CoChat
Sign Up
Cited by 372Estrogen and related hormone effectsRetinoids in leukemia and cellular processesNuclear Receptors and Signaling

A Novel Orphan Receptor Specific for a Subset of Thyroid Hormone-Responsive Elements and Its Interaction with the Retinoid/Thyroid Hormone Receptor Subfamily

Open access
Apfel, R, Benbrook, D, Lernhardt, E, Ortiz, M A, Salbert, G, Pfahl, M·1994·Molecular and Cellular Biology
DOI 10.1128/mcb.14.10.7025PMC PMC359232
Open this paper in CoChat — free account

Abstract

The steroid/hormone nuclear receptor superfamily comprises several subfamilies of receptors that interact with overlapping DNA sequences and/or related ligands. The thyroid/retinoid hormone receptor subfamily has recently attracted much interest because of the complex network of its receptor interactions. The retinoid X receptors (RXRs), for instance, play a very central role in this subfamily, forming heterodimers with several receptors. Here we describe a novel member of this subfamily that interacts with RXR. Using a v-erbA probe, we obtained a cDNA which encodes a novel 445-amino-acid protein, RLD-1, that contains the characteristic domains of nuclear receptors. Northern (RNA) blot analysis showed that in mature rats, the receptor is highly expressed in spleen, pituitary, lung, liver, and fat. In addition, weaker expression is observed in several other tissues. Amino acid sequence alignment and DNA-binding data revealed that the DNA-binding domain of the new receptor is related to that of the thyroid/retinoid subgroup of nuclear receptors. RLD-1 preferentially binds as a heterodimer with RXR to a direct repeat of the half-site sequence 5'-G/AGGTCA-3', separated by four nucleotides (DR-4). Surprisingly, this binding is dependent to a high degree on the nature of the spacing nucleotides. None of the known nuclear receptor ligands activated RLD-1. In contrast, a DR-4-dependent constitutive transcriptional activation of a chloramphenicol acetyltransferase reporter gene by the RLD-1/RXR alpha heterodimer was observed. Our data suggest a highly specific role for this novel receptor within the network of gene regulation by the thyroid/retinoid receptor subfamily.

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 · 10.1128/mcb.14.10.7025

Cites

2 of 2 references verified0 citation errors · 0 not checkable

Statistics

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

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • LXRs (LXRβ and LXRα) are nuclear hormone receptor transcription factors that drive transcriptional activation of Apoe, as well as other genes involved in cholesterol, fatty acid, and glucose metabolism.

    “Liver-X receptors (LXRβ and LXRα) are members of the nuclear hormone receptor family of transcription factors that drive transcriptional activation of Apoe, as well as other genes involved in cholesterol, fatty acid, and glucose metabolism”

    From LXR/ApoE Activation Restricts Innate Immune Suppression in Cancer (2018) · cites this paper as Apfel et al., 1994

    Our copy describes RLD-1 as a nuclear receptor and reports its activation of a reporter gene (Abstract; page not provided). It does not identify RLD-1 as LXRα or LXRβ or address Apoe or genes involved in cholesterol, fatty-acid, and glucose metabolism. Searches for LXR, Apoe, and those metabolic terms found no passage establishing the attributed claim. (LLM, conf=0.76)

    Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Research works printed but not linked: 61

