WordNet

first in order of importance; "the alpha male in the group of chimpanzees"; "the alpha star in a constellation is the brightest or main star"
the 1st letter of the Greek alphabet
the beginning of a series or sequence; "the Alpha and Omega, the first and the last, the beginning and the end"--Revelations
early testing stage of a software or hardware product; "alpha version"
a cellular structure that is postulated to exist in order to mediate between a chemical agent that acts on nervous tissue and the physiological response
the 24th letter of the Roman alphabet (同)x, ex
any high mountain

PrepTutorEJDIC

アルファ(ギリシア語アルファベットの第1字A,α;英語のA,aに相当) / アルファ星(星座の主星)
=sense organ / 受信装置
Christ / Christian
高山,高峰
x-axis

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/05/26 22:56:14」(JST)

wiki en

Retinoid X receptor alpha (RXR-alpha), also known as NR2B1 (nuclear receptor subfamily 2, group B, member 1) is a nuclear receptor that in humans is encoded by the RXRA gene.^[1]

Function

Retinoid X receptors (RXRs) and retinoic acid receptors (RARs), are nuclear receptors that mediate the biological effects of retinoids by their involvement in retinoic acid-mediated gene activation. These receptors exert their action by binding, as homodimers or heterodimers, to specific sequences in the promoters of target genes and regulating their transcription. The protein encoded by this gene is a member of the steroid and thyroid hormone receptor superfamily of transcription factors.^[2] In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone deacetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the cytochrome P450 system genes.^[3]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. ^{[§ 1]}

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|{{{bSize}}}px|alt=Vitamin D Synthesis Pathway edit]]

File:VitaminDSynthesis WP1531.png

Vitamin D Synthesis Pathway edit

^ The interactive pathway map can be edited at WikiPathways: "VitaminDSynthesis_WP1531".

Interactions

Retinoid X receptor alpha has been shown to interact with:

BCL3,^[4]
BRD8,^[5]
CLOCK,^[6]
FXR^[7]
IGFBP3,^[8]
ITGB3BP,^[9]
LXR-β,^[7]
MyoD,^[10]
NCOA6,^[11]^[12]^[13]^[14]
NFKBIB,^[15]
NPAS2,^[6]
NRIP1,^[16]^[17]
NR4A1,^[18]
NCOA2,^[19]
NCOA3,^[20]
POU2F1,^[21]^[22]
PPARGC1A,^[23]
PPAR-γ,^[24]^[25]^[26]
RNF8,^[27]
RAR-α,^[28]^[29]
SHP,^[30]^[31]
TADA3L,^[32]
TBP,^[33]
TRIM24,^[34]^[35]
TR-β,^[36]^[37] and
VDR.^[19]^[38]

