International Union of Pharmacology. LXI. Peroxisome Proliferator-Activated Receptors

The peroxisome proliferator-activated receptor-γ is a negative regulator of macrophage activation

Ricote, M., Li, A. C., Willson, T. M., Kelly, C. J., & Glass, C. K. (1998) · Nature · doi:10.1038/34178 · Cited by 3,525

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

The coregulator exchange in transcriptional functions of nuclear receptors

Glass, C. K., & Rosenfeld, M. G. (2000) · Genes & Development · doi:10.1101/gad.14.2.121 · Cited by 2,233

Differential expression of peroxisome proliferator-activated receptors (PPARs): tissue distribution of PPAR-alpha, -beta, and -gamma in the adult rat

Braissant, O., Foufelle, F., Scotto, C., Dauça, M., & Wahli, W. (1996) · Endocrinology · doi:10.1210/endo.137.1.8536636 · Cited by 2,217

Fatty acids and eicosanoids regulate gene expression through direct interactions with peroxisome proliferator-activated receptors α and γ

Kliewer, S. A., Sundseth, S. S., Jones, S. A., Brown, P. J., Wisely, G. B., Koble, C. S., Devchand, P., Wahli, W., Willson, T. M., Lenhard, J. M., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.9.4318 · Cited by 2,164

Hypolipidemic drugs, polyunsaturated fatty acids, and eicosanoids are ligands for peroxisome proliferator-activated receptors α and δ

Forman, B. M., Chen, J., & Evans, R. M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.9.4312 · Cited by 2,116

Roles of PPARs in health and disease

Kersten, S., Desvergne, B., & Wahli, W. (2000) · Nature · doi:10.1038/35013000 · Cited by 1,956

The PPARs: From Orphan Receptors to Drug Discovery

Willson, T. M., Brown, P. J., Sternbach, D. D., & Henke, B. R. (2000) · Journal of Medicinal Chemistry · doi:10.1021/jm990554g · Cited by 1,816

The PPARα–leukotriene B4 pathway to inflammation control

Devchand, P. R., Keller, H., Peters, J. M., Vazquez, M., Gonzalez, F. J., & Wahli, W. (1996) · Nature · doi:10.1038/384039a0 · Cited by 1,345

Peroxisome-Proliferator-Activated Receptor δ Activates Fat Metabolism to Prevent Obesity

Wang, Y.-X., Lee, C.-H., Tiep, S., Yu, R. T., Ham, J., Kang, H., & Evans, R. M. (2003) · Cell · doi:10.1016/s0092-8674(03)00269-1 · Cited by 1,296

A unified nomenclature system for the nuclear receptor superfamily

(1999) · Cell · doi:10.1016/s0092-8674(00)80726-6 · Cited by 1,208

Molecular recognition of fatty acids by peroxisome proliferator-activated receptors

Xu, H. E., Lambert, M. H., Montana, V. G., Parks, D. J., Blanchard, S. G., Brown, P. J., Sternbach, D. D., Lehmann, J. M., Wisely, G. B., Willson, T. M., et al. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80467-0 · Cited by 1,169

Peroxisome Proliferator-activated Receptors α and γ Are Activated by Indomethacin and Other Non-steroidal Anti-inflammatory Drugs

Lehmann, J. M., Lenhard, J. M., Oliver, B. B., Ringold, G. M., & Kliewer, S. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.6.3406 · Cited by 1,110

The mouse peroxisome proliferator activated receptor recognizes a response element in the 5′ flanking sequence of the rat acyl CoA oxidase gene

Tugwood, J. D., Issemann, I., Anderson, R. G., Bundell, K. R., McPheat, W. L., & Green, S. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05072.x · Cited by 895

Activation of peroxisome proliferator-activated receptor δ induces fatty acid β-oxidation in skeletal muscle and attenuates metabolic syndrome

