2,546
The adipocyte-secreted protein Acrp30 enhances hepatic insulin action
Berg, A. H., Combs, T. P., Du, X., Brownlee, M., & Scherer, P. E. (2001) · Nature Medicine · doi:10.1038/90992 · Cited by 2,526
Gut hormone PYY3-36 physiologically inhibits food intake
Batterham, R. L., Cowley, M. A., Small, C. J., Herzog, H., Cohen, M. A., Dakin, C. L., Wren, A. M., Brynes, A. E., Low, M. J., Ghatei, M. A., et al. (2002) · Nature · doi:10.1038/nature00887 · Cited by 2,351
A role for glucagon-like peptide-1 in the central regulation of feeding
Turton, M. D., O'Shea, D., Gunn, I., Beak, S. A., Edwards, C. M. B., Meeran, K., Choi, S. J., Taylor, G. M., Heath, M. M., Lambert, P. D., et al. (1996) · Nature · doi:10.1038/379069a0 · Cited by 1,950
Research works printed but not linked: 80
- Tartaglia, L. et al. Identification and expression cloning of a leptin receptor OB-R. Cell 83, 1263–1271 (1995). · DOI · Paper page
- Seeley, R. & Woods, S. Monitoring of stored and available fuel by the CNS: implications for obesity. Nat. Rev. Neurosci. 4, 901–909 (2003). · DOI
- Drazen, D. & Woods, S. Peripheral signals in the control of satiety and hunger. Curr. Opin. Clin. Nutr. Metab. Care 6, 621–629 (2003). · DOI
- Bachman, E. et al. βAR signaling required for diet-induced thermogenesis and obesity resistance. Science 297, 843–845 (2002). · DOI · Paper page
- Wu, Z. et al. Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1. Cell 98, 115–124 (1999). · DOI · Paper page
- Fleury, C. et al. Uncoupling protein-2: a novel gene linked to obesity and hyperinsulinemia. Nat. Genet. 15, 269–272 (1997). · DOI · Paper page
- Gimeno, R.E. et al. Cloning and characterization of an uncoupling protein homolog: a potential molecular mediator of human thermogenesis. Diabetes 46, 900–906 (1997). · DOI · Paper page
- Boss, O. et al. Uncoupling protein-3: a new member of the mitochondrial carrier family with tissue-specific expression. FEBS Lett. 408, 39–42 (1997). · DOI · Paper page
- Vidal-Puig, A., Solanes, G., Grujic, D., Flier, J.S. & Lowell, B.B. UCP3: an uncoupling protein homologue expressed preferentially and abundantly in skeletal muscle and brown adipose tissue. Biochem. Biophys. Res. Commun. 235, 79–82 (1997). · DOI · Paper page
- Clapham, J.C. et al. Mice overexpressing human uncoupling protein-3 in skeletal muscle are hyperphagic and lean. Nature 406, 415–418 (2000). · DOI · Paper page
- Enerback, S. et al. Mice lacking mitochondrial uncoupling protein are cold-sensitive but not obese. Nature 387, 90–94 (1997). · DOI · Paper page
- Arsenijevic, D. et al. Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production. Nat. Genet. 26, 435–439 (2000). · DOI · Paper page
- Levine, J., Eberhardt, N. & Jensen, M. Role of nonexercise activity thermogenesis in resistance to fat gain in humans. Science 283, 212–214 (1999). · DOI · Paper page
- Ullrich, A. et al. Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes. Nature 313, 756–761 (1985). · DOI · Paper page
- Ebina, Y. et al. The human insulin receptor cDNA: the structural basis for hormone-activated transmembrane signaling. Cell 40, 747–758 (1985). · DOI · Paper page
- Sun, X.J. et al. Role of IRS-2 in insulin and cytokine signaling. Nature 377, 173–177 (1995). · DOI · Paper page
- Accili, D. et al. Early neonatal death in mice homozygous for a null allele of the insulin receptor gene. Nature Genet. 12, 106–109 (1996). · DOI · Paper page
- Michael, M. et al. Loss of insulin signaling in hepatocytes leads to severe insulin resistance and progressive hepatic dysfunction. Mol. Cell 6, 87–97 (2000). · DOI · Paper page