References

^ Mangelsdorf DJ, Ong ES, Dyck JA, Evans RM (May 1990). "Nuclear receptor that identifies a novel retinoic acid response pathway". Nature 345 (6272): 224–9. Bibcode:1990Natur.345..224M. doi:10.1038/345224a0. PMID 2159111.
^ "Entrez Gene: RXRA retinoid X receptor, alpha".
^ "Retinoic acid receptor RXR-alpha - Homo sapiens (Human)". UniProt.
^ Na SY, Choi HS, Kim JW, Na DS, Lee JW (1998). "Bcl3, an IkappaB protein, as a novel transcription coactivator of the retinoid X receptor". J. Biol. Chem. 273 (47): 30933–8. doi:10.1074/jbc.273.47.30933. PMID 9812988.
^ Monden T, Kishi M, Hosoya T, Satoh T, Wondisford FE, Hollenberg AN, Yamada M, Mori M (1999). "p120 acts as a specific coactivator for 9-cis-retinoic acid receptor (RXR) on peroxisome proliferator-activated receptor-gamma/RXR heterodimers". Mol. Endocrinol. 13 (10): 1695–703. doi:10.1210/me.13.10.1695. PMID 10517671.
^ ^a ^b McNamara P, Seo SB, Rudic RD, Sehgal A, Chakravarti D, FitzGerald GA (2001). "Regulation of CLOCK and MOP4 by nuclear hormone receptors in the vasculature: a humoral mechanism to reset a peripheral clock". Cell 105 (7): 877–89. doi:10.1016/S0092-8674(01)00401-9. PMID 11439184.
^ ^a ^b Seol W, Choi HS, Moore DD (1995). "Isolation of proteins that interact specifically with the retinoid X receptor: two novel orphan receptors". Mol. Endocrinol. 9 (1): 72–85. doi:10.1210/mend.9.1.7760852. PMID 7760852.
^ Liu B, Lee HY, Weinzimer SA, Powell DR, Clifford JL, Kurie JM, Cohen P (2000). "Direct functional interactions between insulin-like growth factor-binding protein-3 and retinoid X receptor-alpha regulate transcriptional signaling and apoptosis". J. Biol. Chem. 275 (43): 33607–13. doi:10.1074/jbc.M002547200. PMID 10874028.
^ Li D, Desai-Yajnik V, Lo E, Schapira M, Abagyan R, Samuels HH (1999). "NRIF3 is a novel coactivator mediating functional specificity of nuclear hormone receptors". Mol. Cell. Biol. 19 (10): 7191–202. PMC 84712. PMID 10490654.
^ Froeschlé A, Alric S, Kitzmann M, Carnac G, Auradé F, Rochette-Egly C, Bonnieu A (1998). "Retinoic acid receptors and muscle b-HLH proteins: partners in retinoid-induced myogenesis". Oncogene 16 (26): 3369–78. doi:10.1038/sj.onc.1201894. PMID 9692544.
^ Lee SK, Anzick SL, Choi JE, Bubendorf L, Guan XY, Jung YK, Kallioniemi OP, Kononen J, Trent JM, Azorsa D, Jhun BH, Cheong JH, Lee YC, Meltzer PS, Lee JW (1999). "A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo". J. Biol. Chem. 274 (48): 34283–93. doi:10.1074/jbc.274.48.34283. PMID 10567404.
^ Lee SK, Jung SY, Kim YS, Na SY, Lee YC, Lee JW (2001). "Two distinct nuclear receptor-interaction domains and CREB-binding protein-dependent transactivation function of activating signal cointegrator-2". Mol. Endocrinol. 15 (2): 241–54. doi:10.1210/me.15.2.241. PMID 11158331.
^ Kong HJ, Park MJ, Hong S, Yu HJ, Lee YC, Choi YH, Cheong J (2003). "Hepatitis B virus X protein regulates transactivation activity and protein stability of the cancer-amplified transcription coactivator ASC-2". Hepatology 38 (5): 1258–66. doi:10.1053/jhep.2003.50451. PMID 14578865.
^ Ko L, Cardona GR, Iwasaki T, Bramlett KS, Burris TP, Chin WW (2002). "Ser-884 adjacent to the LXXLL motif of coactivator TRBP defines selectivity for ERs and TRs". Mol. Endocrinol. 16 (1): 128–40. doi:10.1210/mend.16.1.0755. PMID 11773444.
^ Na SY, Kim HJ, Lee SK, Choi HS, Na DS, Lee MO, Chung M, Moore DD, Lee JW (1998). "IkappaBbeta interacts with the retinoid X receptor and inhibits retinoid-dependent transactivation in lipopolysaccharide-treated cells". J. Biol. Chem. 273 (6): 3212–5. doi:10.1074/jbc.273.6.3212. PMID 9452433.
^ Farooqui M, Franco PJ, Thompson J, Kagechika H, Chandraratna RA, Banaszak L, Wei LN (2003). "Effects of retinoid ligands on RIP140: molecular interaction with retinoid receptors and biological activity". Biochemistry 42 (4): 971–9. doi:10.1021/bi020497k. PMID 12549917.
^ L'Horset F, Dauvois S, Heery DM, Cavaillès V, Parker MG (1996). "RIP-140 interacts with multiple nuclear receptors by means of two distinct sites". Mol. Cell. Biol. 16 (11): 6029–36. PMC 231605. PMID 8887632.
^ Lin B, Kolluri SK, Lin F, Liu W, Han YH, Cao X, Dawson MI, Reed JC, Zhang XK (2004). "Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3". Cell 116 (4): 527–40. doi:10.1016/S0092-8674(04)00162-X. PMID 14980220.
^ ^a ^b Zhang C, Baudino TA, Dowd DR, Tokumaru H, Wang W, MacDonald PN (2001). "Ternary complexes and cooperative interplay between NCoA-62/Ski-interacting protein and steroid receptor coactivators in vitamin D receptor-mediated transcription". J. Biol. Chem. 276 (44): 40614–20. doi:10.1074/jbc.M106263200. PMID 11514567.
^ Chen H, Lin RJ, Schiltz RL, Chakravarti D, Nash A, Nagy L, Privalsky ML, Nakatani Y, Evans RM (1997). "Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300". Cell 90 (3): 569–80. doi:10.1016/S0092-8674(00)80516-4. PMID 9267036.