Tanaka, T., Yamamoto, J., Iwasaki, S., Asaba, H., Hamura, H., Ikeda, Y., Watanabe, M., Magoori, K., Ioka, R. X., Tachibana, K., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0306981100 · Cited by 832

Role of the Adipocyte, Free Fatty Acids, and Ectopic Fat in Pathogenesis of Type 2 Diabetes Mellitus: Peroxisomal Proliferator-Activated Receptor Agonists Provide a Rational Therapeutic Approach

Bays, H., Mandarino, L., & DeFronzo, R. A. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2003-030723 · Cited by 664

The Effects of Rosiglitazone on Insulin Sensitivity, Lipolysis, and Hepatic and Skeletal Muscle Triglyceride Content in Patients With Type 2 Diabetes

Mayerson, A. B., Hundal, R. S., Dufour, S., Lebon, V., Befroy, D., Cline, G. W., Enocksson, S., Inzucchi, S. E., Shulman, G. I., & Petersen, K. F. (2002) · Diabetes · doi:10.2337/diabetes.51.3.797 · Cited by 647

Peroxisome Proliferator-activated Receptor α Activators Improve Insulin Sensitivity and Reduce Adiposity

Guerre-Millo, M., Gervois, P., Raspé, E., Madsen, L., Poulain, P., Derudas, B., Herbert, J.-M., Winegar, D. A., Willson, T. M., Fruchart, J.-C., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.22.16638 · Cited by 605

Effects of peroxisome proliferator-activated receptor δ on placentation, adiposity, and colorectal cancer

Barak, Y., Liao, D., He, W., Ong, E. S., Nelson, M. C., Olefsky, J. M., Boland, R., & Evans, R. M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.012610299 · Cited by 586

Diabetes, Plasma Insulin, and Cardiovascular Disease: Subgroup Analysis From the Department of Veterans Affairs High-Density Lipoprotein Intervention Trial (VA-HIT)

Rubins, H. B. (2002) · Archives of Internal Medicine · doi:10.1001/archinte.162.22.2597 · Cited by 586

Functional Consequences of Cysteine Modification in the Ligand Binding Sites of Peroxisome Proliferator Activated Receptors by GW9662

Leesnitzer, L. M., Parks, D. J., Bledsoe, R. K., Cobb, J. E., Collins, J. L., Consler, T. G., Davis, R. G., Hull-Ryde, E. A., Lenhard, J. M., Patel, L., et al. (2002) · Biochemistry · doi:10.1021/bi0159581 · Cited by 566

Coordinate Regulation of the Expression of the Fatty Acid Transport Protein and Acyl-CoA Synthetase Genes by PPARα and PPARγ Activators

Martin, G., Schoonjans, K., Lefebvre, A.-M., Staels, B., & Auwerx, J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.45.28210 · Cited by 551

Peroxisome proliferator‐activated receptor δ controls muscle development and oxydative capability

Luquet, S., Lopez‐Soriano, J., Holst, D., Fredenrich, A., Melki, J., Rassoulzadegan, M., & Grimaldi, P. A. (2003) · The FASEB Journal · doi:10.1096/fj.03-0269fje · Cited by 509

Muscle-specific PPARγ-deficient mice develop increased adiposity and insulin resistance but respond to thiazolidinediones

Norris, A. W., Chen, L., Fisher, S. J., Szanto, I., Ristow, M., Jozsi, A. C., Hirshman, M. F., Rosen, E. D., Goodyear, L. J., Gonzalez, F. J., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci17305 · Cited by 417

Fibrates downregulate apolipoprotein C-III expression independent of induction of peroxisomal acyl coenzyme A oxidase. A potential mechanism for the hypolipidemic action of fibrates.

