Peroxisome proliferator-activated receptor delta

PPARD

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1GWX, 1Y0S, 2AWH, 2B50, 2BAW, 2ENV, 2GWX, 2J14, 2Q5G, 2XYJ, 2XYW, 2XYX, 2ZNP, 2ZNQ, 3D5F, 3DY6, 3ET2, 3GWX, 3GZ9, 3OZ0, 3PEQ, 3SP9, 3TKM

Identifiers

Aliases

PPARD, FAAR, NR1C2, NUC1, NUCI, NUCII, PPARB, peroxisome proliferator activated receptor delta

External IDs

MGI: 101884 HomoloGene: 4544 GeneCards: PPARD

Genetically Related Diseases

type 2 diabetes mellitus, diabetic cataract^[1]

Targeted by Drug

GW0742X, gw-501516, tretinoin^[2]

Gene ontology
Molecular function	• sequence-specific DNA binding • transcription coactivator activity • zinc ion binding • metal ion binding • NF-kappaB binding • steroid hormone receptor activity • fatty acid binding • protein binding • linoleic acid binding • drug binding • protein heterodimerization activity • lipid binding • transcription factor activity, sequence-specific DNA binding • transcription factor binding • RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding • DNA binding • transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding
Cellular component	• nucleoplasm • nuclear chromatin • nucleus
Biological process	• fatty acid catabolic process • positive regulation of myoblast proliferation • positive regulation of epidermis development • cell differentiation • negative regulation of smooth muscle cell proliferation • negative regulation of myoblast differentiation • regulation of transcription, DNA-templated • placenta development • regulation of transcription from RNA polymerase II promoter • positive regulation of vasodilation • negative regulation of smooth muscle cell migration • wound healing • mRNA transcription • cholesterol metabolic process • negative regulation of apoptotic process • response to glucose • response to activity • response to organic substance • generation of precursor metabolites and energy • regulation of fat cell differentiation • transcription, DNA-templated • positive regulation of transcription, DNA-templated • response to vitamin A • heart development • cell-substrate adhesion • keratinocyte proliferation • positive regulation of gene expression • proteoglycan metabolic process • regulation of cell proliferation • negative regulation of cell growth • fatty acid oxidation • positive regulation of cell proliferation • glucose metabolic process • phospholipid biosynthetic process • negative regulation of epithelial cell proliferation • positive regulation of skeletal muscle tissue regeneration • apoptotic signaling pathway • vitamin A metabolic process • positive regulation of phosphatidylinositol 3-kinase signaling • keratinocyte migration • adipose tissue development • transcription initiation from RNA polymerase II promoter • regulation of skeletal muscle satellite cell proliferation • positive regulation of fat cell differentiation • negative regulation of transcription, DNA-templated • negative regulation of inflammatory response • cellular response to lipopolysaccharide • cellular response to hypoxia • negative regulation of collagen biosynthetic process • glucose transport • positive regulation of insulin secretion • steroid hormone mediated signaling pathway • apoptotic process • cell proliferation • negative regulation of transcription from RNA polymerase II promoter • intracellular receptor signaling pathway • axon ensheathment • decidualization • fatty acid transport • embryo implantation • negative regulation of pri-miRNA transcription from RNA polymerase II promoter • lipid metabolic process • fatty acid beta-oxidation
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


5467


19015

Ensembl


ENSG00000112033


ENSMUSG00000002250

UniProt


Q03181


P35396

RefSeq (mRNA)


NM_001171818 NM_001171819 NM_001171820 NM_006238 NM_177435


NM_011145

RefSeq (protein)


NP_001165289.1 NP_001165290.1 NP_001165291.1 NP_006229.1 NP_803184.1


NP_035275.1

Location (UCSC)