^ Préfontaine GG, Walther R, Giffin W, Lemieux ME, Pope L, Haché RJ (1999). "Selective binding of steroid hormone receptors to octamer transcription factors determines transcriptional synergism at the mouse mammary tumor virus promoter". J. Biol. Chem. 274 (38): 26713–9. doi:10.1074/jbc.274.38.26713. PMID 10480874.
^ Kakizawa T, Miyamoto T, Ichikawa K, Kaneko A, Suzuki S, Hara M, Nagasawa T, Takeda T, Mori Ji, Kumagai M, Hashizume K (1999). "Functional interaction between Oct-1 and retinoid X receptor". J. Biol. Chem. 274 (27): 19103–8. doi:10.1074/jbc.274.27.19103. PMID 10383413.
^ Delerive P, Wu Y, Burris TP, Chin WW, Suen CS (2002). "PGC-1 functions as a transcriptional coactivator for the retinoid X receptors". J. Biol. Chem. 277 (6): 3913–7. doi:10.1074/jbc.M109409200. PMID 11714715.
^ Tontonoz P, Graves RA, Budavari AI, Erdjument-Bromage H, Lui M, Hu E, Tempst P, Spiegelman BM (1994). "Adipocyte-specific transcription factor ARF6 is a heterodimeric complex of two nuclear hormone receptors, PPAR gamma and RXR alpha". Nucleic Acids Res. 22 (25): 5628–34. doi:10.1093/nar/22.25.5628. PMC 310126. PMID 7838715.
^ Berger J, Patel HV, Woods J, Hayes NS, Parent SA, Clemas J, Leibowitz MD, Elbrecht A, Rachubinski RA, Capone JP, Moller DE (2000). "A PPARgamma mutant serves as a dominant negative inhibitor of PPAR signaling and is localized in the nucleus". Mol. Cell. Endocrinol. 162 (1-2): 57–67. doi:10.1016/S0303-7207(00)00211-2. PMID 10854698.
^ Gampe RT, Montana VG, Lambert MH, Miller AB, Bledsoe RK, Milburn MV, Kliewer SA, Willson TM, Xu HE (2000). "Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the molecular basis of heterodimerization among nuclear receptors". Mol. Cell 5 (3): 545–55. doi:10.1016/S1097-2765(00)80448-7. PMID 10882139.
^ Takano Y, Adachi S, Okuno M, Muto Y, Yoshioka T, Matsushima-Nishiwaki R, Tsurumi H, Ito K, Friedman SL, Moriwaki H, Kojima S, Okano Y (2004). "The RING finger protein, RNF8, interacts with retinoid X receptor alpha and enhances its transcription-stimulating activity". J. Biol. Chem. 279 (18): 18926–34. doi:10.1074/jbc.M309148200. PMID 14981089.
^ Benkoussa M, Brand C, Delmotte MH, Formstecher P, Lefebvre P (2002). "Retinoic acid receptors inhibit AP1 activation by regulating extracellular signal-regulated kinase and CBP recruitment to an AP1-responsive promoter". Mol. Cell. Biol. 22 (13): 4522–34. doi:10.1128/MCB.22.13.4522-4534.2002. PMC 133906. PMID 12052862.
^ Bugge TH, Pohl J, Lonnoy O, Stunnenberg HG (1992). "RXR alpha, a promiscuous partner of retinoic acid and thyroid hormone receptors". EMBO J. 11 (4): 1409–18. PMC 556590. PMID 1314167.
^ Lee YK, Dell H, Dowhan DH, Hadzopoulou-Cladaras M, Moore DD (2000). "The orphan nuclear receptor SHP inhibits hepatocyte nuclear factor 4 and retinoid X receptor transactivation: two mechanisms for repression". Mol. Cell. Biol. 20 (1): 187–95. doi:10.1128/MCB.20.1.187-195.2000. PMC 85074. PMID 10594021.
^ Brendel C, Schoonjans K, Botrugno OA, Treuter E, Auwerx J (2002). "The small heterodimer partner interacts with the liver X receptor alpha and represses its transcriptional activity". Mol. Endocrinol. 16 (9): 2065–76. doi:10.1210/me.2001-0194. PMID 12198243.
^ Zeng M, Kumar A, Meng G, Gao Q, Dimri G, Wazer D, Band H, Band V (2002). "Human papilloma virus 16 E6 oncoprotein inhibits retinoic X receptor-mediated transactivation by targeting human ADA3 coactivator". J. Biol. Chem. 277 (47): 45611–8. doi:10.1074/jbc.M208447200. PMID 12235159.
^ Schulman IG, Chakravarti D, Juguilon H, Romo A, Evans RM (1995). "Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation". Proc. Natl. Acad. Sci. U.S.A. 92 (18): 8288–92. Bibcode:1995PNAS...92.8288S. doi:10.1073/pnas.92.18.8288. PMC 41142. PMID 7667283.
^ Thénot S, Henriquet C, Rochefort H, Cavaillès V (1997). "Differential interaction of nuclear receptors with the putative human transcriptional coactivator hTIF1". J. Biol. Chem. 272 (18): 12062–8. doi:10.1074/jbc.272.18.12062. PMID 9115274.
^ Lee WY, Noy N (2002). "Interactions of RXR with coactivators are differentially mediated by helix 11 of the receptor's ligand binding domain". Biochemistry 41 (8): 2500–8. doi:10.1021/bi011764. PMID 11851396.
^ Monden T, Wondisford FE, Hollenberg AN (1997). "Isolation and characterization of a novel ligand-dependent thyroid hormone receptor-coactivating protein". J. Biol. Chem. 272 (47): 29834–41. doi:10.1074/jbc.272.47.29834. PMID 9368056.
^ Jeyakumar M, Tanen MR, Bagchi MK (1997). "Analysis of the functional role of steroid receptor coactivator-1 in ligand-induced transactivation by thyroid hormone receptor". Mol. Endocrinol. 11 (6): 755–67. doi:10.1210/mend.11.6.0003. PMID 9171239.
^ Baudino TA, Kraichely DM, Jefcoat SC, Winchester SK, Partridge NC, MacDonald PN (1998). "Isolation and characterization of a novel coactivator protein, NCoA-62, involved in vitamin D-mediated transcription". J. Biol. Chem. 273 (26): 16434–41. doi:10.1074/jbc.273.26.16434. PMID 9632709.

