Cited by 802Estrogen and related hormone effectsGenomics and Chromatin DynamicsDiffusion and Search Dynamics

The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.

The Glucocorticoid Receptor: Rapid Exchange with Regulatory Sites in Living Cells

McNally, James G., Müller, Waltraud G., Walker, Dawn, Wolford, Ronald, Hager, Gordon L.·2000·Science

Open this paper in CoChat — free account

Abstract

Steroid receptors bind to site-specific response elements in chromatin and modulate gene expression in a hormone-dependent fashion. With the use of a tandem array of mouse mammary tumor virus reporter elements and a form of glucocorticoid receptor labeled with green fluorescent protein, targeting of the receptor to response elements in live mouse cells was observed. Photobleaching experiments provide direct evidence that the hormone-occupied receptor undergoes rapid exchange between chromatin and the nucleoplasmic compartment. Thus, the interaction of regulatory proteins with target sites in chromatin is a more dynamic process than previously believed.

Integrity signals

Registry

Crossref · 10.1126/science.287.5456.1262

Cites

32 of 32 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Nuclear Receptor Coregulators: Cellular and Molecular Biology
McKenna, N. J., Lanz, R. B., & O’Malley, B. W. (1999) · Endocrine Reviews · doi:10.1210/edrv.20.3.0366 · Cited by 1,941
Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer
Heim, R., & Tsien, R. Y. (1996) · Current Biology · doi:10.1016/s0960-9822(02)00450-5 · Cited by 1,490
Steroid receptor coactivator-1 is a histone acetyltransferase
Spencer, T. E., Jenster, G. W., Burcin, M. M., Allis, C. D., Zhou, J., Mizzen, C. A., McKenna, N. J., Oñate, S. A., Tsai, S. Y., Tsai, M., et al. (1997) · Nature · doi:10.1038/38304 · Cited by 1,242
Regulation of Transcription by a Protein Methyltransferase
Chen, D., Ma, H., Hong, H., Koh, S. S., Huang, S., Schurter, B. T., Aswad, D. W., & Stallcup, M. R. (1999) · Science · doi:10.1126/science.284.5423.2174 · Cited by 1,214
Coactivator and corepressor complexes in nuclear receptor function
Xu, L., Glass, C. K., & Rosenfeld, M. G. (1999) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(99)80021-5 · Cited by 909
Histone Deacetylase Activity Is Required for Full Transcriptional Repression by mSin3A
Hassig, C. A., Fleischer, T. C., Billin, A. N., Schreiber, S. L., & Ayer, D. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80214-7 · Cited by 740
Sequence‐specific positioning of nucleosomes over the steroid‐inducible MMTV promoter.
Richard-Foy, H., & Hager, G. L. (1987) · The EMBO Journal · doi:10.1002/j.1460-2075.1987.tb02507.x · Cited by 594
A human homologue of Saccharomyces cerevisiae SNF2/SWI2 and Drosophila brm genes potentiates transcriptional activation by the glucocorticoid receptor.
Muchardt, C., & Yaniv, M. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06112.x · Cited by 588
Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex
Fryer, C. J., & Archer, T. K. (1998) · Nature · doi:10.1038/30032 · Cited by 511
Roles of SWI1, SWI2, and SWI3 Proteins for Transcriptional Enhancement by Steroid Receptors
Yoshinaga, S. K., Peterson, C. L., Herskowitz, I., & Yamamoto, K. R. (1992) · Science · doi:10.1126/science.1360703 · Cited by 477

Flagged first, then by citations

Show all 32 references

Research works printed but not linked: 1

Ostrowski M. C., Richard-Foy H., Wolford R. G., Berard D. S., Hager G. L., Mol. Cell. Biol. 3, 2045 (1983).