Chr 6: 35.34 – 35.43 Mb

Chr 17: 28.23 – 28.3 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Peroxisome proliferator-activated receptor beta or delta (PPAR-β or PPAR-δ), also known as NR1C2 (nuclear receptor subfamily 1, group C, member 2) is a nuclear receptor that in humans is encoded by the PPARD gene.^[5]

This gene encodes a member of the peroxisome proliferator-activated receptor (PPAR) family. It was first identified in Xenopus in 1993.^[6]

Function

PPARδ is a nuclear hormone receptor that governs a variety of biological processes and may be involved in the development of several chronic diseases, including diabetes, obesity, atherosclerosis, and cancer.^[7]^[8]

PPARδ may function as an integrator of transcription repression and nuclear receptor signaling. It activates transcription of a variety of target genes by binding to specific DNA elements. Well described target genes of PPARδ include PDK4, ANGPTL4, PLIN2, and CD36. The expression of this gene is found to be elevated in colorectal cancer cells.^[9] The elevated expression can be repressed by adenomatosis polyposis coli (APC), a tumor suppressor protein involved in the APC/beta-catenin signaling pathway. Knockout studies in mice suggested the role of this protein in myelination of the corpus callosum, epidermal cell proliferation, and glucose^[10] and lipid metabolism.^[11]

This protein has been shown to be involved in differentiation, lipid accumulation,^[12] directional sensing, polarization, and migration in keratinocytes.^[13]

Role in cancer

Studies into the role of PPARδ in cancer have produced contradictory results and there is no scientific consensus on whether it promotes or prevents cancer formation.^[14]^[15]

Pharmacology

Several high affinity ligands for PPARδ have been developed, including GW501516 and GW0742, which play an important role in research. In one study utilizing such a ligand, it has been shown that agonism of PPARδ changes the body's fuel preference from glucose to lipids.^[16]

Tissue distribution

PPARδ is highly expressed in many tissues, including colon, small intestine, liver and keratinocytes, as well as in heart, spleen, skeletal muscle, lung, brain and thymus.^[17]

Knockout studies

Knockout mice lacking the ligand binding domain of PPARδ are viable. However these mice are smaller than the wild type both neo and postnatally. In addition, fat stores in the gonads of the mutants are smaller. The mutants also display increased epidermal hyperplasia upon induction with TPA.^[18]

Ligands

PPARδ is activated in the cell by various fatty acids and fatty acid derivatives.^[7] Examples of naturally occurring fatty acids that bind with and activate PPAR delta include arachidonic acid and certain members of the 15-Hydroxyicosatetraenoic acid family of arachidonic acid metabolites including 15(S)-HETE, 15(R)-HETE, and 15-HpETE.^[19] Several synthetic ligands have been identified that selectively bind PPARδ.

Agonists

Interactions

Peroxisome proliferator-activated receptor delta has been shown to interact with HDAC3^[21]^[22] and NCOR2.^[22]