External links

FactorBook RXRA

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

UpToDate Contents

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English Journal

Epigallocatechin gallate inhibits hepatitis B virus via farnesoid X receptor alpha.

Xu J1, Gu W2, Li C2, Li X2, Xing G2, Li Y2, Song Y3, Zheng W2.
Journal of natural medicines.J Nat Med.2016 Mar 11. [Epub ahead of print]
Plants possess various natural antiviral properties. Epigallocatechin-3-gallate (EGCG), a major component of green tea, inhibits a variety of viruses. However, the clinical application of EGCG is currently hindered by a scarcity of information on its molecular mechanism of action. In the present stu
PMID 26968537

Solution behavior of the intrinsically disordered N-terminal domain of the Retinoid X Receptor alpha in the context of full-length protein.

Belorusova AY, Osz J, Petoukhov M, Peluso-Iltis C, Kieffer B, Svergun DI, Rochel N.
Biochemistry.Biochemistry.2016 Mar 3. [Epub ahead of print]
Retinoid X receptors (RXRs) are transcription factors with important functions in embryonic development, metabolic processes, differentiation and apoptosis. A particular feature of RXRs is their ability to act as obligatory heterodimerisation partners of class II nuclear receptors. At the same time,
PMID 26937780

IL-1β induced RXRα overexpression through activation of NF-κB signaling in gastric carcinoma.

Ren HY1, Huang GL2, Liu WM3, Zhang W4, Liu Y1, Su GQ1, Shen DY5.
Biomedicine & pharmacotherapy = Biomédecine & pharmacothérapie.Biomed Pharmacother.2016 Mar;78:329-34. doi: 10.1016/j.biopha.2016.01.033. Epub 2016 Feb 8.
BACKGROUND: Abnormal expression of Retinoid X Receptor α (RXRα) seems to be a frequent incident in a variety of cancers. However, the expression pattern and the mechanisms in gastric carcinoma (GC) remain unclear.METHODS: In GC tissues and cell lines, the expression levels of RXRα mRNA and protei
PMID 26898458

Japanese Journal

肝臓星細胞によるビタミンAの代謝・貯蔵メカニズムとその意義(若手シンポジウム「ビタミン基礎研究の進展を担う若手研究者たち」,<特集>ビタミン基礎研究の進展を担う若手研究者たち(第64回大会若手シンポジウム))

目崎喜弘
ビタミン 87(1), 33-37, 2013-01-25
… Here we present a hypothesis that an increased retinoid signaling in activated HSCs makes a feedback loop toward vitamin A restoration. … The hypothesis is based on our previous finding that HSCs acquire retinoid responsiveness after activation in vitro by post-transcriptional up regulation of retinoic acid receptor alpha gene expression …
NAID 110009578810

Effects of Time Culture and Prototypical Cytochrome P450 3A (CYP3A) Inducers on CYP2B22, CYP2C, CYP3A and Nuclear Receptor (NR) mRNAs in Long-term Cryopreserved Pig Hepatocytes (CPHs)

Giantin Mery,Zancanella Vanessa,Lopparelli Rosa Maria,Granato Anna,Carletti Monica,Vilei Maria Teresa,Muraca Maurizio,Baratto Chiara,Dacasto Mauro
Drug Metabolism and Pharmacokinetics 27(5), 495-505, 2012
… In the time-course study, a crush and rise effect was observed for pregnane X receptor (NR1I2) and constitutive androstane receptor (NR1I3) mRNAs, while a time-dependent increase of retinoid X receptor alpha (NR2B1) was noticed. …
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1.ALPHA.,25-dihydroxyvitamin D3 Rapidly Modulates Ca2+ Influx in Osteoblasts Mediated by Ca2+ Channels

