The DOI matches its Crossref record; 136 of the 136 references it cites were found in a registry or an index.
Nuclear receptors: integration of multiple signalling pathways through phosphorylation
Abstract
Nuclear receptors (NRs) orchestrate the transcription of specific gene networks in response to binding of their cognate ligand. They also act as mediators in a variety of signalling pathways through integrating diverse phosphorylation events. NR phosphorylation concerns all three major domains, the N-terminal activation function (AF-1), the ligand-binding and the DNA binding domains. Often, phosphorylation of NRs by kinases that are associated with general transcription factors (e.g. cdk7 within TFIIH), or activated in response to a variety of signals (MAPKs, Akt, PKA, PKC), facilitates the recruitment of coactivators or of components of the transcription machinery and, therefore, cooperates with the ligand to enhance transcription activation. But phosphorylation can also contribute to the termination of the ligand response through inducing DNA dissociation or NR degradation or through decreasing ligand affinity. These different modes of regulation reveal an unexpected complexity of the dynamics of NR-mediated transcription. In addition, deregulation of NR phosphorylation may impact their action in certain diseases or cancers.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“For several years, RARs and RXRs have been known to be phosphoproteins ( 129 ).”
From Vitamin A and retinoid signaling: genomic and nongenomic effects (2013) · cites this paper as [129]
Citations
Cites
2 retracted
Endoh, H., Maruyama, K., Masuhiro, Y., Kobayashi, Y., Goto, M., Tai, H., Yanagisawa, J., METZGER, D., Hashimoto, S., & Kato, S. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.01458-13 · Cited by 363
RetractedWatanabe, M., Yanagisawa, J., Kitagawa, H., Takeyama, K., Ogawa, S., Arao, Y., Suzawa, M., Kobayashi, Y., Yano, T., Yoshikawa, H., et al. (2001) · The EMBO Journal · doi:10.1093/emboj/20.6.1341 · Cited by 267
RetractedThe nuclear receptor superfamily: the second decade
Mangelsdorf, D. J., Thummel, C., Beato, M., Herrlich, P., Schütz, G., Umesono, K., Blumberg, B., Kastner, P., Mark, M., Chambon, P., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90199-x · Cited by 6,964
Mammalian MAP kinase signalling cascades
Chang, L., & Karin, M. (2001) · Nature · doi:10.1038/35065000 · Cited by 5,118
Cellular survival: a play in three Akts
Datta, S. R., Brunet, A., & Greenberg, M. E. (1999) · Genes & Development · doi:10.1101/gad.13.22.2905 · Cited by 4,216
Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological Functions*
Pearson, G. W., Robinson, F. L., Gibson, T. B., Xu, B.-E., Karandikar, M. S., Berman, K. S., & Cobb, M. H. (2001) · Endocrine Reviews · doi:10.1210/edrv.22.2.0428 · Cited by 4,111
Blume-Jensen, P., & Hunter, T. (2001) · Nature · doi:10.1038/35077225 · Cited by 3,738
Molecular basis of agonism and antagonism in the oestrogen receptor
Brzozowski, A. M., Pike, A. C. W., Dauter, Z., Hubbard, R. E., Bonn, T., Engström, O., Öhman, L., Greene, G. L., Gustafsson, J.-Å., & Carlquist, M. (1997) · Nature · doi:10.1038/39645 · Cited by 3,355
Morgan, D. O. (1995) · Nature · doi:10.1038/374131a0 · Cited by 3,288
A decade of molecular biology of retinoic acid receptors