References

↑ "Diseases that are genetically associated with PPARD view/edit references on wikidata".
↑ "Drugs that physically interact with Peroxisome proliferator-activated receptor delta view/edit references on wikidata".
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Schmidt A, Endo N, Rutledge SJ, Vogel R, Shinar D, Rodan GA (1992). "Identification of a new member of the steroid hormone receptor superfamily that is activated by a peroxisome proliferator and fatty acids". Mol. Endocrinol. 6 (10): 1634–41. doi:10.1210/me.6.10.1634. PMID 1333051.
↑ Krey G, Keller H, Mahfoudi A, Medin J, Ozato K, Dreyer C, Wahli W (1993). "Xenopus peroxisome proliferator activated receptors: genomic organization, response element recognition, heterodimer formation with retinoid X receptor and activation by fatty acids". J Steroid Biochem Mol Biol. 47 (1–6): 65–73. doi:10.1016/0960-0760(93)90058-5. PMID 8274443.
1 2 Berger J, Moller DE (2002). "The mechanisms of action of PPARs". Annu. Rev. Med. 53: 409–35. doi:10.1146/annurev.med.53.082901.104018. PMID 11818483. (subscription required (help)).
↑ Feige JN, Gelman L, Michalik L, Desvergne B, Wahli W (2006). "From molecular action to physiological outputs: peroxisome proliferator-activated receptors are nuclear receptors at the crossroads of key cellular functions". Prog. Lipid Res. 45 (2): 120–59. doi:10.1016/j.plipres.2005.12.002. PMID 16476485.
↑ Takayama O, Yamamoto H, Damdinsuren B, Sugita Y, Ngan CY, Xu X, Tsujino T, Takemasa I, Ikeda M, Sekimoto M, Matsuura N, Monden M (2006). "Expression of PPARδ in multistage carcinogenesis of the colorectum: implications of malignant cancer morphology". Br. J. Cancer. 95 (7): 889–95. doi:10.1038/sj.bjc.6603343. PMC 2360534. PMID 16969348.
↑ Lee CH, Olson P, Hevener A, Mehl I, Chong LW, Olefsky JM, Gonzalez FJ, Ham J, Kang H, Peters JM, Evans RM (2006). "PPARδ regulates glucose metabolism and insulin sensitivity". Proc. Natl. Acad. Sci. U.S.A. 103 (9): 3444–9. doi:10.1073/pnas.0511253103. PMC 1413918. PMID 16492734.
↑ "Entrez Gene: PPARD peroxisome proliferator-activated receptor delta".
↑ Schmuth M, Haqq CM, Cairns WJ, Holder JC, Dorsam S, Chang S, Lau P, Fowler AJ, Chuang G, Moser AH, Brown BE, Mao-Qiang M, Uchida Y, Schoonjans K, Auwerx J, Chambon P, Willson TM, Elias PM, Feingold KR (April 2004). "Peroxisome proliferator-activated receptor (PPAR)-beta/delta stimulates differentiation and lipid accumulation in keratinocytes". J. Invest. Dermatol. 122 (4): 971–83. doi:10.1111/j.0022-202X.2004.22412.x. PMID 15102088.
↑ Tan NS, Icre G, Montagner A, Bordier-ten-Heggeler B, Wahli W, Michalik L (October 2007). "The Nuclear Hormone Receptor Peroxisome Proliferator-Activated Receptor β/δ Potentiates Cell Chemotactism, Polarization, and Migration". Mol. Cell. Biol. 27 (20): 7161–75. doi:10.1128/MCB.00436-07. PMC 2168901. PMID 17682064.
↑ Tachibana K, Yamasaki D, Ishimoto K, Doi T (2008). "The Role of PPARs in Cancer". PPAR Res. 2008: 102737. doi:10.1155/2008/102737. PMC 2435221. PMID 18584037.
↑ Peters JM, Shah YM, Gonzalez FJ (March 2012). "The role of peroxisome proliferator-activated receptors in carcinogenesis and chemoprevention". Nat. Rev. Cancer. 12 (3): 181–95. doi:10.1038/nrc3214. PMC 3322353. PMID 22318237.
↑ Brunmair B, Staniek K, Dörig J, Szöcs Z, Stadlbauer K, Marian V, Gras F, Anderwald C, Nohl H, Waldhäusl W, Fürnsinn C (November 2006). "Activation of PPAR-δ in isolated rat skeletal muscle switches fuel preference from glucose to fatty acids". Diabetologia. 49 (11): 2713–22. doi:10.1007/s00125-006-0357-6. PMID 16960684.
↑ Girroir EE, Hollingshead HE, He P, Zhu B, Perdew GH, Peters JM (July 2008). "Quantitative expression patterns of peroxisome proliferator-activated receptor-β/δ (PPARβ/δ) protein in mice". Biochem. Biophys. Res. Commun. 371 (3): 456–61. doi:10.1016/j.bbrc.2008.04.086. PMC 2586836. PMID 18442472.
↑ Peters JM, Lee SS, Li W, Ward JM, Gavrilova O, Everett C, Reitman ML, Hudson LD, Gonzalez FJ (1993). "Growth, Adipose, Brain, and Skin Alterations Resulting from Targeted Disruption of the Mouse Peroxisome Proliferator-Activated Receptor β(δ)". Mol Cell Biol. 20 (14): 5119–28. doi:10.1128/MCB.20.14.5119-5128.2000. PMC 85961. PMID 10866668.
↑ Mol. Pharmacol. 77:171-184, 2010
↑ van der Veen JN, Kruit JK, Havinga R, Baller JF, Chimini G, Lestavel S, Staels B, Groot PH, Groen AK, Kuipers F (March 2005). "Reduced cholesterol absorption upon PPAR-δ activation coincides with decreased intestinal expression of NPC1L1". J. Lipid Res. 46 (3): 526–34. doi:10.1194/jlr.M400400-JLR200. PMID 15604518.
↑ Franco PJ, Li G, Wei LN (August 2003). "Interaction of nuclear receptor zinc finger DNA binding domains with histone deacetylase". Mol. Cell. Endocrinol. 206 (1–2): 1–12. doi:10.1016/S0303-7207(03)00254-5. PMID 12943985.
1 2 Shi Y, Hon M, Evans RM (March 2002). "The peroxisome proliferator-activated receptor δ, an integrator of transcriptional repression and nuclear receptor signaling". Proc. Natl. Acad. Sci. U.S.A. 99 (5): 2613–8. doi:10.1073/pnas.052707099. PMC 122396. PMID 11867749.