  1. Amy C. M., Williams-Ahlf B., Naggert J., Smith S. Molecular cloning of the mammalian fatty acid synthase gene and identification of the promoter region. Biochem J. 1990 Nov 1;271(3):675–679. doi: 10.1042/bj2710675. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  2. Baes M., Gulick T., Choi H. S., Martinoli M. G., Simha D., Moore D. D. A new orphan member of the nuclear hormone receptor superfamily that interacts with a subset of retinoic acid response elements. Mol Cell Biol. 1994 Mar;14(3):1544–1552. doi: 10.1128/mcb.14.3.1544-1552.1994. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  3. Carlberg C., Bendik I., Wyss A., Meier E., Sturzenbecker L. J., Grippo J. F., Hunziker W. Two nuclear signalling pathways for vitamin D. Nature. 1993 Feb 18;361(6413):657–660. doi: 10.1038/361657a0. [DOI] [PubMed] [Google Scholar] · DOI
  4. Chirgwin J. M., Przybyla A. E., MacDonald R. J., Rutter W. J. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry. 1979 Nov 27;18(24):5294–5299. doi: 10.1021/bi00591a005. [DOI] [PubMed] [Google Scholar] · DOI
  5. Cooney A. J., Tsai S. Y., O'Malley B. W., Tsai M. J. Chicken ovalbumin upstream promoter transcription factor (COUP-TF) dimers bind to different GGTCA response elements, allowing COUP-TF to repress hormonal induction of the vitamin D3, thyroid hormone, and retinoic acid receptors. Mol Cell Biol. 1992 Sep;12(9):4153–4163. doi: 10.1128/mcb.12.9.4153-4163.1992. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  6. Damm K., Heyman R. A., Umesono K., Evans R. M. Functional inhibition of retinoic acid response by dominant negative retinoic acid receptor mutants. Proc Natl Acad Sci U S A. 1993 Apr 1;90(7):2989–2993. doi: 10.1073/pnas.90.7.2989. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  7. Danielian P. S., White R., Lees J. A., Parker M. G. Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors. EMBO J. 1992 Mar;11(3):1025–1033. doi: 10.1002/j.1460-2075.1992.tb05141.x. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  8. Davis I. J., Hazel T. G., Lau L. F. Transcriptional activation by Nur77, a growth factor-inducible member of the steroid hormone receptor superfamily. Mol Endocrinol. 1991 Jun;5(6):854–859. doi: 10.1210/mend-5-6-854. [DOI] [PubMed] [Google Scholar] · DOI
  9. Debuire B., Henry C., Bernissa M., Biserte G., Claverie J. M., Saule S., Martin P., Stehelin D. Sequencing the erbA gene of avian erythroblastosis virus reveals a new type of oncogene. Science. 1984 Jun 29;224(4656):1456–1459. doi: 10.1126/science.6328658. [DOI] [PubMed] [Google Scholar] · DOI
  10. Disela C., Glineur C., Bugge T., Sap J., Stengl G., Dodgson J., Stunnenberg H., Beug H., Zenke M. v-erbA overexpression is required to extinguish c-erbA function in erythroid cell differentiation and regulation of the erbA target gene CAII. Genes Dev. 1991 Nov;5(11):2033–2047. doi: 10.1101/gad.5.11.2033. [DOI] [PubMed] [Google Scholar] · DOI
  11. Evans R. M. The steroid and thyroid hormone receptor superfamily. Science. 1988 May 13;240(4854):889–895. doi: 10.1126/science.3283939. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  12. Feinberg A. P., Vogelstein B. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal Biochem. 1983 Jul 1;132(1):6–13. doi: 10.1016/0003-2697(83)90418-9. [DOI] [PubMed] [Google Scholar] · DOI
  13. Forman B. M., Samuels H. H. Interactions among a subfamily of nuclear hormone receptors: the regulatory zipper model. Mol Endocrinol. 1990 Sep;4(9):1293–1301. doi: 10.1210/mend-4-9-1293. [DOI] [PubMed] [Google Scholar] · DOI
  14. Forman B. M., Yang C. R., Au M., Casanova J., Ghysdael J., Samuels H. H. A domain containing leucine-zipper-like motifs mediate novel in vivo interactions between the thyroid hormone and retinoic acid receptors. Mol Endocrinol. 1989 Oct;3(10):1610–1626. doi: 10.1210/mend-3-10-1610. [DOI] [PubMed] [Google Scholar] · DOI
  15. Freedman L. P., Arce V., Perez Fernandez R. DNA sequences that act as high affinity targets for the vitamin D3 receptor in the absence of the retinoid X receptor. Mol Endocrinol. 1994 Mar;8(3):265–273. doi: 10.1210/mend.8.3.8015545. [DOI] [PubMed] [Google Scholar] · DOI
  16. Graupner G., Wills K. N., Tzukerman M., Zhang X. K., Pfahl M. Dual regulatory role for thyroid-hormone receptors allows control of retinoic-acid receptor activity. Nature. 1989 Aug 24;340(6235):653–656. doi: 10.1038/340653a0. [DOI] [PubMed] [Google Scholar] · DOI