- Kulkarni, R. et al. Tissue-specific knockout of the insulin receptor in pancreatic β cells creates an insulin secretory defect similar to that in type 2 diabetes. Cell 96, 329–339 (1999). · DOI · Paper page
- Bruning, J. et al. A muscle-specific insulin receptor knockout exhibits features of the metabolic syndrome of NIDDM without altering glucose tolerance. Mol. Cell 2, 559–569 (1998). · DOI · Paper page
- Mu, J., Brozinick, J., Valladares, O., Bucan, M. & Birnbaum, M. A role for AMP-activated protein kinase in contraction- and hypoxia-regulated glucose transport in skeletal muscle. Mol. Cell 7, 1085–1094 (2001). · DOI · Paper page
- Bluher, M., Kahn, B. & Kahn, R. Extended longevity in mice lacking the insulin receptor in adipose tissue. Science 299, 572–574 (2003). · DOI · Paper page
- Lauro, D. et al. Impaired glucose tolerance in mice with a targeted impairment of insulin action in muscle and adipose tissue. Nat. Genet. 20, 294–298 (1998). · DOI
- Guerra, C. et al. Brown adipose tissue-specific insulin receptor knockout shows a diabetic phenotype without insulin resistance. J. Clin. Invest. 108, 1205–1213 (2001). · DOI
- Tamemoto, H. et al. Insulin resistance and growth retardation in mice lacking insulin receptor substrate-1. Nature 372, 182–186 (1994). · DOI · Paper page
- Withers, D. et al. Disruption of IRS-2 causes type 2 diabetes in mice. Nature 391, 900–904 (1998). · DOI
- Dresner, A. et al. Effects of free fatty acids on glucose transport and IRS-1-associated phosphatidylinositol 3-kinase activity. J. Clin. Invest. 103, 253–259 (1999). · DOI · Paper page
- Perseghin, G. et al. Intramyocellular triglyceride content is a determinant of in vivo insulin resistance in humans: a 1H–13C nuclear magnetic resonance spectroscopy assessment in offspring of type 2 diabetic parents. Diabetes 48, 1600–1606 (1999). · DOI · Paper page
- Petersen, K.F. et al. Mitochondrial dysfunction in the elderly: possible role in insulin resistance. Science 300, 1140–1142 (2003). · DOI · Paper page
- Kim, J.K. et al. Tissue-specific overexpression of lipoprotein lipase causes tissue-specific insulin resistance. Proc. Natl. Acad. Sci. USA 98, 7522–7527 (2001). · DOI · Paper page
- Dreyer, C. et al. Control of the peroxisomal β-oxidation pathway by a novel family of nuclear hormone receptors. Cell 68, 879–887 (1992). · DOI · Paper page
- Kliewer, S.A. et al. Differential expression and activation of a family of murine peroxisome proliferator-activated receptors. Proc. Natl. Acad. Sci USA 91, 7355–7359 (1994). · DOI · Paper page
- Chawla, A., Repa, J.J., Evans, R.M. & Mangelsdorf, D.J. Nuclear receptors and lipid physiology: opening the X-files. Science 294, 1866–1870 (2001). · DOI · Paper page
- Rosen, E.D., Walkey, C.J., Puigserver, P. & Spiegelman, B.M. Transcriptional regulation of adipogenesis. Genes Dev. 14, 1293–1307 (2000). · DOI · Paper page
- Tontonoz, P., Hu, E. & Spiegelman, B.M. Stimulation of adipogenesis in fibroblasts by PPARγ2, a lipid-activated transcription factor. Cell 79, 1147–1156 (1994). · DOI
- Barak, Y. et al. PPARγ is required for placental, cardiac, and adipose tissue development. Mol. Cell 4, 585–595 (1999). · DOI
- Rosen, E.D. et al. PPARγ is required for the differentiation of adipose tissue in vivo and in vitro. Mol. Cell 4, 611–617 (1999). · DOI · Paper page
- Kubota, N. et al. PPARγ mediates high-fat diet-induced adipocyte hypertrophy and insulin resistance. Mol. Cell 4, 597–609 (1999). · DOI · Paper page
- Agarwal, A.K. & Garg, A. A novel heterozygous mutation in peroxisome proliferator-activated receptor-γ gene in a patient with familial partial lipodystrophy. J. Clin. Endocrinol. Metab. 87, 408–411 (2002).