External links

PPAR delta at the US National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

PDB gallery

1gwx: MOLECULAR RECOGNITION OF FATTY ACIDS BY PEROXISOME PROLIFERATOR-ACTIVATED RECEPTORS

1y0s: Crystal structure of PPAR delta complexed with GW2331

2awh: Human Nuclear Receptor-Ligand Complex 1

2b50: Human Nuclear Receptor-Ligand Complex 2

2baw: Human Nuclear Receptor-Ligand Complex 1

2gwx: MOLECULAR RECOGNITION OF FATTY ACIDS BY PEROXISOME PROLIFERATOR-ACTIVATED RECEPTORS

2j14: 3,4,5-TRISUBSTITUTED ISOXAZOLES AS NOVEL PPARDELTA AGONISTS: PART2

3gwx: MOLECULAR RECOGNITION OF FATTY ACIDS BY PEROXISOME PROLIFERATOR-ACTIVATED RECEPTORS

Transcription factors and intracellular receptors

(1) Basic domains

(1.1) Basic leucine zipper (bZIP)	Activating transcription factor AATF 1 2 3 4 5 6 7 AP-1 c-Fos FOSB FOSL1 FOSL2 JDP2 c-Jun JUNB JunD BACH 1 2 BATF BLZF1 C/EBP α β γ δ ε ζ CREB 1 3 L1 CREM DBP DDIT3 GABPA HLF MAF B F G K NFE 2 L1 L2 L3 NFIL3 NRL NRF 1 2 3 XBP1

(1.2) Basic helix-loop-helix (bHLH)	ATOH1 AhR AHRR ARNT ASCL1 BHLH 2 3 9 ARNTL ARNTL ARNTL2 CLOCK EPAS1 FIGLA HAND 1 2 HES 5 6 HEY 1 2 L HES1 HIF 1A 3A ID 1 2 3 4 LYL1 MESP2 MXD4 MYCL1 MYCN Myogenic regulatory factors MyoD Myogenin MYF5 MYF6 Neurogenins 1 2 3 NeuroD 1 2 NPAS 1 2 3 OLIG 1 2 Pho4 Scleraxis SIM 1 2 TAL 1 2 Twist USF1