  17. Green S., Chambon P. Nuclear receptors enhance our understanding of transcription regulation. Trends Genet. 1988 Nov;4(11):309–314. doi: 10.1016/0168-9525(88)90108-4. [DOI] [PubMed] [Google Scholar] · DOI
  18. Hazel T. G., Misra R., Davis I. J., Greenberg M. E., Lau L. F. Nur77 is differentially modified in PC12 cells upon membrane depolarization and growth factor treatment. Mol Cell Biol. 1991 Jun;11(6):3239–3246. doi: 10.1128/mcb.11.6.3239-3246.1991. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  19. Hermann T., Hoffmann B., Piedrafita F. J., Zhang X. K., Pfahl M. V-erbA requires auxiliary proteins for dominant negative activity. Oncogene. 1993 Jan;8(1):55–65. [PubMed] [Google Scholar]
  20. Hermann T., Hoffmann B., Zhang X. K., Tran P., Pfahl M. Heterodimeric receptor complexes determine 3,5,3'-triiodothyronine and retinoid signaling specificities. Mol Endocrinol. 1992 Jul;6(7):1153–1162. doi: 10.1210/mend.6.7.1324421. [DOI] [PubMed] [Google Scholar] · DOI
  21. Hermann T., Zhang X. K., Tzukerman M., Wills K. N., Graupner G., Pfahl M. Regulatory functions of a non-ligand-binding thyroid hormone receptor isoform. Cell Regul. 1991 Jul;2(7):565–574. doi: 10.1091/mbc.2.7.565. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  22. Hoffmann B., Lehmann J. M., Zhang X. K., Hermann T., Husmann M., Graupner G., Pfahl M. A retinoic acid receptor-specific element controls the retinoic acid receptor-beta promoter. Mol Endocrinol. 1990 Nov;4(11):1727–1736. doi: 10.1210/mend-4-11-1727. [DOI] [PubMed] [Google Scholar] · DOI
  23. Huggenvik J. I., Collard M. W., Kim Y. W., Sharma R. P. Modification of the retinoic acid signaling pathway by the catalytic subunit of protein kinase-A. Mol Endocrinol. 1993 Apr;7(4):543–550. doi: 10.1210/mend.7.4.8388997. [DOI] [PubMed] [Google Scholar] · DOI
  24. Hunt C. R., Ro J. H., Dobson D. E., Min H. Y., Spiegelman B. M. Adipocyte P2 gene: developmental expression and homology of 5'-flanking sequences among fat cell-specific genes. Proc Natl Acad Sci U S A. 1986 Jun;83(11):3786–3790. doi: 10.1073/pnas.83.11.3786. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  25. Hwung Y. P., Crowe D. T., Wang L. H., Tsai S. Y., Tsai M. J. The COUP transcription factor binds to an upstream promoter element of the rat insulin II gene. Mol Cell Biol. 1988 May;8(5):2070–2077. doi: 10.1128/mcb.8.5.2070-2077.1988. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  26. Jurutka P. W., Hsieh J. C., MacDonald P. N., Terpening C. M., Haussler C. A., Haussler M. R., Whitfield G. K. Phosphorylation of serine 208 in the human vitamin D receptor. The predominant amino acid phosphorylated by casein kinase II, in vitro, and identification as a significant phosphorylation site in intact cells. J Biol Chem. 1993 Mar 25;268(9):6791–6799. [PubMed] [Google Scholar]
  27. Kim H. S., Crone D. E., Sprung C. N., Tillman J. B., Force W. R., Crew M. D., Mote P. L., Spindler S. R. Positive and negative thyroid hormone response elements are composed of strong and weak half-sites 10 nucleotides in length. Mol Endocrinol. 1992 Sep;6(9):1489–1501. doi: 10.1210/mend.6.9.1435790. [DOI] [PubMed] [Google Scholar] · DOI
  28. Kimura A., Nishiyori A., Murakami T., Tsukamoto T., Hata S., Osumi T., Okamura R., Mori M., Takiguchi M. Chicken ovalbumin upstream promoter-transcription factor (COUP-TF) represses transcription from the promoter of the gene for ornithine transcarbamylase in a manner antagonistic to hepatocyte nuclear factor-4 (HNF-4). J Biol Chem. 1993 May 25;268(15):11125–11133. [PubMed] [Google Scholar]
  29. Kliewer S. A., Umesono K., Heyman R. A., Mangelsdorf D. J., Dyck J. A., Evans R. M. Retinoid X receptor-COUP-TF interactions modulate retinoic acid signaling. Proc Natl Acad Sci U S A. 1992 Feb 15;89(4):1448–1452. doi: 10.1073/pnas.89.4.1448. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  30. Kliewer S. A., Umesono K., Mangelsdorf D. J., Evans R. M. Retinoid X receptor interacts with nuclear receptors in retinoic acid, thyroid hormone and vitamin D3 signalling. Nature. 1992 Jan 30;355(6359):446–449. doi: 10.1038/355446a0. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  31. Kurokawa R., Yu V. C., När A., Kyakumoto S., Han Z., Silverman S., Rosenfeld M. G., Glass C. K. Differential orientations of the DNA-binding domain and carboxy-terminal dimerization interface regulate binding site selection by nuclear receptor heterodimers. Genes Dev. 1993 Jul;7(7B):1423–1435. doi: 10.1101/gad.7.7b.1423. [DOI] [PubMed] [Google Scholar] · DOI