Chambon, P. (1996) · The FASEB Journal · doi:10.1096/fasebj.10.9.8801176 · Cited by 2,889
Research works printed but not linked: 14
- Glass, 1994, Endocr. Rev., 15, 391
- Giguere, 1999, Endocr. Rev., 20, 689
- Pearson, 2001, Endocr. Rev., 22, 153
- Arnold, 1995, Mol. Endocrinol., 9, 24
- Migliaccio, 1993, Oncogene, 8, 2183
- Huggenvick, 1994, Mol. Endocrinol., 7, 543
- Rochette-Egly, 1995, Mol. Endocrinol., 9, 860
- Rochette-Egly, 2001, Histol. Histopathol., 16, 909
- Endoh, 1999, Mol. Cell Biol., 19, 5363, 10.1128/MCB.19.8.5363 · DOI
- Rochette-Egly, 2000, Mol. Endocrinol., 14, 1398
- Matsushima-Nishiwaki, 2001, Cancer Res., 61, 7675
- Wen, 2000, Cancer Res., 60, 6841
- Zhang, 1995, Mol. Endocrinol., 9, 1029
- Joel, 1995, Mol. Endocrinol., 9, 1041
Cited by
Sorted by citations
Items 101–200 of 292
Wu, L., Cai, X., Dong, H., Wei, J., Huang, Y., Yang, X., Wu, Y., & Lin, Y. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00709.x · Cited by 47
Liu, Y., Mo, J. Q., Hu, Q., Boivin, G. P., Levin, L., Lu, S., Yang, D., Dong, Z., & Lu, S. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0645 · Cited by 45
Hess, R. A. (2014) · Spermatogenesis · doi:10.4161/21565562.2014.979103 · Cited by 44
Nuclear and extranuclear effects of vitamin A
Iskakova, M., Karbyshev, M. S., Piskunov, A., & Rochette‐Egly, C. (2015) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2014-0522 · Cited by 47
Self-citationPhosphorylation of Steroidogenic Factor 1 Is Mediated by Cyclin-Dependent Kinase 7
Lewis, A. E., Rusten, M., Høivik, E. A., Vikse, E. L., Hansson, M. L., Wallberg, A. E., & Bakke, M. (2007) · Molecular Endocrinology · doi:10.1210/me.2006-0478 · Cited by 44
Gianni’, M., Couturier‐Tarrade, A., Nigro, E. A., Garattini, E., & Rochette‐Egly, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304952200 · Cited by 44
Self-citationZellweger, T., Stürm, S., Rey, S., Zlobec, I., Gsponer, J. R., Rentsch, C. A., Terracciano, L., Bachmann, A., Bubendorf, L., & Ruiz, C. F. (2013) · Endocrine Related Cancer · doi:10.1530/erc-12-0402 · Cited by 43
Lu (2010) · International Journal of Oncology · doi:10.3892/ijo_00000538 · Cited by 43
Urushitani, H., Katsu, Y., Ohta, Y., Shiraishi, H., Iguchi, T., & Horiguchi, T. (2011) · Aquatic Toxicology · doi:10.1016/j.aquatox.2011.02.012 · Cited by 42
Nuclear receptors in the cross-talk of drug metabolism and inflammation
Gerbal‐Chaloin, S., Iankova, I., Maurel, P., & Daujat‐Chavanieu, M. (2013) · Drug Metabolism Reviews · doi:10.3109/03602532.2012.756011 · Cited by 41
Targeting hepatic kisspeptin receptor ameliorates nonalcoholic fatty liver disease in a mouse model
Guzman, S., Dragan, M., Kwon, H., Oliveira, V. D., Rao, S., Bhatt, V., Kalemba, K. M., Shah, A., Rustgi, V. K., Wang, H., et al. (2022) · Journal of Clinical Investigation · doi:10.1172/jci145889 · Cited by 43
Urushitani, H., Katsu, Y., Ohta, Y., Shiraishi, H., Iguchi, T., & Horiguchi, T. (2013) · Aquatic Toxicology · doi:10.1016/j.aquatox.2013.09.008 · Cited by 42
Synergistic Effects of PPAR γ Ligands and Retinoids in Cancer Treatment
Shimizu, M., & Moriwaki, H. (2008) · PPAR Research · doi:10.1155/2008/181047 · Cited by 40
Murthy, K. N. C., Jayaprakasha, G. K., & Patil, B. S. (2015) · Toxicology · doi:10.1016/j.tox.2015.01.008 · Cited by 39