- Hegele, R.A., Cao, H., Frankowski, C., Mathews, S.T. & Leff, T. PPARG F388L, a transactivation-deficient mutant, in familial partial lipodystrophy. Diabetes 51, 3586–3590 (2002). · DOI · Paper page
- Savage, D.B. et al. Human metabolic syndrome resulting from dominant-negative mutations in the nuclear receptor peroxisome proliferator-activated receptor-γ. Diabetes 52, 910–917 (2003). · DOI · Paper page
- Wu, Z. et al. Cross-regulation of C/EBP and PPARγ controls the transcriptional pathway of adipogenesis and insulin sensitivity. Mol. Cell 3, 151–158 (1999). · DOI · Paper page
- Rosen, E.D. et al. C/EBPalpha induces adipogenesis through PPARγ: a unified pathway. Genes Dev. 16, 22–26 (2002). · DOI · Paper page
- Forman, B.M. et al. Deoxy-delta 12, 14-prostaglandin J2 is a ligand for the adipocyte determination factor PPARγ. Cell 83, 803–812 (1995). · DOI
- Lehmann, J.M. et al. An antidiabetic thiazolidinedione is a high affinity ligand for peroxisome proliferator-activated receptor γ (PPARγ). J. Biol. Chem. 270, 12953–12956 (1995). · DOI
- Yamauchi, T. et al. The mechanisms by which both heterozygous peroxisome proliferator-activated receptor γ (PPARγ) deficiency and PPARγ agonist improve insulin resistance. J. Biol. Chem. 276, 41245–41254 (2001). · DOI · Paper page
- Guan, H.-P. et al. A futile metabolic cycle activated in adipocytes by antidiabetic agents. Nat. Med. 8, 1122–1128 (2002). · DOI · Paper page
- Peraldi, P., Xu, M. & Spiegelman, B.M. Thiazolidinediones block tumor necrosis factor-α-induced inhibition of insulin signaling. J. Clin. Invest. 100, 1863–1869 (1997). · DOI · Paper page
- Steppan, C.M. et al. The hormone resistin links obesity to diabetes. Nature 409, 307–312 (2001). · DOI · Paper page
- Rajala, M.W., Obici, S., Scherer, P.E. & Rossetti, L. Adipose-derived resistin and gut-derived resistin-like molecule-β selectively impair insulin action on glucose production. J. Clin. Invest. 111, 225–300 (2003). · DOI · Paper page
- Combs, T.P., Berg, A.H., Obici, S., Scherer, P.E. & Rossetti, L. Endogenous glucose production is inhibited by the adipose-derived protein Acrp30. J. Clin. Invest. 108, 1875–1881 (2001). · DOI · Paper page
- Yamauchi, T. et al. The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity. Nat. Med. 7, 941–946 (2001). · DOI · Paper page
- Ribon, V., Johnson, J.H., Camp, H.S. & Saltiel, A.R. Thiazolidinediones and insulin resistance: peroxisome proliferator activated receptor γ activation stimulates expression of the CAP gene. Proc. Natl. Acad. Sci. USA 95, 14751–14756 (1998). · DOI
- Burant, C.F. et al. Troglitazone action is independent of adipose tissue. J. Clin. Invest. 100, 2900–2908 (1997). · DOI · Paper page
- Chao, L. et al. Adipose tissue is required for the antidiabetic, but not for the hypolipidemic, effect of thiazolidinediones. J. Clin. Invest. 106, 1221–1228 (2000). · DOI · Paper page
- Gavrilova, O. et al. Liver peroxisome proliferator-activated receptor γ contributes to hepatic steatosis, triglyceride clearance, and regulation of body fat mass. J. Biol. Chem. 278, 34268–34276 (2003). · DOI · Paper page
- Kim, J.K. et al. Differential effects of rosiglitazone on skeletal muscle and liver insulin resistance in A-ZIP/F-1 fatless mice. Diabetes 52, 1311–1318 (2003). · DOI
- Miles, P.D., Barak, Y., He, W., Evans, R.M. & Olefsky, J.M. Improved insulin-sensitivity in mice heterozygous for PPAR-γ deficiency. J. Clin. Invest. 105, 287–292 (2000). · DOI · Paper page
- Berger, J.P. et al. Distinct properties and advantages of a novel peroxisome proliferator-activated protein γ selective modulator. Mol. Endocrinol. 17, 662–676 (2003). · DOI · Paper page
- Rangwala, S.M. et al. Genetic modulation of PPARg phosphorylation regulates insulin sensitivity. Dev. Cell 5, 657–663 (2003). · DOI