(1.3) bHLH-ZIP	AP-4 MAX MXD3 MITF MNT MLX MXI1 Myc SREBP 1 2

(1.4) NF-1	NFI A B C X SMAD R-SMAD 1 2 3 5 9 I-SMAD 6 7 4)

(1.5) RF-X	RFX 1 2 3 4 5 6 ANK

(1.6) Basic helix-span-helix (bHSH)	AP-2 α β γ δ ε

(2) Zinc finger DNA-binding domains

(2.1) Nuclear receptor (Cys₄)

subfamily 1	Thyroid hormone α β CAR FXR LXR α β PPAR α β/δ γ PXR RAR α β γ ROR α β γ Rev-ErbA α β VDR

subfamily 2	COUP-TF (I II Ear-2 HNF4 α γ PNR RXR α β γ Testicular receptor 2 4 TLX

subfamily 3	Steroid hormone Androgen Estrogen α β Glucocorticoid Mineralocorticoid Progesterone Estrogen related α β γ

subfamily 4	NUR NGFIB NOR1 NURR1

subfamily 5	LRH-1 SF1

subfamily 6	GCNF

subfamily 0	DAX1 SHP

(2.2) Other Cys₄

GATA
- 1
- 2
- 3
- 4
- 5
- 6
MTA
- 1
- 2
- 3
TRPS1

(2.3) Cys₂His₂

General transcription factors
- TFIIA
- TFIIB
- TFIID
- TFIIE
  - 1
  - 2
- TFIIF
- 1
- 2
  - TFIIH
  - 1
  - 2
  - 4
  - 2I
  - 3A
  - 3C1
  - 3C2

ATBF1
BCL
- 6
- 11A
- 11B
CTCF
E4F1
EGR
- 1
- 2
- 3
- 4
ERV3
GFI1
GLI-Krüppel family
- 1
- 2
- 3
- REST
- S1
- S2
- YY1
HIC
- 1
- 2
HIVEP
- 1
- 2
- 3
IKZF
- 1
- 2
- 3
ILF
- 2
- 3
KLF
- 1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 9
- 10
- 11
- 12
- 13
- 14
- 15
- 17
MTF1
MYT1
OSR1
PRDM9
SALL
- 1
- 2
- 3
- 4
SP
- 1
- 2
- 4
- 7
- 8
TSHZ3
WT1
Zbtb7
- 7A
- 7B
ZBTB
- 11
- 16
- 17
- 20
- 32
- 33
- 40
zinc finger
- 3
- 7
- 9
- 10
- 19
- 22
- 24
- 33B
- 34
- 35
- 41
- 43
- 44
- 51
- 74
- 143
- 146
- 148
- 165
- 202
- 217
- 219
- 238
- 239
- 259
- 267
- 268
- 281
- 295
- 300
- 318
- 330
- 346
- 350
- 365
- 366
- 384
- 423
- 451
- 452
- 471
- 593
- 638
- 644
- 649
- 655

(2.4) Cys₆

HIVEP1

(2.5) Alternating composition

AIRE
DIDO1
GRLF1
ING
- 1
- 2
- 4
JARID
- 1A
- 1B
- 1C
- 1D
- 2
JMJD1B

(2.6) WRKY

WRKY

(3) Helix-turn-helix domains

(3.1) Homeodomain	ARX CDX 1 2 CRX CUTL1 DBX 1 2 DLX 3 4 5 EMX 1 2 EN 1 2 FHL 1 2 3 HESX1 HHEX HLX Homeobox A1 A2 A3 A4 A5 A7 A9 A10 A11 A13 B1 B2 B3 B4 B5 B6 B7 B8 B9 B13 C4 C5 C6 C8 C9 C10 C11 C12 C13 D1 D3 D4 D8 D9 D10 D11 D12 D13 HOPX IRX 1 2 3 4 5 6 MKX LMX 1A 1B MEIS 1 2 MEOX2 MNX1 MSX 1 2 NANOG NKX 2-1 2-2 2-3 2-5 3-1 3-2 6-1 6-2 NOBOX PBX 1 2 3 PHF 1 3 6 8 10 16 17 20 21A PHOX 2A 2B PITX 1 2 3 POU domain PIT-1 BRN-3: A B C Octamer transcription factor: 1 2 3/4 6 7 11 OTX 1 2 PDX1 SATB2 SHOX2 SIX 1 2 3 4 5 VAX1 ZEB 1 2