  32. Laudet V., Hänni C., Coll J., Catzeflis F., Stéhelin D. Evolution of the nuclear receptor gene superfamily. EMBO J. 1992 Mar;11(3):1003–1013. doi: 10.1002/j.1460-2075.1992.tb05139.x. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  33. Lazar M. A., Hodin R. A., Darling D. S., Chin W. W. A novel member of the thyroid/steroid hormone receptor family is encoded by the opposite strand of the rat c-erbA alpha transcriptional unit. Mol Cell Biol. 1989 Mar;9(3):1128–1136. doi: 10.1128/mcb.9.3.1128-1136.1989. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  34. Lazar M. A., Hodin R. A., Darling D. S., Chin W. W. Identification of a rat c-erbA alpha-related protein which binds deoxyribonucleic acid but does not bind thyroid hormone. Mol Endocrinol. 1988 Oct;2(10):893–901. doi: 10.1210/mend-2-10-893. [DOI] [PubMed] [Google Scholar] · DOI
  35. Lee M. O., Hobbs P. D., Zhang X. K., Dawson M. I., Pfahl M. A synthetic retinoid antagonist inhibits the human immunodeficiency virus type 1 promoter. Proc Natl Acad Sci U S A. 1994 Jun 7;91(12):5632–5636. doi: 10.1073/pnas.91.12.5632. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  36. Lehmann J. M., Jong L., Fanjul A., Cameron J. F., Lu X. P., Haefner P., Dawson M. I., Pfahl M. Retinoids selective for retinoid X receptor response pathways. Science. 1992 Dec 18;258(5090):1944–1946. doi: 10.1126/science.1335166. [DOI] [PubMed] [Google Scholar] · DOI
  37. Lehmann J. M., Zhang X. K., Graupner G., Lee M. O., Hermann T., Hoffmann B., Pfahl M. Formation of retinoid X receptor homodimers leads to repression of T3 response: hormonal cross talk by ligand-induced squelching. Mol Cell Biol. 1993 Dec;13(12):7698–7707. doi: 10.1128/mcb.13.12.7698-7707.1993. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  38. Leid M., Kastner P., Lyons R., Nakshatri H., Saunders M., Zacharewski T., Chen J. Y., Staub A., Garnier J. M., Mader S. Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently. Cell. 1992 Jan 24;68(2):377–395. doi: 10.1016/0092-8674(92)90478-u. [DOI] [PubMed] [Google Scholar] · DOI
  39. Luckow B., Schütz G. Cell-type specificity of regulatory elements identified by linker scanning mutagenesis in the promoter of the chicken lysozyme gene. Nucleic Acids Res. 1989 Nov 11;17(21):8451–8462. doi: 10.1093/nar/17.21.8451. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  40. MacDonald P. N., Dowd D. R., Nakajima S., Galligan M. A., Reeder M. C., Haussler C. A., Ozato K., Haussler M. R. Retinoid X receptors stimulate and 9-cis retinoic acid inhibits 1,25-dihydroxyvitamin D3-activated expression of the rat osteocalcin gene. Mol Cell Biol. 1993 Sep;13(9):5907–5917. doi: 10.1128/mcb.13.9.5907-5917.1993. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  41. Mader S., Chen J. Y., Chen Z., White J., Chambon P., Gronemeyer H. The patterns of binding of RAR, RXR and TR homo- and heterodimers to direct repeats are dictated by the binding specificites of the DNA binding domains. EMBO J. 1993 Dec 15;12(13):5029–5041. doi: 10.1002/j.1460-2075.1993.tb06196.x. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  42. Mader S., Leroy P., Chen J. Y., Chambon P. Multiple parameters control the selectivity of nuclear receptors for their response elements. Selectivity and promiscuity in response element recognition by retinoic acid receptors and retinoid X receptors. J Biol Chem. 1993 Jan 5;268(1):591–600. [PubMed] [Google Scholar]
  43. O'Malley B. W., Conneely O. M. Orphan receptors: in search of a unifying hypothesis for activation. Mol Endocrinol. 1992 Sep;6(9):1359–1361. doi: 10.1210/mend.6.9.1331771. [DOI] [PubMed] [Google Scholar] · DOI
  44. Paulsen R. E., Weaver C. A., Fahrner T. J., Milbrandt J. Domains regulating transcriptional activity of the inducible orphan receptor NGFI-B. J Biol Chem. 1992 Aug 15;267(23):16491–16496. [PubMed] [Google Scholar]
  45. Pfahl M., Apfel R., Bendik I., Fanjul A., Graupner G., Lee M. O., La-Vista N., Lu X. P., Piedrafita J., Ortiz M. A. Nuclear retinoid receptors and their mechanism of action. Vitam Horm. 1994;49:327–382. doi: 10.1016/s0083-6729(08)61150-4. [DOI] [PubMed] [Google Scholar] · DOI