- Ristow, M., Muller-Wieland, D., Pfeiffer, A., Krone, W. & Kahn, R. Obesity associated with a mutation in a genetic regulator of adipocyte differentiation. N. Engl. J. Med. 339, 953–959 (1998). · DOI
- Matsusue, K. et al. Liver-specific disruption of PPARγ in leptin-deficient mice improves fatty liver but aggravates diabetic phenotypes. J. Clin. Invest. 111, 737–747 (2003). · DOI · Paper page
- He, W. et al. Adipose-specific peroxisome proliferator-activated receptor γ knockout causes insulin resistance in fat and liver but not in muscle. Proc. Natl. Acad. Sci. USA 100, 15712–15717 (2003). · DOI · Paper page
- Koutnikova, H. et al. Compensation by the muscle limits the metabolic consequences of lipodystrophy in PPAR γ hypomorphic mice. Proc. Natl. Acad. Sci. USA 100, 14457–14462 (2003). · DOI
- Hevener, A.L. et al. Muscle-specific Pparg deletion causes insulin resistance. Nat Med. 9, 1491–1497 (2003). · DOI · Paper page
- Reddy, J.K. & Hashimoto, T. Peroxisomal β-oxidation and peroxisome proliferator-activated receptor α: an adaptive metabolic system. Annu. Rev. Nutr. 21, 193–230 (2001). · DOI · Paper page
- Kersten, S. et al. Peroxisome proliferator-activated receptor α mediates the adaptive response to fasting. J. Clin. Invest. 103, 1489–1498 (1999). · DOI · Paper page
- Chou, C.J. et al. WY14,643, a peroxisome proliferator-activated receptor α (PPARα) agonist, improves hepatic and muscle steatosis and reverses insulin resistance in lipoatrophic A-ZIP/F-1 mice. J. Biol. Chem. 277, 24484–24489 (2002). · DOI
- Kim, H. et al. Peroxisome proliferator-activated receptor-α agonist treatment in a transgenic model of type 2 diabetes reverses the lipotoxic state and improves glucose homeostasis. Diabetes 52, 1770–1778 (2003). · DOI
- Peters, J.M. et al. Growth, adipose, brain, and skin alterations resulting from targeted disruption of the mouse peroxisome proliferator-activated receptor β(δ). Mol. Cell. Biol. 20, 5119–5128 (2000). · DOI
- Oliver, W.R. et al. A selective peroxisome proliferator-activated receptor δ agonist promotes reverse cholesterol transport. Proc. Natl. Acad. Sci. USA 98, 5306–5311 (2001). · DOI · Paper page
- Puigserver, P. et al. A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis. Cell 92, 829–839 (1998). · DOI · Paper page
- Muoio, D.M. et al. Fatty acid homeostasis and induction of lipid regulatory genes in skeletal muscles of peroxisome proliferator-activated receptor (PPAR) α knock-out mice. Evidence for compensatory regulation by PPAR δ. J. Biol. Chem. 277, 26089–26097 (2002). · DOI · Paper page
- Dressel, U. et al. The peroxisome proliferator-activated receptor β/δ agonist, GW501516, regulates the expression of genes involved in lipid catabolism and energy uncoupling in skeletal muscle cells. Mol. Endocrinol. 17, 2477–2493 (2003). · DOI · Paper page
- Gupta, R. et al. Activation of nuclear hormone receptor peroxisome proliferator-activated receptor-δ accelerates intestinal adenoma growth. Nat. Med. 10, 245–247 (2004). · DOI · Paper page
- Saez, E. et al. Activators of the nuclear receptor PPARγ enhance colon polyp formation. Nat. Med. 4, 1058–1061 (1998). · DOI · Paper page
- Sarraf, P. et al. Differentiation and reversal of malignant changes in colon cancer through PPARγ. Nat. Med. 4, 1046–1052 (1998). · DOI · Paper page
- Lefebvre, A.-M. et al. Activation of the peroxisome proliferator-activated receptor γ promotes the development of colon tumors in C57BL/6J-APCMin/+ mice. Nat. Med. 4, 1053–1057 (1998). · DOI · Paper page
- Lee, C.H. et al. Transcriptional repression of atherogenic inflammation: modulation by PPARδ. Science 302, 453–457 (2003). · DOI · Paper page
- Ricote, M., Valledor, A.F. & Glass, C.K. Decoding transcriptional programs regulated by PPARs and LXRs in the macrophage: effects on lipid homeostasis, inflammation, and atherosclerosis. Arterioscler. Thromb. Vasc. Biol. 24, 230–239 (2004). · DOI