(3.2) Paired box	PAX 1 2 3 4 5 6 7 8 9 PRRX 1 2 RAX

(3.3) Fork head / winged helix	E2F 1 2 3 4 5 FOX proteins A1 A2 A3 C1 C2 D3 D4 E1 E3 F1 G1 H1 I1 J1 J2 K1 K2 L2 M1 N1 N3 O1 O3 O4 P1 P2 P3 P4

(3.4) Heat shock factors	HSF 1 2 4

(3.5) Tryptophan clusters	ELF 2 4 5 EGF ELK 1 3 4 ERF ETS 1 2 ERG SPIB ETV 1 4 5 6 FLI1 Interferon regulatory factors 1 2 3 4 5 6 7 8 MYB MYBL2

(3.6) TEA domain	transcriptional enhancer factor 1 2 3 4

(4) β-Scaffold factors with minor groove contacts

(4.1) Rel homology region	NF-κB NFKB1 NFKB2 REL RELA RELB NFAT C1 C2 C3 C4 5

(4.2) STAT	STAT 1 2 3 4 5 6

(4.3) p53	p53 TBX 1 2 3 5 19 21 22 TBR1 TBR2 TFT MYRF TP63

(4.4) MADS box	Mef2 A B C D SRF

(4.6) TATA-binding proteins	TBP TBPL1

(4.7) High-mobility group	BBX HMGB 1 2 3 4 HMGN 1 2 3 4 HNF 1A 1B LEF1 SOX 1 2 3 4 5 6 8 9 10 11 12 13 14 15 18 21 SRY SSRP1 TCF 3 4 TOX 1 2 3 4

(4.9) Grainyhead	TFCP2

(4.10) Cold-shock domain	CSDA YBX1

(4.11) Runt	CBF CBFA2T2 CBFA2T3 RUNX1 RUNX2 RUNX3 RUNX1T1

(0) Other transcription factors

(0.2) HMGI(Y)	HMGA 1 2 HBP1

(0.3) Pocket domain	Rb RBL1 RBL2

(0.5) AP-2/EREBP-related factors	Apetala 2 EREBP B3

(0.6) Miscellaneous	ARID 1A 1B 2 3A 3B 4A CAP IFI 16 35 MLL 2 3 T1 MNDA NFY A B C Rho/Sigma

see also transcription factor/coregulator deficiencies

Nuclear receptor modulators

CAR

Agonists	6,7-Dimethylesculetin Amiodarone Artemisinin Benfuracarb Carbamazepine Carvedilol Chlorpromazine Chrysin CITCO Clotrimazole Cyclophosphamide Cypermethrin DHEA Efavirenz Ellagic acid Griseofulvin Methoxychlor Mifepristone Nefazodone Nevirapine Nicardipine Octicizer Permethrin Phenobarbital Phenytoin Pregnanedione (5β-dihydroprogesterone) Reserpine TCPOBOP Telmisartan Tolnaftate Troglitazone Valproic acid

Antagonists	3,17β-Estradiol 3α-Androstanol 3α-Androstenol 3β-Androstanol 17-Androstanol AITC Ethinyl estradiol Meclizine Nigramide J Okadaic acid PK-11195 S-07662 T-0901317

ERR

ERRα

Agonists	6,3′,4′-Trihydroxyflavone Biochanin A Cholesterol Daidzein Genistein

Antagonists	Diethylstilbestrol XCT-790

ERRβ

Agonists	DY-131 (GSK-9089) GSK-4716 (GW-4716)