  46. Pfahl M. Nuclear receptor/AP-1 interaction. Endocr Rev. 1993 Oct;14(5):651–658. doi: 10.1210/edrv-14-5-651. [DOI] [PubMed] [Google Scholar] · DOI
  47. Pfahl M., Tzukerman M., Zhang X. K., Lehmann J. M., Hermann T., Wills K. N., Graupner G. Nuclear retinoic acid receptors: cloning, analysis, and function. Methods Enzymol. 1990;189:256–270. doi: 10.1016/0076-6879(90)89297-u. [DOI] [PubMed] [Google Scholar] · DOI
  48. Segraves W. A., Hogness D. S. The E75 ecdysone-inducible gene responsible for the 75B early puff in Drosophila encodes two new members of the steroid receptor superfamily. Genes Dev. 1990 Feb;4(2):204–219. doi: 10.1101/gad.4.2.204. [DOI] [PubMed] [Google Scholar] · DOI
  49. Sladek F. M., Zhong W. M., Lai E., Darnell J. E., Jr Liver-enriched transcription factor HNF-4 is a novel member of the steroid hormone receptor superfamily. Genes Dev. 1990 Dec;4(12B):2353–2365. doi: 10.1101/gad.4.12b.2353. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  50. Takimoto G. S., Tasset D. M., Eppert A. C., Horwitz K. B. Hormone-induced progesterone receptor phosphorylation consists of sequential DNA-independent and DNA-dependent stages: analysis with zinc finger mutants and the progesterone antagonist ZK98299. Proc Natl Acad Sci U S A. 1992 Apr 1;89(7):3050–3054. doi: 10.1073/pnas.89.7.3050. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  51. Thomas H. E., Stunnenberg H. G., Stewart A. F. Heterodimerization of the Drosophila ecdysone receptor with retinoid X receptor and ultraspiracle. Nature. 1993 Apr 1;362(6419):471–475. doi: 10.1038/362471a0. [DOI] [PubMed] [Google Scholar] · DOI
  52. Tran P., Zhang X. K., Salbert G., Hermann T., Lehmann J. M., Pfahl M. COUP orphan receptors are negative regulators of retinoic acid response pathways. Mol Cell Biol. 1992 Oct;12(10):4666–4676. doi: 10.1128/mcb.12.10.4666-4676.1992. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  53. Umesono K., Murakami K. K., Thompson C. C., Evans R. M. Direct repeats as selective response elements for the thyroid hormone, retinoic acid, and vitamin D3 receptors. Cell. 1991 Jun 28;65(7):1255–1266. doi: 10.1016/0092-8674(91)90020-y. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  54. Wang L. H., Tsai S. Y., Sagami I., Tsai M. J., O'Malley B. W. Purification and characterization of chicken ovalbumin upstream promoter transcription factor from HeLa cells. J Biol Chem. 1987 Nov 25;262(33):16080–16086. [PubMed] [Google Scholar]
  55. Wilson T. E., Fahrner T. J., Johnston M., Milbrandt J. Identification of the DNA binding site for NGFI-B by genetic selection in yeast. Science. 1991 May 31;252(5010):1296–1300. doi: 10.1126/science.1925541. [DOI] [PubMed] [Google Scholar] · DOI
  56. Yu V. C., Delsert C., Andersen B., Holloway J. M., Devary O. V., När A. M., Kim S. Y., Boutin J. M., Glass C. K., Rosenfeld M. G. RXR beta: a coregulator that enhances binding of retinoic acid, thyroid hormone, and vitamin D receptors to their cognate response elements. Cell. 1991 Dec 20;67(6):1251–1266. doi: 10.1016/0092-8674(91)90301-e. [DOI] [PubMed] [Google Scholar] · DOI
  57. Zenke M., Muñoz A., Sap J., Vennström B., Beug H. v-erbA oncogene activation entails the loss of hormone-dependent regulator activity of c-erbA. Cell. 1990 Jun 15;61(6):1035–1049. doi: 10.1016/0092-8674(90)90068-p. [DOI] [PubMed] [Google Scholar] · DOI
  58. Zhang X. K., Hoffmann B., Tran P. B., Graupner G., Pfahl M. Retinoid X receptor is an auxiliary protein for thyroid hormone and retinoic acid receptors. Nature. 1992 Jan 30;355(6359):441–446. doi: 10.1038/355441a0. [DOI] [PubMed] [Google Scholar] · DOI
  59. Zhang X. K., Lehmann J., Hoffmann B., Dawson M. I., Cameron J., Graupner G., Hermann T., Tran P., Pfahl M. Homodimer formation of retinoid X receptor induced by 9-cis retinoic acid. Nature. 1992 Aug 13;358(6387):587–591. doi: 10.1038/358587a0. [DOI] [PubMed] [Google Scholar] · DOI
  60. Zhang X. K., Tran P. B., Pfahl M. DNA binding and dimerization determinants for thyroid hormone receptor alpha and its interaction with a nuclear protein. Mol Endocrinol. 1991 Dec;5(12):1909–1920. doi: 10.1210/mend-5-12-1909. [DOI] [PubMed] [Google Scholar] · DOI
  61. Zhang X. K., Wills K. N., Graupner G., Tzukerman M., Hermann T., Pfahl M. Ligand-binding domain of thyroid hormone receptors modulates DNA binding and determines their bifunctional roles. New Biol. 1991 Feb;3(2):169–181. [PubMed] [Google Scholar]