Cited by
Hepatic Stellate Cells: Protean, Multifunctional, and Enigmatic Cells of the Liver
Friedman, S. L. (2008) · Physiological Reviews · doi:10.1152/physrev.00013.2007 · Cited by 2,842
Adiponectin and adiponectin receptors in insulin resistance, diabetes, and the metabolic syndrome
Kadowaki, T. (2006) · Journal of Clinical Investigation · doi:10.1172/jci29126 · Cited by 2,824
(1998) · PubMed · Cited by 2,737
Macrophage-specific PPARγ controls alternative activation and improves insulin resistance
Odegaard, J. I., Ricardo-Gonzalez, R. R., Goforth, M. H., Morel, C. R., Subramanian, V., Mukundan, L., Eagle, A. R., Vats, D., Brombacher, F., Ferrante, A. W., et al. (2007) · Nature · doi:10.1038/nature05894 · Cited by 2,107
PPARγ signaling and metabolism: the good, the bad and the future
Ahmadian, M., Suh, J. M., Hah, N., Liddle, C., Atkins, A. R., Downes, M., & Evans, R. M. (2013) · Nature Medicine · doi:10.1038/nm.3159 · Cited by 2,016
Self-citationMacrophage-mediated inflammation in metabolic disease
Chawla, A., Nguyen, K. D., & Goh, Y. P. S. (2011) · Nature reviews. Immunology · doi:10.1038/nri3071 · Cited by 1,314
Anatomical profiling of nuclear receptor expression reveals a hierarchical transcriptional network
Bookout, A. L., Jeong, Y., Downes, M., Yu, R. T., Evans, R. M., & Mangelsdorf, D. J. (2006) · Cell · doi:10.1016/j.cell.2006.06.049 · Cited by 1,015
Self-citationPeroxisome Proliferator-Activated Receptor Alpha Target Genes
Rakhshandehroo, M., Knoch, B., Müller, M., & Kersten, S. (2010) · PPAR Research · doi:10.1155/2010/612089 · Cited by 1,020
Tyagi, S., Gupta, P., Saini, A., Kaushal, C., & Sharma, S. (2011) · Journal of Advanced Pharmaceutical Technology & Research · doi:10.4103/2231-4040.90879 · Cited by 1,017
Jin, Q., Yu, L., Wang, L., Zhang, Z., Kasper, L. H., Lee, J., Wang, C., Brindle, P. K., Dent, S. Y. R., & Ge, K. (2011) · The EMBO Journal · doi:10.1038/emboj.2010.318 · Cited by 877
Feige, J. N., Gelman, L., Michalik, L., Desvergne, B., & Wahli, W. (2006) · Progress in Lipid Research · doi:10.1016/j.plipres.2005.12.002 · Cited by 786
Dietary fats and prevention of type 2 diabetes
Risérus, U., Willett, W. C., & Hu, F. B. (2009) · Progress in Lipid Research · doi:10.1016/j.plipres.2008.10.002 · Cited by 753
Feige, J. N., Lagouge, M., Canto, C., Strehle, A., Houten, S. M., Milne, J. C., Lambert, P. D., Mataki, C., Elliott, P. J., & Auwerx, J. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.08.017 · Cited by 719
Targeting adipose tissue in the treatment of obesity-associated diabetes
Kusminski, C. M., Bickel, P. E., & Scherer, P. E. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.75 · Cited by 678
Stahlhut, R. W., van Wijngaarden, E., Dye, T. D., Cook, S., & Swan, S. H. (2007) · Environmental Health Perspectives · doi:10.1289/ehp.9882 · Cited by 646
Alternative macrophage activation and metabolism
Odegaard, J. I., & Chawla, A. (2011) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-011110-130138 · Cited by 640
The Liver as an Endocrine Organ—Linking NAFLD and Insulin Resistance
Watt, M. J., Miotto, P. M., De Nardo, W., & Montgomery, M. K. (2019) · Endocrine Reviews · doi:10.1210/er.2019-00034 · Cited by 615
Schaeffer, L., Gohlke, H., Müller, M., Heid, I. M., Palmer, L. J., Kompauer, I., Demmelmair, H., Illig, T., Koletzko, B., & Heinrich, J. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl117 · Cited by 561
Relaxin family peptides and their receptors
Bathgate, R. A. D., Halls, M. L., van der Westhuizen, E. T., Callander, G. E., Kocan, M., & Summers, R. J. (2013) · Physiological Reviews · doi:10.1152/physrev.00001.2012 · Cited by 534
High-fat diets cause insulin resistance despite an increase in muscle mitochondria