Orphan nuclear receptor NR2F6 acts as an essential gatekeeper of Th17 CD4+ T cell effector functions
Hermann‐Kleiter, N., & Baier, G. (2014) · Cell Communication and Signaling · doi:10.1186/1478-811x-12-38 · Cited by 40
Sivertsson, L., Edebert, I., Porsmyr‐Palmertz, M., Ingelman‐Sundberg, M., & Neve, E. P. A. (2012) · Molecular Pharmacology · doi:10.1124/mol.112.082305 · Cited by 39
Staudinger, J. L., & Lichti-Kaiser, K. (2007) · Molecular Pharmaceutics · doi:10.1021/mp700098c · Cited by 39
Evidence for 1,25-Dihydroxyvitamin D3-independent Transactivation by the Vitamin D Receptor
Ellison, T. I., Eckert, R. L., & MacDonald, P. N. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609717200 · Cited by 39
Ghose, R., Guo, T., & Haque, N. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.10.003 · Cited by 37
Dily, F. L., Métivier, R., Guéguen, M., Péron, C. L., Flouriot, G., Tas, P., & Pakdel, F. (2007) · Breast Cancer Research and Treatment · doi:10.1007/s10549-007-9693-6 · Cited by 37
Ghose, R., Guo, T., Vallejo, J. G., & Gandhi, A. S. (2011) · Drug Metabolism and Disposition · doi:10.1124/dmd.110.037382 · Cited by 36
Sinha, S., Uchibe, K., Usami, Y., Pacifici, M., & Iwamoto, M. (2016) · Bone · doi:10.1016/j.bone.2016.02.008 · Cited by 37
Helzer, K. T., Ozers, M. S., Meyer, M. B., Benkusky, N. A., Solodin, N. M., Reese, R., Warren, C. L., Pike, J. W., & Alarid, E. T. (2018) · Molecular and Cellular Biology · doi:10.1128/mcb.00417-18 · Cited by 36
Spironolactone and XPB: An Old Drug with a New Molecular Target
Gabbard, R. D., Hoopes, R. R., & Kemp, M. G. (2020) · Biomolecules · doi:10.3390/biom10050756 · Cited by 35
Nuclear and Extra-Nuclear Effects of Retinoid Acid Receptors: How They Are Interconnected
Piskunov, A., Tanoury, Z. A., & Rochette‐Egly, C. (2014) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-017-9050-5_6 · Cited by 38
Self-citationTsai, T., Lee, Y.-L., Hsiao, W.-C., Tsao, Y., & Chen, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412169200 · Cited by 34
Tanoury, Z. A., Piskunov, A., Andriamoratsiresy, D., Gaouar, S., Lutzing, R., Ye, T., Jost, B., Keime, C., & Rochette‐Egly, C. (2013) · Journal of Cell Science · doi:10.1242/jcs.131946 · Cited by 33
Self-citationBecnel, L. B., Ochsner, S. A., Darlington, Y. F., McOwiti, A., Kankanamge, W. H., Dehart, M., Naumov, A., & McKenna, N. J. (2017) · Science Signaling · doi:10.1126/scisignal.aah6275 · Cited by 31
Ghose, R., White, D., Guo, T., Vallejo, J. G., & Karpen, S. J. (2007) · Drug Metabolism and Disposition · doi:10.1124/dmd.107.018051 · Cited by 32
Retinoid Signaling in Cancer and Its Promise for Therapy
Coyle, K. M. (2013) · Journal of Carcinogenesis & Mutagenesis · doi:10.4172/2157-2518.s7-006 · Cited by 32
Domi, E., Caputi, F. F., Romualdi, P., Domi, A., Scuppa, G., Candeletti, S., Atkins, A. L., Heilig, M. A., Demopulos, G. A., Gaitanaris, G., et al. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.1922-19.2019 · Cited by 32
Retinoic Acid Receptors: Structural Basis for Coregulator Interaction and Exchange
le Maire, A., & Bourguet, W. (2014) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-017-9050-5_3 · Cited by 32
Xie, Y., Wolff, D. W., Lin, M., & Tu, Y. (2007) · Molecular Pharmacology · doi:10.1124/mol.107.033894 · Cited by 32
Wang, G., & Sadar, M. D. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20802 · Cited by 32