Sorted by citations

Items 201–300 of 799

Functional Domain and Motif Analyses of Androgen Receptor Coregulator ARA70 and Its Differential Expression in Prostate Cancer
Hu, Y., Yeh, S., Yeh, S.-D., Sampson, E. R., Huang, J., Li, P., Hsu, C.-L., Ting, H., Lin, H., Wang, L., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401781200 · Cited by 98
Quantifying transcription factor kinetics: At work or at play?
Mueller, F., Stasevich, T. J., Mazza, D., & McNally, J. G. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.833891 · Cited by 98
Human Ccr4‐Not complex is a ligand‐dependent repressor of nuclear receptor‐mediated transcription
Winkler, G. S., Mulder, K. W., Bardwell, V. J., Kalkhoven, E., & Timmers, H. T. M. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601194 · Cited by 98
Accessory Factors Facilitate the Binding of Glucocorticoid Receptor to the Phosphoenolpyruvate Carboxykinase Gene Promoter
Stafford, J. M., Wilkinson, J. C., Beechem, J., & Granner, D. K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105370200 · Cited by 96
Highly Compacted Chromatin Formed In Vitro Reflects the Dynamics of Transcription Activation In Vivo
Li, G., Margueron, R., Hu, G., Stokes, D. L., Wang, Y.-H., & Reinberg, D. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.042 · Cited by 96
Quantifying effects of ligands on androgen receptor nuclear translocation, intranuclear dynamics, and solubility
Marcelli, M., Stenoien, D. L., Szafran, A. T., Simeoni, S., Agoulnik, I. U., Weigel, N. L., Moran, T., Mikic, I., Price, J. H., & Mancini, M. A. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20593 · Cited by 96
Visualization of Glucocorticoid Receptor and Mineralocorticoid Receptor Interactions in Living Cells with GFP-Based Fluorescence Resonance Energy Transfer
Nishi, M., Tanaka, M., Matsuda, K., Sunaguchi, M., & Kawata, M. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.5495-03.2004 · Cited by 96
Glucocorticoid receptor-mediated chromatin remodeling in vivo
Deroo, B. J., & Archer, T. (2001) · Oncogene · doi:10.1038/sj.onc.1204328 · Cited by 95
The Development and Enhancement of FRAP as a Key Tool for Investigating Protein Dynamics
Lippincott‐Schwartz, J., Snapp, E. L., & Phair, R. D. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2018.08.007 · Cited by 94
Dynamics of nuclear receptor movement and transcription
Hager, G. L., Nagaich, A. K., Johnson, T. A., Walker, D. A., & John, S. (2003) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/j.bbaexp.2003.09.016 · Cited by 94
Proinflammatory Cytokines Enhance Estrogen-dependent Expression of the Multidrug Transporter Gene ABCG2 through Estrogen Receptor and NFκB Cooperativity at Adjacent Response Elements
Pradhan, M., Bembinster, L. A., Baumgarten, S. C., & Frasor, J. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.155309 · Cited by 92
Cross-Validating FRAP and FCS to Quantify the Impact of Photobleaching on In Vivo Binding Estimates
Stasevich, T. J., Mueller, F., Michelman‐Ribeiro, A., Rosales, T., Knutson, J. R., & McNally, J. G. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.08.059 · Cited by 92
Altered subcellular distribution of MSK1 induced by glucocorticoids contributes to NF‐κB inhibition
Beck, I. M. E., Berghe, W. V., Vermeulen, L., Bougarne, N., Cruyssen, B. V., Haegeman, G., & Bosscher, K. D. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.95 · Cited by 92
A matter of time — How transient transcription factor interactions create dynamic gene regulatory networks
Swift, J., & Coruzzi, G. M. (2016) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2016.08.007 · Cited by 92
Regulation of the RNA polymerase II pre-initiation complex by its associated coactivators
Malik, S., & Roeder, R. G. (2023) · Nature Reviews Genetics · doi:10.1038/s41576-023-00630-9 · Cited by 96
Acetylation of Steroidogenic Factor 1 Protein Regulates Its Transcriptional Activity and Recruits the Coactivator GCN5
Jacob, A. L. J., Lund, J., Martı́nez, P., & Hedin, L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104427200 · Cited by 90
The androgen receptor ligand-binding domain stabilizes DNA binding in living cells
Farla, P., Hersmus, R., Geverts, B., Mari, P., Nigg, A. L., Dubbink, H. J., Trapman, J., & Houtsmuller, A. B. (2004) · Journal of Structural Biology · doi:10.1016/j.jsb.2004.01.002 · Cited by 90
Chromatin Remodeling Complexes Interact Dynamically with a Glucocorticoid Receptor–regulated Promoter
Johnson, T. A., Elbi, C., Parekh, B. S., Hager, G. L., & John, S. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-02-0123 · Cited by 90
Aldosterone: Its Receptor, Target Genes, and Actions
Pearce, D., Bhargava, A., & Cole, T. J. (2003) · Vitamins and hormones · doi:10.1016/s0083-6729(03)01002-1 · Cited by 93
Gene regulation and large-scale chromatin organization in the nucleus
Dillon, N. (2006) · Chromosome Research · doi:10.1007/s10577-006-1027-8 · Cited by 88
Quantitation of GFP-fusion proteins in single living cells
Dundr, M., McNally, J. G., Cohen, J., & Misteli, T. (2002) · Journal of Structural Biology · doi:10.1016/s1047-8477(02)00521-x · Cited by 89
Imaging Molecular Interactions in Living Cells
Day, R. N., & Schaufele, F. (2005) · Molecular Endocrinology · doi:10.1210/me.2005-0028 · Cited by 91