Hancock, C. R., Han, D.-H., Chen, M., Terada, S., Yasuda, T., Wright, D. C., & Holloszy, J. O. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802057105 · Cited by 538
Control of Macrophage Activation and Function by PPARs
Chawla, A. (2010) · Circulation Research · doi:10.1161/circresaha.110.216523 · Cited by 531
PER2 controls lipid metabolism by direct regulation of PPARγ
Grimaldi, B., Bellet, M. M., Katada, S., Astarita, G., Hirayama, J., Amin, R. H., Granneman, J. G., Piomelli, D., Leff, T., & Sassone-Corsi, P. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.10.005 · Cited by 489
Berberine in Cardiovascular and Metabolic Diseases: From Mechanisms to Therapeutics
Feng, X., Sureda, A., Jafari, S., Memariani, Z., Tewari, D., Annunziata, G., Barrea, L., Hassan, S. T. S., Šmejkal, K., Malaník, M., et al. (2019) · Theranostics · doi:10.7150/thno.30787 · Cited by 465
Nitrolinoleic acid. An endogenous peroxisome proliferator-activated receptor γ ligand
Schopfer, F. J., Lin, Y., Baker, P. R. S., Cui, T., Garcia-Barrio, M., Zhang, J., Chen, K., Chen, Y. E., & Freeman, B. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408384102 · Cited by 428
Critical review on the presence of phthalates in food and evidence of their biological impact
Giuliani, A., Zuccarini, M., Cichelli, A., Khan, H., & Reale, M. (2020) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph17165655 · Cited by 420
Pharmacological approaches to restore mitochondrial function
Andreux, P. A., Houtkooper, R. H., & Auwerx, J. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4023 · Cited by 383
PPAR-δ senses and orchestrates clearance of apoptotic cells to promote tolerance
Mukundan, L., Odegaard, J. I., Morel, C. R., Heredia, J. E., Mwangi, J. W., Ricardo-Gonzalez, R. R., Goh, Y. P. S., Eagle, A. R., Dunn, S. E., Awakuni, J. U. H., et al. (2009) · Nature Medicine · doi:10.1038/nm.2048 · Cited by 368
Mitochondria are impaired in the adipocytes of type 2 diabetic mice.
Choo, H.-J., Kim, J.-H., Kwon, O.-B., Lee, C. S., Mun, J. Y., Han, S. S., Yoon, Y.-S., Yoon, G., Choi, K.-M., & Ko, Y.-G. (2006) · Diabetologia · doi:10.1007/s00125-006-0170-2 · Cited by 365
Fatty Acid Transduction of Nitric Oxide Signaling
Baker, P. R. S., Lin, Y., Schopfer, F. J., Woodcock, S. R., Groeger, A. L., Batthyany, C., Sweeney, S., Long, M. H., Iles, K. E., Baker, L. M. S., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504212200 · Cited by 358
Nitrated Fatty Acids: Endogenous Anti-inflammatory Signaling Mediators
Cui, T., Schopfer, F. J., Zhang, J., Chen, K., Ichikawa, T., Baker Paul, R. S., Batthyany, C., Chacko, B. K., Feng, X., Patel, R. P., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603357200 · Cited by 351
The Role of Angiopoietin-Like Proteins in Angiogenesis and Metabolism
Hato, T., Tabata, M., & Oike, Y. (2008) · Trends in Cardiovascular Medicine · doi:10.1016/j.tcm.2007.10.003 · Cited by 351
Rong, J. X., Qiu, Y., Hansen, M. K., Zhu, L., Zhang, V., Xie, M., Okamoto, Y., Mattie, M. D., Higashiyama, H., Asano, S., et al. (2007) · Diabetes · doi:10.2337/db06-1135 · Cited by 335
Yoon, M. (2009) · Pharmacological Research · doi:10.1016/j.phrs.2009.02.004 · Cited by 336
Sun, Q., Cornelis, M. C., Townsend, M. K., Tobias, D. K., Eliassen, A. H., Franke, A. A., Hauser, R., & Hu, F. B. (2014) · Environmental Health Perspectives · doi:10.1289/ehp.1307201 · Cited by 274
Effect of intermittent fasting and refeeding on insulin action in healthy men
Halberg, N., Henriksen, M., Söderhamn, N., Stallknecht, B., Ploug, T., Schjerling, P., & Dela, F. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00683.2005 · Cited by 259
Garcia-Roves, P., Huss, J. M., Han, D.-H., Hancock, C. R., Iglesias-Gutierrez, E., Chen, M., & Holloszy, J. O. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0704024104 · Cited by 246
Powelka, A. M. (2005) · Journal of Clinical Investigation · doi:10.1172/jci26040 · Cited by 236