Smutný, T., Bitman, M., Urban, M., Dubecka, M., Vrzal, R., Dvořák, Z., & Pávek, P. (2014) · Archives of Toxicology · doi:10.1007/s00204-014-1254-2 · Cited by 31
Protein kinase C α modulates liver X receptor α transactivation
Delvecchio, C. J., & Capone, J. P. (2008) · Journal of Endocrinology · doi:10.1677/joe-07-0525 · Cited by 33
Liu, J., Hernández, S. E., Swift, S., & Singhal, N. (2018) · Water Research · doi:10.1016/j.watres.2018.01.018 · Cited by 30
The multi-faceted role of retinoid X receptor in cardiovascular diseases
Shao, M., Lu, L., Wang, Q. Q., Ma, L., Tian, X., Li, C., Li, C., Guo, D., Wang, Q., Wang, W., et al. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111264 · Cited by 30
Vucetic, Z., Zhang, Z., Zhao, J., Wang, F., Soprano, K. J., & Soprano, D. R. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01199-07 · Cited by 29
Huq, M. D. M., Gupta, P. K., Tsai, N., & Wei, L. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600180-mcp200 · Cited by 29
Targeting truncated RXRα for cancer therapy
Zhang, X.-K., Zhou, H., & Su, Y. (2015) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmv104 · Cited by 31
Regulation of PXR in drug metabolism: chemical and structural perspectives
Gee, R. R. F., Huber, A. D., & Chen, T. (2024) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1080/17425255.2024.2309212 · Cited by 32
Nuclear GRP75 Binds Retinoic Acid Receptors to Promote Neuronal Differentiation of Neuroblastoma
Shih, Y., Lee, H., Nakagawara, A., Juan, H., Jeng, Y., Tsay, Y., Lin, D., Hsieh, F.-J., Pan, C., Hsu, W., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026236 · Cited by 29
Tanoury, Z. A., Gaouar, S., Piskunov, A., Ye, T., Urban, S., Jost, B., Keime, C., Davidson, I., Dierich, A., & Rochette‐Egly, C. (2014) · Journal of Cell Science · doi:10.1242/jcs.145979 · Cited by 28
Self-citationGarattini, E., Gianni’, M., & Terao, M. (2007) · Vitamins and hormones · doi:10.1016/s0083-6729(06)75012-9 · Cited by 28
Botta, E., Nardò, T., Orioli, D., Guglielmino, R., Ricotti, R., Bondanza, S., Benedicenti, F., Zambruno, G., & Stefanini, M. (2008) · Human Mutation · doi:10.1002/humu.20912 · Cited by 29
Molecular Mechanisms of Retinoid Receptors in Diabetes-Induced Cardiac Remodeling
Pan, J., Guleria, R. S., Zhu, S., & Baker, K. M. (2014) · Journal of Clinical Medicine · doi:10.3390/jcm3020566 · Cited by 29
Function of Pparγ and Its Ligands in Lung Cancer
Li, M., Lee, T. W., Yim, A. P. C., & Chen, G. G. (2006) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360600552587 · Cited by 28
Unifying Electrostatic Mechanism for Receptor-Ligand Activity
Kovacic, P., Pozos, R. S., & DRASKOVICH, C. D. (2007) · Journal of Receptors and Signal Transduction · doi:10.1080/10799890701699686 · Cited by 28
Álba, G., Reyes-Quiróz, M. E., Santa‐María, C., Ramírez, R., Geniz, I., Jiménez, J., Martín‐Nieto, J., Pintado, E., & Sobrino, F. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042195 · Cited by 27
Intracellular Signaling Pathways Regulate Hormone-Dependent Kallikrein Gene Expression
Paliouras, M., & Diamandis, E. P. (2008) · Tumor Biology · doi:10.1159/000135686 · Cited by 27
Glucocorticoids reduce inflammation in cystic fibrosis bronchial epithelial cells