Antagonists	4-Hydroxytamoxifen (afimoxifene) Diethylstilbestrol

ERRγ

Agonists	Bisphenol A DY-131 (GSK-9089) GSK-4716 (GW-4716)

Antagonists	4-Hydroxytamoxifen (afimoxifene) Diethylstilbestrol

FXR

Agonists	Bile acids Cafestol Chenodeoxycholic acid Fexaramine GW-4064 Obeticholic acid

Antagonists	Guggulsterone

LXR

Agonists	22R-Hydroxycholesterol 24S-Hydroxycholesterol 27-Hydroxycholesterol Cholestenoic acid DMHCA GW-3965 Hypocholamide T-0901317

Antagonists	Efavirenz

PPAR

PPARα

Agonists	15-HETE 15-HpETE Aleglitazar Aluminium clofibrate Arachidonic acid Bezafibrate Clofibrate CP-775146 Daidzein DHEA Elafibranor Etomoxir Fenofibrate Genistein Gemfibrozil GW-7647 Leukotriene B₄ LG-101506 LG-100754 Lobeglitazone Muraglitazar Oleylethanolamide Palmitoylethanolamide Pemafibrate Perfluorononanoic acid Perfluorooctanoic acid Pioglitazone Saroglitazar Sodelglitazar Tesaglitazar Tetradecylthioacetic acid Troglitazone WY-14643

Antagonists	GW-6471 MK-886

PPARδ

Agonists	15-HETE 15-HpETE Arachidonic acid Bezafibrate Daidzein Elafibranor Fonadelpar Genistein GW-0742 GW-501516 L-165,041 LG-101506 MBX-8025 Sodelglitazar Tetradecylthioacetic acid

Antagonists	FH-535 GSK-0660 GSK-3787

PPARγ

Agonists	5-Oxo-ETE 5-Oxo-15-hydroxy-ETE 15-Deoxy-Δ^12,14-prostaglandin J₂ 15-HETE 15-HpETE Aleglitazar Arachidonic acid Balaglitazone Berberine Bezafibrate Cevoglitazar Ciglitazone Daidzein Darglitazone Edaglitazone Efatutazone Englitazone Etalocib Farglitazar Genistein GW-1929 Ibuprofen Imiglitazar Indeglitazar LG-100268 LG-100754 LG-101506 Lobeglitazone Muraglitazar (muroglitazar) nTZDpa Naveglitazar Netoglitazone Oxeglitazar Peliglitazar Pemaglitazar Perfluorononanoic acid Pioglitazone Prostaglandin J₂ Ragaglitazar Reglitazar Rivoglitazone Rosiglitazone RS5444 Saroglitazar Sipoglitazar Sodelglitazar Telmisartan Tesaglitazar Troglitazone

SPPARMs	BADGE EPI-001 INT-131 MK-0533 S26948

Antagonists	FH-535 GW-9662 SR-202 T-0070907

Unknown	SR-1664

Unselective

Agonists	Ciprofibrate Clinofibrate Clofibride Englitazone Etofibrate Farglitazar Netoglitazone Ronifibrate Rivoglitazone Simfibrate