Uchida Yushi,Endoh Takayuki,Shibukawa Yoshiyuki,Tazaki Masakazu,Sueishi Kenji
The Bulletin of Tokyo Dental College 51(4), 221-226, 2010
… The actions of VD are mediated through the vitamin D receptor (VDR). … Liganded VDR heterodimerizes with the retinoid X receptor and interacts with a vitamin D response element (VDRE). …
NAID 130004471704

「レチノイドX受容体α」

retinoid X receptor, alpha
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1BY4, 1DSZ, 1FBY, 1FM6, 1FM9, 1G1U, 1G5Y, 1K74, 1LBD, 1MV9, 1MVC, 1MZN, 1R0N, 1RDT, 1RXR, 1XLS, 1XV9, 1XVP, 1YNW, 2ACL, 2NLL, 2P1T, 2P1U, 2P1V, 2ZXZ, 2ZY0, 3DZU, 3DZY, 3E00, 3E94, 3FAL, 3FC6, 3FUG, 3H0A, 3KWY, 3NSP, 3NSQ, 3OAP, 3OZJ, 3PCU, 3R29, 3R2A, 3R5M, 3UVV, 4CN2, 4CN3, 4CN5, 4CN7, 4J5W, 4J5X, 4K4J, 4K6I, 4M8E, 4M8H, 4N5G, 4N8R, 4NQA, 4OC7, 4POH, 4POJ, 4PP3, 4PP5, 4RFW, 4RMC, 4RMD, 4RME, 4ZO1, 5EC9
Identifiers
Aliases	RXRA, NR2B1, Retinoid X receptor alpha
External IDs	MGI: 98214 HomoloGene: 2220 GeneCards: 6256
Gene ontology
Molecular function	• DNA binding; • sequence-specific DNA binding; • RNA polymerase II regulatory region sequence-specific DNA binding; • protein domain specific binding; • transcription factor activity, sequence-specific DNA binding; • protein complex binding; • vitamin D response element binding; • transcription coactivator activity; • transcription factor binding; • retinoic acid-responsive element binding; • zinc ion binding; • metal ion binding; • steroid hormone receptor activity; • RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding; • protein binding; • retinoic acid receptor binding; • protein heterodimerization activity; • enzyme binding; • transcription regulatory region DNA binding; • double-stranded DNA binding; • chromatin DNA binding; • retinoic acid receptor activity; • vitamin D receptor binding; • 9-cis retinoic acid receptor activity;
Cellular component	• receptor complex; • nucleoplasm; • axon; • RNA polymerase II transcription factor complex; • nuclear chromatin; • cell nucleus;
Biological process	• steroid hormone mediated signaling pathway; • regulation of branching involved in prostate gland morphogenesis; • response to selenium ion; • regulation of transcription, DNA-templated; • response to vitamin D; • response to organic cyclic compound; • response to retinoic acid; • gene expression; • cellular lipid metabolic process; • response to nutrient; • axon regeneration; • placenta development; • peroxisome proliferator activated receptor signaling pathway; • regulation of transcription from RNA polymerase II promoter; • bile acid metabolic process; • female pregnancy; • ageing; • response to glucocorticoid; • cholesterol metabolic process; • in utero embryonic development; • negative regulation of transcription from RNA polymerase II promoter; • cardiac muscle cell proliferation; • secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development; • transcription, DNA-templated; • positive regulation of transcription, DNA-templated; • ventricular cardiac muscle tissue morphogenesis; • response to vitamin A; • heart development; • retinoic acid receptor signaling pathway; • maternal placenta development; • regulation of myelination; • modulation by virus of host morphology or physiology; • vitamin metabolic process; • small molecule metabolic process; • bile acid and bile salt transport; • cellular response to insulin stimulus; • positive regulation of apoptotic process; • ventricular cardiac muscle cell differentiation; • liver development; • camera-type eye development; • response to ethanol; • inflammatory response; • viral process; • protein homotetramerization; • transcription initiation from RNA polymerase II promoter; • embryo implantation; • positive regulation of translational initiation by iron; • positive regulation of transcription from RNA polymerase II promoter; • positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; • midgut development; • negative regulation of cell proliferation;
	Sources:Amigo / QuickGO
RNA expression pattern
	; ;
	More reference expression data
Orthologs
	6256
	20181
	ENSG00000186350
	ENSMUSG00000015846
	P19793
	P28700
	NM_002957; NM_001291920; NM_001291921
	NM_001290481; NM_001290482; NM_011305
	NP_001278850.1; NP_002948.1
	NP_035435.1
	Wikidata
View/Edit Human	View/Edit Mouse

　　[★]

英: retinoid X receptor alpha

「alpha」

　　[★]

α、アルファ

関: alfa

「X」

　　[★] キサントシン, xanthosine 　　

[WikiPathways-4] The interactive pathway map can be edited at WikiPathways: "VitaminDSynthesis_WP1531".