Rebeyrol, C., Saint‐Criq, V., Guillot, L., Riffault, L., Corvol, H., Chadelat, K., Ray, D. W., Clément, A., Tabary, O., & Rouzic, P. L. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.01.005 · Cited by 27
Samarut, E., Amal, I., Markov, G. V., Stote, R., Dejaegere, A., Laudet, V., & Rochette-Egly, C. (2011) · Molecular Biology and Evolution · doi:10.1093/molbev/msr035 · Cited by 26
Self-citationThe Function and Evolution of Nuclear Receptors in Insect Embryonic Development
Jarvela, A. M. C., & Pick, L. (2017) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2017.01.003 · Cited by 26
Rap2 regulates androgen sensitivity in human prostate cancer cells
Bigler, D., Gioeli, D. G., Conaway, M. R., Weber, M. J., & Theodorescu, D. (2007) · The Prostate · doi:10.1002/pros.20644 · Cited by 26
Zhang, F., Liu, F., Yan, M., Ji, H., Hu, L., Li, X., Qian, J., He, X., Zhang, L., Shen, A., et al. (2009) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2009.10.016 · Cited by 25
Evolution of Nuclear Receptors in Insects
Bonneton, F., & Laudet, V. (2011) · Elsevier eBooks · doi:10.1016/b978-0-12-384749-2.10006-8 · Cited by 28
Andela, V. B., & Rosier, R. N. (2004) · Molecular Cancer · doi:10.1186/1476-4598-3-8 · Cited by 25
Phosphorylation Control of Nuclear Receptors
Lalevée, S., Ferry, C., & Rochette‐Egly, C. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-738-9_15 · Cited by 24
Self-citationLoss of FKBP5 impedes adipocyte differentiation under both normoxia and hypoxic stress
Zhang, L., Qiu, B., Wang, T., Wang, J., Liu, M. R., Xu, Y., Wang, C., Deng, R., Williams, K. E., Yang, Z., et al. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.02.126 · Cited by 23
Retinoic acid and arsenic trioxide cooperate for apoptosis through phosphorylated RXR alpha
Tarrade, A., Bastien, J., Bruck, N., Bauer, A., Gianni, M., & Rochette-Egly, C. (2005) · Oncogene · doi:10.1038/sj.onc.1208402 · Cited by 23
Self-citationMinireview: What is Known about SUMOylation Among NR4A Family Members?
Dodat, F., Mader, S., & Lévesque, D. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167212 · Cited by 22
Ross, A. C. (2010) · Humana Press eBooks · doi:10.1007/978-1-60761-627-6_16 · Cited by 22
Chen, L., Giorgianni, F., & Beranová-Giorgianni, Š. (2009) · Journal of Proteome Research · doi:10.1021/pr900338q · Cited by 22
The Juvenile Hormone Receptor and Molecular Mechanisms of Juvenile Hormone Action
Dubrovsky, E. B., & Bernardo, T. J. (2014) · Advances in insect physiology · doi:10.1016/b978-0-12-417010-0.00004-5 · Cited by 22
Xie, G., Zhou, Y., Tu, X., Ye, X., Xu, L., Xiao, Z., Wang, Q., Wang, X., Du, M., Chen, Z., et al. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.11.012 · Cited by 19
Fenne, I. S., Hoang, T., Flågeng, M. H., Sagen, J. V., Lien, E. A., & Mellgren, G. (2008) · Endocrinology · doi:10.1210/en.2008-0037 · Cited by 20
Vitamin E activates CRABP‐II gene expression in cultured human fibroblasts, role of protein kinase C
Gimeno, A., Zaragozá, R., Vinã, J. R., & Miralles, V. J. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.05.073 · Cited by 20
Zhou, Q., Apionishev, S., & Kalderon, D. (2006) · Genetics · doi:10.1534/genetics.106.061036 · Cited by 21
RXRα modulates hepatic stellate cell activation and liver fibrosis by targeting CaMKKβ–AMPKα axis