Cited by

Sorted by citations

Authors
Apfel, R., Benbrook, D., Lernhardt, E., Ortiz, M. A., Salbert, G., & Pfahl, M.
Affiliations
Sanford Burnham Prebys Medical Discovery Institute (US)
ORCID
Venue
Molecular and Cellular Biology
Publisher
Informa UK Limited
Published
1994-10
Volume
14
Issue
10
Pages
7025-7035
ISSN
  • 0270-7306 (ISSN-L)
  • 1098-5549
DOI
10.1128/mcb.14.10.7025
PMC
PMC359232
OpenAlex
W2113624181
Cited by
372
References
2
Citations by year
2026: 1 · 2025: 5 · 2024: 7 · 2023: 15 · 2022: 8 · 2021: 5 · 2020: 17 · 2019: 8 · 2018: 14 · 2017: 15 · 2016: 6 · 2015: 13 · 2014: 12 · 2013: 29 · 2012: 16
FWCI
5.48
Type
journal article
Language
en
Open access
Locations
  • Molecular and Cellular Biology (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5r01ca050676-03)
  • National Cancer Institute (CA50676, CA55681, R01CA055681)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinoids in leukemia and cellular processes
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nuclear Receptors and Signaling
Keywords
orphan nuclear receptor, retinoid X receptor, DNA-binding domain, constitutive transcriptional activation, v-erbA, gene expression regulation
MeSH terms
Liver X Receptors, Amino Acid Sequence, Animals, Base Sequence, Cells, Cultured, Cloning, Molecular, DNA-Binding Proteins, Gene Expression Regulation, Molecular Sequence Data, Protein Binding, Receptors, Thyroid Hormone, Regulatory Sequences, Nucleic Acid, Thyroid Hormones, Tissue Distribution, Transcription Factors, Sequence Homology, Amino Acid, Sequence Analysis, DNA, Receptors, Cytoplasmic and Nuclear, Receptors, Retinoic Acid, Retinoid X Receptors, Rats, Orphan Nuclear Receptors

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