PPARs as Nuclear Receptors for Nutrient and Energy Metabolism
Hong, F., Pan, S., Guo, Y., Xu, P., & Zhai, Y. (2019) · Molecules · doi:10.3390/molecules24142545 · Cited by 233
Mechanisms of Disease: pathogenesis of nonalcoholic fatty liver disease
Sanyal, A. J. (2005) · Nature Clinical Practice Gastroenterology & Hepatology · doi:10.1038/ncpgasthep0084 · Cited by 216
Angiopoietin-related growth factor antagonizes obesity and insulin resistance
Oike, Y., Akao, M., Yasunaga, K., Yamauchi, T., Morisada, T., Ito, Y., Urano, T., Kimura, Y., Kubota, Y., Maekawa, H., et al. (2005) · Nature Medicine · doi:10.1038/nm1214 · Cited by 200
Yang, H., Youm, Y.-H., & Dixit, V. D. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900562 · Cited by 196
Obesity, Peroxisome Proliferator-Activated Receptor, and Atherosclerosis in Type 2 Diabetes
Blaschke, F., Takata, Y., Caglayan, E., Law, R. E., & Hsueh, W. A. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000191663.12164.77 · Cited by 176
Molecular recognition of nitrated fatty acids by PPARγ
Li, Y., Zhang, J., Schopfer, F. J., Martynowski, D., Garcia-Barrio, M. T., Kovach, A., Suino-Powell, K., Baker, P. R. S., Freeman, B. A., Chen, Y. E., et al. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1447 · Cited by 168
FSH regulates fat accumulation and redistribution in aging through the Gαi/Ca 2+ /CREB pathway
Liu, X., Chan, H. C., Ding, G., Cai, J., Song, Y., Wang, T., Zhang, D., Chen, H., Yu, M. K., Wu, Y., et al. (2015) · Aging Cell · doi:10.1111/acel.12331 · Cited by 164
Atherton, H. J., Bailey, N. J., Zhang, W., Taylor, J., Major, H., Shockcor, J., Clarke, K., & Griffin, J. L. (2006) · Physiological Genomics · doi:10.1152/physiolgenomics.00060.2006 · Cited by 159
The Role of Mitochondria in the Pathophysiology of Skeletal Muscle Insulin Resistance
Pagel-Langenickel, I., Bao, J., Pang, L., & Sack, M. N. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0003 · Cited by 154
Liver X receptors as regulators of macrophage inflammatory and metabolic pathways
A-González, N., & Castrillo, A. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.12.015 · Cited by 139
Fat-induced satiety factor oleoylethanolamide enhances memory consolidation
Campolongo, P., Roozendaal, B., Trezza, V., Cuomo, V., Astarita, G., Fu, J., McGaugh, J. L., & Piomelli, D. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903038106 · Cited by 133
Extracellular ATP is generated by ATP synthase complex in adipocyte lipid rafts.
Kim, B.-W., Choo, H.-J., Lee, J.-W., Kim, J.-H., & Ko, Y.-G. (2004) · Experimental & Molecular Medicine · doi:10.1038/emm.2004.60 · Cited by 128
A dysregulated acetyl/SUMO switch of FXR promotes hepatic inflammation in obesity
Kim, D., Xiao, Z., Kwon, S., Sun, X., Ryerson, D., Tkac, D., Ma, P., Wu, S., Chiang, C., Zhou, E., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201489527 · Cited by 126
Social Isolation Affects the Development of Obesity and Type 2 Diabetes in Mice
Nonogaki, K., Nozue, K., & Oka, Y. (2007) · Endocrinology · doi:10.1210/en.2007-0296 · Cited by 115
Rector, R. S., Thyfault, J. P., Laye, M. J., Morris, R. T., Borengasser, S. J., Uptergrove, G. M., Chakravarthy, M. V., Booth, F. W., & Ibdah, J. A. (2008) · The Journal of Physiology · doi:10.1113/jphysiol.2008.156745 · Cited by 110
Golfman, L. S., Wilson, C. R., Sharma, S., Burgmaier, M., Young, M. E., Guthrie, P. H., Van Arsdall, M., Adrogue, J. V., Brown, K. K., & Taegtmeyer, H. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00055.2005 · Cited by 99
Hafizi Abu Bakar, M., Kian Kai, C., Wan Hassan, W. N., Sarmidi, M. R., Yaakob, H., & Zaman Huri, H. (2015) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.2601 · Cited by 91