[pmid2159111-1] Mangelsdorf DJ, Ong ES, Dyck JA, Evans RM (May 1990). "Nuclear receptor that identifies a novel retinoic acid response pathway". Nature 345 (6272): 224–9. Bibcode:1990Natur.345..224M. doi:10.1038/345224a0. PMID 2159111.

[entrez-2] "Entrez Gene: RXRA retinoid X receptor, alpha".

[urlRetinoic_acid_receptor_RXR-alpha_-_Homo_sapiens_.28Human.29-3] "Retinoic acid receptor RXR-alpha - Homo sapiens (Human)". UniProt.

[pmid9812988-5] Na SY, Choi HS, Kim JW, Na DS, Lee JW (1998). "Bcl3, an IkappaB protein, as a novel transcription coactivator of the retinoid X receptor". J. Biol. Chem. 273 (47): 30933–8. doi:10.1074/jbc.273.47.30933. PMID 9812988.

[pmid10517671-6] Monden T, Kishi M, Hosoya T, Satoh T, Wondisford FE, Hollenberg AN, Yamada M, Mori M (1999). "p120 acts as a specific coactivator for 9-cis-retinoic acid receptor (RXR) on peroxisome proliferator-activated receptor-gamma/RXR heterodimers". Mol. Endocrinol. 13 (10): 1695–703. doi:10.1210/me.13.10.1695. PMID 10517671.

[pmid11439184-7] McNamara P, Seo SB, Rudic RD, Sehgal A, Chakravarti D, FitzGerald GA (2001). "Regulation of CLOCK and MOP4 by nuclear hormone receptors in the vasculature: a humoral mechanism to reset a peripheral clock". Cell 105 (7): 877–89. doi:10.1016/S0092-8674(01)00401-9. PMID 11439184.

[pmid7760852-8] Seol W, Choi HS, Moore DD (1995). "Isolation of proteins that interact specifically with the retinoid X receptor: two novel orphan receptors". Mol. Endocrinol. 9 (1): 72–85. doi:10.1210/mend.9.1.7760852. PMID 7760852.

[pmid10874028-9] Liu B, Lee HY, Weinzimer SA, Powell DR, Clifford JL, Kurie JM, Cohen P (2000). "Direct functional interactions between insulin-like growth factor-binding protein-3 and retinoid X receptor-alpha regulate transcriptional signaling and apoptosis". J. Biol. Chem. 275 (43): 33607–13. doi:10.1074/jbc.M002547200. PMID 10874028.

[pmid10490654-10] Li D, Desai-Yajnik V, Lo E, Schapira M, Abagyan R, Samuels HH (1999). "NRIF3 is a novel coactivator mediating functional specificity of nuclear hormone receptors". Mol. Cell. Biol. 19 (10): 7191–202. PMC 84712. PMID 10490654.

[pmid9692544-11] Froeschlé A, Alric S, Kitzmann M, Carnac G, Auradé F, Rochette-Egly C, Bonnieu A (1998). "Retinoic acid receptors and muscle b-HLH proteins: partners in retinoid-induced myogenesis". Oncogene 16 (26): 3369–78. doi:10.1038/sj.onc.1201894. PMID 9692544.

[pmid10567404-12] Lee SK, Anzick SL, Choi JE, Bubendorf L, Guan XY, Jung YK, Kallioniemi OP, Kononen J, Trent JM, Azorsa D, Jhun BH, Cheong JH, Lee YC, Meltzer PS, Lee JW (1999). "A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo". J. Biol. Chem. 274 (48): 34283–93. doi:10.1074/jbc.274.48.34283. PMID 10567404.

[pmid11158331-13] Lee SK, Jung SY, Kim YS, Na SY, Lee YC, Lee JW (2001). "Two distinct nuclear receptor-interaction domains and CREB-binding protein-dependent transactivation function of activating signal cointegrator-2". Mol. Endocrinol. 15 (2): 241–54. doi:10.1210/me.15.2.241. PMID 11158331.

[pmid14578865-14] Kong HJ, Park MJ, Hong S, Yu HJ, Lee YC, Choi YH, Cheong J (2003). "Hepatitis B virus X protein regulates transactivation activity and protein stability of the cancer-amplified transcription coactivator ASC-2". Hepatology 38 (5): 1258–66. doi:10.1053/jhep.2003.50451. PMID 14578865.