Cai, L., Yin, M., Peng, S., Fen, L., Lai, L., Zhang, X., Xie, L., Wang, C., Zhou, H., Zhan, Y., et al. (2025) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2025.05.023 · Cited by 21
Zhang, D., Song, Y., Kong, P., Xu, X., Gao, Y., Dou, Y., Weng, L., Wang, X., Lin, Y.-L., Zhang, F., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04239-w · Cited by 19
Uchibe, K., Son, J., Larmour, C., Pacifici, M., Enomoto‐Iwamoto, M., & Iwamoto, M. (2016) · Journal of Orthopaedic Research® · doi:10.1002/jor.23347 · Cited by 19
Pulmonary Parenchymal Injuries
Tomlanovich, M. C. (1983) · Emergency Medicine Clinics of North America · doi:10.1016/s0733-8627(20)30795-1 · Cited by 20
Retinoids and TRAIL: Two Cooperating Actors to Fight Against Cancer
Altucci, L., & Gronemeyer, H. (2004) · Vitamins and hormones · doi:10.1016/s0083-6729(04)67017-8 · Cited by 19
Nutrigenomics and Proteomics in Health and Disease
Mine, Y., Miyashita, K., & Shahidi, F. (2009) · Wiley eBooks · doi:10.1002/9780813807263 · Cited by 18
Protein Multifunctionality: Principles and Mechanisms
Zaretsky, J. Z., & Wreschner, D. H. (2008) · Translational Oncogenomics · doi:10.4137/tog.s657 · Cited by 18
An improved high throughput protein-protein interaction assay for nuclear hormone receptors
Goodson, M. L., Farboud, B., & Privalsky, M. L. (2007) · Nuclear Receptor Signaling · doi:10.1621/nrs.05002 · Cited by 18
Aswani, B. S., Hegde, M., Vishwa, R., Alqahtani, M. S., Abbas, M., Almubarak, H. A., Sethi, G., & Kunnumakkara, A. B. (2024) · Military Medical Research · doi:10.1186/s40779-024-00564-1 · Cited by 17
Thyroid-Stimulating Hormone Increases HNF-4α Phosphorylation via cAMP/PKA Pathway in the Liver
Song, Y., Zheng, D., Zhao, M., Qin, Y., Wang, T., Wanjia, X., Gao, L., & Zhao, J. (2015) · Scientific Reports · doi:10.1038/srep13409 · Cited by 16
Huffman, J. N., Hoffmann, C., & Taylor, G. T. (2017) · World Journal of Diabetes · doi:10.4239/wjd.v8.i2.45 · Cited by 16
Ermisch, M., Firla, B., & Steinhilber, D. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.04.046 · Cited by 16
Noreault, T. L., Fellows, A. M., Jacobs, J. M., Trask, H. W., Strom, S. C., Evans, R. M., Wrighton, S. A., Sinclair, P. R., Sinclair, J. F., & Nichols, R. C. (2012) · International Immunopharmacology · doi:10.1016/j.intimp.2012.01.008 · Cited by 15
Cao, Z.-G., Xu, X., Xue, Y., & Zhao, S. (2014) · Współczesna Onkologia · doi:10.5114/wo.2014.40456 · Cited by 15
Expression, purification and characterization of methyl DNA binding protein from Bombyx mori
Uno, T., Nomura, Y., Nakamura, M., Nakao, A., Tajima, S., Kanamaru, K., Yamagata, H., & Iwanaga, Y. (2005) · Journal of Insect Science · doi:10.1093/jis/5.1.8 · Cited by 16
Phosphorylation of nuclear receptors: Novelty and therapeutic implications
Shindo, S., Kakizaki, S., Sakaki, T., Kawasaki, Y., Sakuma, T., Negishi, M., & Shizu, R. (2023) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2023.108477 · Cited by 14
Zhang, H., Li, X., Wang, X., Xu, J., Elefant, F., & Wang, J. (2023) · Animal Models and Experimental Medicine · doi:10.1002/ame2.12313 · Cited by 15
McCall, P., Adams, C. E., Willder, J. M., Bennett, L., Qayyum, T., Orange, C., Underwood, M., & Edwards, J. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140816656 · Cited by 14
Involvement of ZIP/p62 in the regulation of PPARα transcriptional activity by p38-MAPK