Goto, T., Kim, Y.-I., Furuzono, T., Takahashi, N., Yamakuni, K., Yang, H.-E., Li, Y., Ohue, R., Nomura, W., Sugawara, T., et al. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.02.154 · Cited by 80
Role of bile acids in the regulation of the metabolic pathways
Taoka, H., Yokoyama, Y., Morimoto, K., Kitamura, N., Tanigaki, T., Takashina, Y., Tsubota, K., & Watanabe, M. (2016) · World Journal of Diabetes · doi:10.4239/wjd.v7.i13.260 · Cited by 80
Xie, L.-W., Atanasov, A. G., Guo, D.-A., Malainer, C., Zhang, J.-X., Zehl, M., Guan, S.-H., Heiss, E. H., Urban, E., Dirsch, V. M., et al. (2014) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2014.01.029 · Cited by 76
Limited therapeutic efficacy of pioglitazone on progression of hepatic fibrosis in rats
Leclercq, I. A. (2006) · Gut · doi:10.1136/gut.2005.079194 · Cited by 67
Dynamic repression by BCL6 controls the genome-wide liver response to fasting and steatosis
Sommars, M. A., Ramachandran, K., Senagolage, M. D., Futtner, C. R., Germain, D. M., Allred, A. L., Omura, Y., Bederman, I. R., & Barish, G. D. (2019) · eLife · doi:10.7554/elife.43922 · Cited by 66
Self-citationEndothelium as a gatekeeper of fatty acid transport
Mehrotra, D., Wu, J., Papangeli, I., & Chun, H. J. (2014) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2013.11.001 · Cited by 60
HAMMOUDA, S., GHZAIEL, I., KHAMLAOUI, W., HAMMAMI, S., MHENNI, S. Y., SAMET, S., HAMMAMI, M., & ZARROUK, A. (2020) · Prostaglandins, Leukotrienes and Essential Fatty Acids · doi:10.1016/j.plefa.2020.102159 · Cited by 50
Abu Bakar, M. H., Azmi, M. N., Shariff, K. A., & Tan, J. S. (2019) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-018-2920-2 · Cited by 47
Xing, X., Li, D., Chen, D., Zhou, L., Chonan, R., Yamahara, J., Wang, J., & Li, Y. (2014) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2014.08.001 · Cited by 46
Sofer, S., Stark, A. H., & Madar, Z. (2015) · Advances in Nutrition · doi:10.3945/an.114.007518 · Cited by 39
Zhuang, L.-N., Hu, W.-X., Xin, S.-M., Zhao, J., & Pei, G. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.256099 · Cited by 34
Lee, J. S., O’Connell, E. M., Pacher, P., & Lohoff, F. W. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10081758 · Cited by 31
Effect of Ketogenic Diet on Obesity and Other Metabolic Disorders: Narrative Review
Baylie, T., Ayelgn, T., Tiruneh, M., & Tesfa, K. (2024) · Diabetes, Metabolic Syndrome and Obesity · doi:10.2147/dmso.s447659 · Cited by 27
Acevedo, L. M., Raya, A. I., Martínez-Moreno, J. M., Aguilera–Tejero, E., & Rivero, J.-L. L. (2017) · PLOS ONE · doi:10.1371/journal.pone.0173028 · Cited by 24
Clark, J. E. (2012) · Journal of Diabetes & Metabolic Disorders · doi:10.1186/2251-6581-11-19 · Cited by 19
Guru, B., Tamrakar, A. K., Manjula, S. N., & Prashantha Kumar, B. R. (2022) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2022.175322 · Cited by 18
Bates, D. J. P., Smitherman, P. K., Townsend, A. J., King, S. B., & Morrow, C. S. (2011) · Biochemistry · doi:10.1021/bi2005784 · Cited by 15
Savoia, C., Ebrahimian, T., Lemarié, C. A., Paradis, P., Iglarz, M., Amiri, F., Javeshgani, D., & Schiffrin, E. L. (2010) · Clinical Science · doi:10.1042/cs20090289 · Cited by 15
PPAR agonists, - could tissue targeting pave the way
Bugge, A., & Holst, D. (2017) · Biochimie · doi:10.1016/j.biochi.2016.10.017 · Cited by 14
Disabled-2 Determines Commitment of a Pre-adipocyte Population in Juvenile Mice
Tao, W., Moore, R., Meng, Y., Yeasky, T. M., Smith, E. R., & Xu, X.-X. (2016) · Scientific Reports · doi:10.1038/srep35947 · Cited by 13
Metadata
- Authors
- Evans, R. M., Barish, G. D., & Wang, Y.-X.
- Venue
- Nature Medicine
- Published
- 2004-03-31
- Volume
- 10
- Issue
- 4
- Pages
- 355-361
- ISSN
- 1078-8956 (ISSN-L)
- 1546-170X
- OpenAlex
- W2163810943
- Cited by
- 1,602
- References
- 25
- FWCI
- 31.71
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.