[pmid11773444-15] Ko L, Cardona GR, Iwasaki T, Bramlett KS, Burris TP, Chin WW (2002). "Ser-884 adjacent to the LXXLL motif of coactivator TRBP defines selectivity for ERs and TRs". Mol. Endocrinol. 16 (1): 128–40. doi:10.1210/mend.16.1.0755. PMID 11773444.

[pmid9452433-16] Na SY, Kim HJ, Lee SK, Choi HS, Na DS, Lee MO, Chung M, Moore DD, Lee JW (1998). "IkappaBbeta interacts with the retinoid X receptor and inhibits retinoid-dependent transactivation in lipopolysaccharide-treated cells". J. Biol. Chem. 273 (6): 3212–5. doi:10.1074/jbc.273.6.3212. PMID 9452433.

[pmid12549917-17] Farooqui M, Franco PJ, Thompson J, Kagechika H, Chandraratna RA, Banaszak L, Wei LN (2003). "Effects of retinoid ligands on RIP140: molecular interaction with retinoid receptors and biological activity". Biochemistry 42 (4): 971–9. doi:10.1021/bi020497k. PMID 12549917.

[pmid8887632-18] L'Horset F, Dauvois S, Heery DM, Cavaillès V, Parker MG (1996). "RIP-140 interacts with multiple nuclear receptors by means of two distinct sites". Mol. Cell. Biol. 16 (11): 6029–36. PMC 231605. PMID 8887632.

[pmid14980220-19] Lin B, Kolluri SK, Lin F, Liu W, Han YH, Cao X, Dawson MI, Reed JC, Zhang XK (2004). "Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3". Cell 116 (4): 527–40. doi:10.1016/S0092-8674(04)00162-X. PMID 14980220.

[pmid11514567-20] Zhang C, Baudino TA, Dowd DR, Tokumaru H, Wang W, MacDonald PN (2001). "Ternary complexes and cooperative interplay between NCoA-62/Ski-interacting protein and steroid receptor coactivators in vitamin D receptor-mediated transcription". J. Biol. Chem. 276 (44): 40614–20. doi:10.1074/jbc.M106263200. PMID 11514567.

[pmid9267036-21] Chen H, Lin RJ, Schiltz RL, Chakravarti D, Nash A, Nagy L, Privalsky ML, Nakatani Y, Evans RM (1997). "Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300". Cell 90 (3): 569–80. doi:10.1016/S0092-8674(00)80516-4. PMID 9267036.

[pmid10480874-22] Préfontaine GG, Walther R, Giffin W, Lemieux ME, Pope L, Haché RJ (1999). "Selective binding of steroid hormone receptors to octamer transcription factors determines transcriptional synergism at the mouse mammary tumor virus promoter". J. Biol. Chem. 274 (38): 26713–9. doi:10.1074/jbc.274.38.26713. PMID 10480874.

[pmid10383413-23] Kakizawa T, Miyamoto T, Ichikawa K, Kaneko A, Suzuki S, Hara M, Nagasawa T, Takeda T, Mori Ji, Kumagai M, Hashizume K (1999). "Functional interaction between Oct-1 and retinoid X receptor". J. Biol. Chem. 274 (27): 19103–8. doi:10.1074/jbc.274.27.19103. PMID 10383413.

[pmid11714715-24] Delerive P, Wu Y, Burris TP, Chin WW, Suen CS (2002). "PGC-1 functions as a transcriptional coactivator for the retinoid X receptors". J. Biol. Chem. 277 (6): 3913–7. doi:10.1074/jbc.M109409200. PMID 11714715.

[pmid7838715-25] Tontonoz P, Graves RA, Budavari AI, Erdjument-Bromage H, Lui M, Hu E, Tempst P, Spiegelman BM (1994). "Adipocyte-specific transcription factor ARF6 is a heterodimeric complex of two nuclear hormone receptors, PPAR gamma and RXR alpha". Nucleic Acids Res. 22 (25): 5628–34. doi:10.1093/nar/22.25.5628. PMC 310126. PMID 7838715.

[pmid10854698-26] Berger J, Patel HV, Woods J, Hayes NS, Parent SA, Clemas J, Leibowitz MD, Elbrecht A, Rachubinski RA, Capone JP, Moller DE (2000). "A PPARgamma mutant serves as a dominant negative inhibitor of PPAR signaling and is localized in the nucleus". Mol. Cell. Endocrinol. 162 (1-2): 57–67. doi:10.1016/S0303-7207(00)00211-2. PMID 10854698.

