Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 1,602

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

Evans, Ronald M, Barish, Grant D, Wang, Yong-Xu·2004·Nature Medicine

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.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1038/nm1025

Cites

25 of 25 references verified0 citation errors · 0 not checkable

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.

A few free checks a day · papers already verified open instantly · results are public

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

Research works printed but not linked: 80

  1. Tartaglia, L. et al. Identification and expression cloning of a leptin receptor OB-R. Cell 83, 1263–1271 (1995). · DOI · Paper page
  2. Seeley, R. & Woods, S. Monitoring of stored and available fuel by the CNS: implications for obesity. Nat. Rev. Neurosci. 4, 901–909 (2003). · DOI
  3. Drazen, D. & Woods, S. Peripheral signals in the control of satiety and hunger. Curr. Opin. Clin. Nutr. Metab. Care 6, 621–629 (2003). · DOI
  4. Bachman, E. et al. βAR signaling required for diet-induced thermogenesis and obesity resistance. Science 297, 843–845 (2002). · DOI · Paper page
  5. Wu, Z. et al. Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1. Cell 98, 115–124 (1999). · DOI · Paper page
  6. Fleury, C. et al. Uncoupling protein-2: a novel gene linked to obesity and hyperinsulinemia. Nat. Genet. 15, 269–272 (1997). · DOI · Paper page
  7. 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
  8. 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
  9. 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
  10. 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
  11. Enerback, S. et al. Mice lacking mitochondrial uncoupling protein are cold-sensitive but not obese. Nature 387, 90–94 (1997). · DOI · Paper page
  12. 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
  13. 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
  14. 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
  15. 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
  16. Sun, X.J. et al. Role of IRS-2 in insulin and cytokine signaling. Nature 377, 173–177 (1995). · DOI · Paper page
  17. 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
  18. 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
  19. 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
  20. 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
  21. 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
  22. 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
  23. 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
  24. 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
  25. Tamemoto, H. et al. Insulin resistance and growth retardation in mice lacking insulin receptor substrate-1. Nature 372, 182–186 (1994). · DOI · Paper page
  26. Withers, D. et al. Disruption of IRS-2 causes type 2 diabetes in mice. Nature 391, 900–904 (1998). · DOI
  27. 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
  28. 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
  29. Petersen, K.F. et al. Mitochondrial dysfunction in the elderly: possible role in insulin resistance. Science 300, 1140–1142 (2003). · DOI · Paper page
  30. 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
  31. 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
  32. 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
  33. 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
  34. Rosen, E.D., Walkey, C.J., Puigserver, P. & Spiegelman, B.M. Transcriptional regulation of adipogenesis. Genes Dev. 14, 1293–1307 (2000). · DOI · Paper page
  35. 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
  36. Barak, Y. et al. PPARγ is required for placental, cardiac, and adipose tissue development. Mol. Cell 4, 585–595 (1999). · DOI
  37. 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
  38. Kubota, N. et al. PPARγ mediates high-fat diet-induced adipocyte hypertrophy and insulin resistance. Mol. Cell 4, 597–609 (1999). · DOI · Paper page
  39. 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).
  40. 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
  41. 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
  42. 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
  43. Rosen, E.D. et al. C/EBPalpha induces adipogenesis through PPARγ: a unified pathway. Genes Dev. 16, 22–26 (2002). · DOI · Paper page
  44. 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
  45. 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
  46. 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
  47. Guan, H.-P. et al. A futile metabolic cycle activated in adipocytes by antidiabetic agents. Nat. Med. 8, 1122–1128 (2002). · DOI · Paper page
  48. 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
  49. Steppan, C.M. et al. The hormone resistin links obesity to diabetes. Nature 409, 307–312 (2001). · DOI · Paper page
  50. 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
  51. 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
  52. 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
  53. 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
  54. Burant, C.F. et al. Troglitazone action is independent of adipose tissue. J. Clin. Invest. 100, 2900–2908 (1997). · DOI · Paper page
  55. 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
  56. 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
  57. 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
  58. 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
  59. 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
  60. Rangwala, S.M. et al. Genetic modulation of PPARg phosphorylation regulates insulin sensitivity. Dev. Cell 5, 657–663 (2003). · DOI
  61. 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
  62. 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
  63. 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
  64. 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
  65. Hevener, A.L. et al. Muscle-specific Pparg deletion causes insulin resistance. Nat Med. 9, 1491–1497 (2003). · DOI · Paper page
  66. 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
  67. 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
  68. 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
  69. 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
  70. 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
  71. 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
  72. Puigserver, P. et al. A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis. Cell 92, 829–839 (1998). · DOI · Paper page
  73. 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
  74. 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
  75. 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
  76. Saez, E. et al. Activators of the nuclear receptor PPARγ enhance colon polyp formation. Nat. Med. 4, 1058–1061 (1998). · DOI · Paper page
  77. Sarraf, P. et al. Differentiation and reversal of malignant changes in colon cancer through PPARγ. Nat. Med. 4, 1046–1052 (1998). · DOI · Paper page
  78. 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
  79. Lee, C.H. et al. Transcriptional repression of atherogenic inflammation: modulation by PPARδ. Science 302, 453–457 (2003). · DOI · Paper page
  80. 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

See all 1,602

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.