Diradourian, C., May, C. L., Caüzac, M., Girard, J. R., Burnol, A., & Pégorier, J. P. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2008.02.002 · Cited by 15
Extracellular signal-regulated kinase-2 phosphorylates RORα4 in vitro
Lechtken, A., Hörnig, M., Werz, O., Corvey, N., Zündorf, I., Dingermann, T., Brandes, R. P., & Steinhilber, D. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.05.016 · Cited by 14
Up‐Regulation of α1A‐Adrenoceptors in Rat Mesenteric Artery Involves Intracellular Signal Pathways
Cao, Y., Xu, C., Luo, G., & Edvinsson, L. I. (2006) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/j.1742-7843.2006.pto_240.x · Cited by 13
Oxombre, B., Kouach, M., Moerman, E., Formstecher, P., & Laine, B. (2004) · Biochemical Journal · doi:10.1042/bj20040473 · Cited by 13
Flajollet, S., Staels, B., & Lefèbvre, P. (2013) · Hormone Molecular Biology and Clinical Investigation · doi:10.1515/hmbci-2013-0013 · Cited by 12
Bour, G., Taneja, R., & Rochette‐Egly, C. (2006) · Advances in developmental biology · doi:10.1016/s1574-3349(06)16007-x · Cited by 16
Self-citationDuplus, E., Gras, C., Soubeyre, V., Vodjdani, G., Lemaigre-Dubreuil, Y., & Brugg, B. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05074.x · Cited by 15
Mochizuki, K., Sakaguchi, N., Takabe, S., & Goda, T. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.06.012 · Cited by 12
Mey, J. (2017) · doi:10.1002/9783527697274.ch16 · Cited by 12
Pondugula, S. R., Tong, A. A., Wu, J., Cui, J., & Chen, T. (2010) · Drug Metabolism and Disposition · doi:10.1124/dmd.110.032128 · Cited by 11
Raingeard, D., Bilbao, E., Sáez-Morquecho, C., de Cerio, O. D., Orbea, A., Cancio, I., & Cajaraville, M. P. (2009) · Marine Genomics · doi:10.1016/j.margen.2009.10.004 · Cited by 11
Huwait, E., Singh, N., Michael, D., Davies, T., Moss, J. W. E., & Ramji, D. (2015) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25157 · Cited by 10
Eleraky, A. F., Helal, G. K., Elshafie, M. F., & Ismail, R. S. (2021) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/1440-1681.13486 · Cited by 9
Metadata
- Authors
- Rochette-Egly, C.
- Venue
- Cellular Signalling
- Publisher
- Elsevier BV
- Published
- 2003-04
- Volume
- 15
- Issue
- 4
- Pages
- 355-366
- ISSN
- 0898-6568 (ISSN-L)
- OpenAlex
- W2056128228
- Cited by
- 291
- References
- 136
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 2 · 2023: 4 · 2022: 4 · 2021: 7 · 2020: 2 · 2019: 7 · 2018: 5 · 2017: 8 · 2016: 7 · 2015: 12 · 2014: 15 · 2013: 21 · 2012: 10
- FWCI
- 2.14
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cellular Signalling (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Estrogen and related hormone effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- nuclear receptors, phosphorylation, transcriptional regulation, transcriptional coactivator, ligand-binding domain, DNA-binding domain, mitogen-activated protein kinase, Akt, protein kinase A, protein kinase C, CDK7, TFIIH, transcription termination, ligand dissociation, cancer
- MeSH terms
- Animals, Cell Nucleus, DNA-Binding Proteins, Hormones, Humans, Neoplasms, Phosphorylation, Protein Binding, RNA, Messenger, Transcription, Genetic, Signal Transduction, Down-Regulation, Up-Regulation, Protein Serine-Threonine Kinases, Receptors, Cytoplasmic and Nuclear
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