Unsorted

Agonists	Seladelpar

PXR

Agonists	17α-Hydroxypregnenolone 17α-Hydroxyprogesterone Δ⁴-Androstenedione Δ⁵-Androstenediol Δ⁵-Androstenedione AA-861 Allopregnanediol Allopregnanedione (5α-dihydroprogesterone) Allopregnanolone Alpha-Lipoic acid Ambrisentan AMI-193 Amlodipine besylate Antimycotics Artemisinin Aurothioglucose Bile acids Bithionol Bosentan Bumecaine Cafestol Cephaloridine Cephradine Chlorpromazine Ciglitazone Clindamycin Clofenvinfos Chloroxine Clotrimazole Colforsin Corticosterone Cyclophosphamide Cyproterone acetate Demecolcine Dexamethasone DHEA DHEA-S Dibunate sodium Diclazuril Dicloxacillin Dimercaprol Dinaline Docetaxel Docusate calcium Dodecylbenzenesulfonic acid Dronabinol Droxidopa Eburnamonine Ecopipam Enzacamene Epothilone B Erythromycin Famprofazone Febantel Felodipine Fenbendazole Fentanyl Flucloxacillin Fluorometholone Griseofulvin Guggulsterone Haloprogin Hetacillin potassium Hyperforin Hypericum perforatum (St John's wort) Indinavir sulfate Lasalocid sodium Levothyroxine Linolenic acid LOE-908 Loratadine Lovastatin Meclizine Methacycline Methylprednisolone Metyrapone Mevastatin Mifepristone Nafcillin Nicardipine Nicotine Nifedipine Nilvadipine Nisoldipine Norelgestromin Omeprazole Orlistat Oxatomide Paclitaxel Phenobarbital Piperine Plicamycin Prednisolone Pregnanediol Pregnanedione (5β-dihydroprogesterone) Pregnanolone Pregnenolone Pregnenolone 16α-carbonitrile Proadifen Progesterone Quingestrone Reserpine Reverse triiodothyronine Rifampicin Rifaximin Rimexolone Riodipine Ritonavir Simvastatin Sirolimus Spironolactone Spiroxatrine SR-12813 Suberoylanilide Sulfisoxazole Suramin Tacrolimus Tenylidone Terconazole Testosterone isocaproate Tetracycline Thiamylal sodium Thiothixene Thonzonium bromide Tianeptine Troglitazone Troleandomycin Tropanyl 3,5-dimethulbenzoate Zafirlukast Zearalanol

Antagonists	Ketoconazole Sesamin

RAR

Agonists	9CDHRA 9-cis-Retinoic acid (alitretinoin) AC-261066 AC-55649 Acitretin Adapalene all-trans-Retinoic acid (tretinoin) AM-580 BMS-493 BMS-753 BMS-961 CD-1530 CD-2314 CD-437 Ch-55 EC 23 Etretinate Fenretinide Isotretinoin Palovarotene Retinoic acid Retinol (vitamin A) Tamibarotene Tazarotene Tazarotenic acid TTNPB

Antagonists	BMS-195614 BMS-493 CD-2665 ER-50891 LE-135 MM-11253

Others	Retinoic acid metabolism inhibitors: Liarozole

RXR

Agonists	9CDHRA 9-cis-Retinoic acid (alitretinoin) all-trans-Retinoic acid (tretinoin) Bexarotene CD 3254 Docosahexaenoic acid Fluorobexarotene Isotretinoin LG-100268 LG-101506 LG-100754 Retinoic acid Retinol (vitamin A) SR-11237

Antagonists	HX-531 HX-630 LG-100754 PA-452 UVI-3003

SHR

See here instead.

VDR

Agonists	7-Dehydrocholesterol 22-Oxacalcitriol 25-Hydroxyergocalciferol Alfacalcidol Calcifediol Calciferol Calcipotriol Calcitriol Cholecalciferol (vitamin D₃) Dihydrotachysterol Doxercalciferol EB-1089 Eldecalcitol Ercalcidiol Ercalcitriol Ergocalciferol (vitamin D₂) Lithocholic acid Paricalcitol Tacalcitol

Agonists	Dextrothyroxine DITPA Eprotirome (KB-2115) KB-2611 KB-130015 Levothyroxine Liothyronine MB-07811 MGL-3196 (VIA-3196) Sobetirome (GC-1, GRX-431) Thyroxine Tiratricol Triiodothyronine VK-0214 VK-2809 ZYT1

Others	Carrier proteins: Albumin Thyroxine-binding globulin Transthyretin

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