[pmid10882139-27] Gampe RT, Montana VG, Lambert MH, Miller AB, Bledsoe RK, Milburn MV, Kliewer SA, Willson TM, Xu HE (2000). "Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the molecular basis of heterodimerization among nuclear receptors". Mol. Cell 5 (3): 545–55. doi:10.1016/S1097-2765(00)80448-7. PMID 10882139.

[pmid14981089-28] Takano Y, Adachi S, Okuno M, Muto Y, Yoshioka T, Matsushima-Nishiwaki R, Tsurumi H, Ito K, Friedman SL, Moriwaki H, Kojima S, Okano Y (2004). "The RING finger protein, RNF8, interacts with retinoid X receptor alpha and enhances its transcription-stimulating activity". J. Biol. Chem. 279 (18): 18926–34. doi:10.1074/jbc.M309148200. PMID 14981089.

[pmid12052862-29] Benkoussa M, Brand C, Delmotte MH, Formstecher P, Lefebvre P (2002). "Retinoic acid receptors inhibit AP1 activation by regulating extracellular signal-regulated kinase and CBP recruitment to an AP1-responsive promoter". Mol. Cell. Biol. 22 (13): 4522–34. doi:10.1128/MCB.22.13.4522-4534.2002. PMC 133906. PMID 12052862.

[pmid1314167-30] Bugge TH, Pohl J, Lonnoy O, Stunnenberg HG (1992). "RXR alpha, a promiscuous partner of retinoic acid and thyroid hormone receptors". EMBO J. 11 (4): 1409–18. PMC 556590. PMID 1314167.

[pmid10594021-31] Lee YK, Dell H, Dowhan DH, Hadzopoulou-Cladaras M, Moore DD (2000). "The orphan nuclear receptor SHP inhibits hepatocyte nuclear factor 4 and retinoid X receptor transactivation: two mechanisms for repression". Mol. Cell. Biol. 20 (1): 187–95. doi:10.1128/MCB.20.1.187-195.2000. PMC 85074. PMID 10594021.

[pmid12198243-32] Brendel C, Schoonjans K, Botrugno OA, Treuter E, Auwerx J (2002). "The small heterodimer partner interacts with the liver X receptor alpha and represses its transcriptional activity". Mol. Endocrinol. 16 (9): 2065–76. doi:10.1210/me.2001-0194. PMID 12198243.

[pmid12235159-33] Zeng M, Kumar A, Meng G, Gao Q, Dimri G, Wazer D, Band H, Band V (2002). "Human papilloma virus 16 E6 oncoprotein inhibits retinoic X receptor-mediated transactivation by targeting human ADA3 coactivator". J. Biol. Chem. 277 (47): 45611–8. doi:10.1074/jbc.M208447200. PMID 12235159.

[pmid7667283-34] Schulman IG, Chakravarti D, Juguilon H, Romo A, Evans RM (1995). "Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation". Proc. Natl. Acad. Sci. U.S.A. 92 (18): 8288–92. Bibcode:1995PNAS...92.8288S. doi:10.1073/pnas.92.18.8288. PMC 41142. PMID 7667283.

[pmid9115274-35] Thénot S, Henriquet C, Rochefort H, Cavaillès V (1997). "Differential interaction of nuclear receptors with the putative human transcriptional coactivator hTIF1". J. Biol. Chem. 272 (18): 12062–8. doi:10.1074/jbc.272.18.12062. PMID 9115274.

[pmid11851396-36] Lee WY, Noy N (2002). "Interactions of RXR with coactivators are differentially mediated by helix 11 of the receptor's ligand binding domain". Biochemistry 41 (8): 2500–8. doi:10.1021/bi011764. PMID 11851396.

[pmid9368056-37] Monden T, Wondisford FE, Hollenberg AN (1997). "Isolation and characterization of a novel ligand-dependent thyroid hormone receptor-coactivating protein". J. Biol. Chem. 272 (47): 29834–41. doi:10.1074/jbc.272.47.29834. PMID 9368056.

[pmid9171239-38] Jeyakumar M, Tanen MR, Bagchi MK (1997). "Analysis of the functional role of steroid receptor coactivator-1 in ligand-induced transactivation by thyroid hormone receptor". Mol. Endocrinol. 11 (6): 755–67. doi:10.1210/mend.11.6.0003. PMID 9171239.

[pmid9632709-39] Baudino TA, Kraichely DM, Jefcoat SC, Winchester SK, Partridge NC, MacDonald PN (1998). "Isolation and characterization of a novel coactivator protein, NCoA-62, involved in vitamin D-mediated transcription". J. Biol. Chem. 273 (26): 16434–41. doi:10.1074/jbc.273.26.16434. PMID 9632709.

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retinoid X receptor alpha