Staels, B., Vu-Dac, N., Kosykh, V. A., Saladin, R., Fruchart, J. C., Dallongeville, J., & Auwerx, J. (1995) · Journal of Clinical Investigation · doi:10.1172/jci117717 · Cited by 410

Impaired skin wound healing in peroxisome proliferator–activated receptor (PPAR)α and PPAR β mutant mice

Michalik, L., Desvergne, B., Tan, N. S., Basu-Modak, S., Escher, P., Rieusset, J., Peters, J. M., Kaya, G., Gonzalez, F. J., Zakany, J., et al. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200011148 · Cited by 406

Critical roles of PPARβ/δ in keratinocyte response to inflammation

Tan, N. S., Michalik, L., Noy, N., Yasmin, R., Pacot, C., Heim, M., Flühmann, B., Desvergne, B., & Wahli, W. (2001) · Genes & Development · doi:10.1101/gad.207501 · Cited by 398

PPARγ coactivator 1β/ERR ligand 1 is an ERR protein ligand, whose expression induces a high-energy expenditure and antagonizes obesity.

Kamei, Y., Ohizumi, H., Fujitani, Y., Nemoto, T., Tanaka, T., Takahashi, N., Kawada, T., Miyoshi, M., Ezaki, O., & Kakizuka, A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2135217100 · Cited by 357

Control of human muscle-type carnitine palmitoyltransferase I gene transcription by peroxisome proliferator-activated receptor

Mascaró, C., Acosta, E., Ortiz, J. A., Marrero, P. F., Hegardt, F. G., & Haro, D. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.15.8560 · Cited by 318

Activation of PPARδ alters lipid metabolism in db/db mice

Leibowitz, M. D., Fiévet, C., Hennuyer, N., Peinado-Onsurbe, J., Duez, H., Berger, J., Cullinan, C. A., Sparrow, C. P., Baffic, J., Berger, G. D., et al. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01554-4 · Cited by 308

Dual and pan-peroxisome proliferator-activated receptors (PPAR) co-agonism: the bezafibrate lessons

Tenenbaum, A., Motro, M., & Fisman, E. Z. (2005) · Cardiovascular Diabetology · doi:10.1186/1475-2840-4-14 · Cited by 246

Retinoic Acid Is a High Affinity Selective Ligand for the Peroxisome Proliferator-activated Receptor β/δ

Shaw, N., Elholm, M., & Noy, N. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c300368200 · Cited by 243

PPAR-α–Null Mice Are Protected From High-Fat Diet–Induced Insulin Resistance

Guerre-Millo, M., Rouault, C., Poulain, P., André, J., Poitout, V., Peters, J. M., Gonzalez, F. J., Fruchart, J.-C., Reach, G., & Staels, B. (2001) · Diabetes · doi:10.2337/diabetes.50.12.2809 · Cited by 241

Fibrates Suppress Fibrinogen Gene Expression in Rodents Via Activation of the Peroxisome Proliferator-Activated Receptor-

Kockx, M., Gervois, P. P., Poulain, P., Derudas, B., Peters, J. M., Gonzalez, F. J., Princen, H. M. G., Kooistra, T., & Staels, B. (1999) · Blood · doi:10.1182/blood.v93.9.2991 · Cited by 139

Peroxisome Proliferator-activated Receptor β/δ Regulates Very Low Density Lipoprotein Production and Catabolism in Mice on a Western Diet

Akiyama, T. E., Lambert, G., Nicol, C. J., Matsusue, K., Peters, J. M., Brewer, H. B., & Gonzalez, F. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312802200 · Cited by 97

Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).

Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894

Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1

Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,897

Untitled work

(1998) · PubMed · Cited by 2,737

International Union of Basic and Clinical Pharmacology. LXXIX. Cannabinoid Receptors and Their Ligands: Beyond CB1 and CB2

Pertwee, R. G., Howlett, A. C., Abood, M. E., Alexander, S. P. H., Di Marzo, V., Elphick, M. R., Greasley, P. J., Hansen, H. S., Kunos, G., Mackie, K., et al. (2010) · Pharmacological Reviews · doi:10.1124/pr.110.003004 · Cited by 1,605

Mitonuclear communication in homeostasis and stress

Quirós, P. M., Mottis, A., & Auwerx, J. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.23 · Cited by 787