Structure and Dynamic Properties of a Glucocorticoid Receptor-Induced Chromatin Transition
Fletcher, T. M., Ryu, B., Baumann, C. T., Warren, B. S., Fragoso, G., John, S., & Hager, G. L. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.17.6466-6475.2000 · Cited by 89
Dissociation Time from DNA Determines Transcriptional Function in a STAT1 Linker Mutant
Yang, E., Henriksen, M. A., Schaefer, O., Zakharova, N., & Darnell, J. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112038200 · Cited by 88
STAT1 from the cell membrane to the DNA
Lillemeier, B. F., Köster, M., & Kerr, I. M. (2001) · The EMBO Journal · doi:10.1093/emboj/20.10.2508 · Cited by 88
Dissecting the binding mechanism of the linker histone in live cells: an integrated FRAP analysis
Stasevich, T. J., Mueller, F., Brown, D. T., & McNally, J. G. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.24 · Cited by 87
Dynamic output and control of the hypothalamic-pituitary-adrenal axis in critical illness and major surgery
Gibbison, B., Angelini, G. D., & Lightman, S. L. (2013) · British Journal of Anaesthesia · doi:10.1093/bja/aet077 · Cited by 87
Subnuclear Distribution of Progesterone Receptors A and B in Normal and Malignant Endometrium
Arnett-Mansfield, R. L., DeFazio, A., Mote, P. A., & Clarke, C. L. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2003-031111 · Cited by 86
Molecular basis for gene-specific transactivation by nuclear receptors
Aagaard, M. M., Siersbæk, R., & Mandrup, S. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.12.018 · Cited by 93
Histone H1 and the dynamic regulation of chromatin function
Brown, D. T. (2003) · Biochemistry and Cell Biology · doi:10.1139/o03-049 · Cited by 86
Coactivator cross-talk specifies transcriptional outputPreprint
Marr, M. T., Isogai, Y., Wright, K. J., & Tjian, R. (2006) · Genes & Development · doi:10.1101/gad.1418806 · Cited by 86
Of JAKs, STATs, blind watchmakers, jeeps and trains
Kerr, I. M., Costa‐Pereira, A. P., Lillemeier, B. F., & Strobl, B. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00411-3 · Cited by 84
Modulation of RNA Polymerase Assembly Dynamics in Transcriptional Regulation
Gorski, S. A., Snyder, S. K., John, S., Grummt, I., & Misteli, T. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.04.021 · Cited by 85
HLA-DM targets the hydrogen bond between the histidine at position β81 and peptide to dissociate HLA-DR–peptide complexes
Narayan, K., Chou, C.-L., Kim, A., Hartman, I. Z., Dalai, S. K., Khoruzhenko, S., & Sadegh‐Nasseri, S. (2006) · Nature Immunology · doi:10.1038/ni1414 · Cited by 85
Fluorescence Recovery after Photobleaching: Application to Nuclear Proteins
Houtsmuller, A. B. (2005) · Advances in biochemical engineering, biotechnology · doi:10.1007/b102214 · Cited by 88
Complexity in Transcription Control at the Activation Domain–Mediator Interface
Balamotis, M. A., Pennella, M. A., Stevens, J. L., Wasylyk, B., Belmont, A. S., & Berk, A. J. (2009) · Science Signaling · doi:10.1126/scisignal.1164302 · Cited by 84
Novel N-Terminal Variant of Human VDR
Sunn, K. L., Cock, T., Crofts, L. A., Eisman, J. A., & Gardiner, E. M. (2001) · Molecular Endocrinology · doi:10.1210/me.15.9.1599 · Cited by 82
A contemporary understanding of progesterone receptor function
Li, X., Lonard, D. M., & O’Malley, B. W. (2004) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2004.04.007 · Cited by 82
Establishing the Role of PPARβ/δ in Carcinogenesis
Peters, J. M., Gonzalez, F. J., & Müller, R. (2015) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.09.004 · Cited by 81
A gradient of glucocorticoid sensitivity among helper T cell cytokines
Banuelos, J., & Lu, N. (2016) · Cytokine & growth factor reviews · doi:10.1016/j.cytogfr.2016.05.002 · Cited by 70
Continuous recycling: a mechanism for modulatory signal transduction.
Freeman, B. C., & Yamamoto, K. R. (2001) · TIBS -Trends in Biochemical Sciences. Regular ed · doi:10.1016/s0968-0004(01)01834-5 · Cited by 81
Nucleocytoplasmic Shuttling of the Thyroid Hormone Receptorα
Bunn, C. F., Neidig, J. A., Freidinger, K. E., Stankiewicz, T. A., Weaver, B. S., Mcgrew, J. R., & Allison, L. A. (2001) · Molecular Endocrinology · doi:10.1210/mend.15.4.0619 · Cited by 80
On the spontaneous stochastic dynamics of a single gene: complexity of the molecular interplay at the promoter
Coulon, A., Gandrillon, O., & Beslon, G. (2010) · BMC Systems Biology · doi:10.1186/1752-0509-4-2 · Cited by 78
Mechanistic Insights Into the Interaction Between Transcription Factors and Epigenetic Modifications and the Contribution to the Development of Obesity
Huang, Q., Ma, C., Chen, L., Luo, D., Chen, R., & Liang, F. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00370 · Cited by 78
A Reaction-Diffusion Model to Study RNA Motion by Quantitative Fluorescence Recovery after Photobleaching
Braga, J., McNally, J. G., & Carmo‐Fonseca, M. (2007) · Biophysical Journal · doi:10.1529/biophysj.106.096693 · Cited by 78
Modifying chromatin to permit steroid hormone receptor-dependent transcription
Kinyamu, H. K., & Archer, T. (2003) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/j.bbaexp.2003.09.015 · Cited by 79
Alternative Effects of the Ubiquitin-Proteasome Pathway on Glucocorticoid Receptor Down-Regulation and Transactivation Are Mediated by CHIP, an E3 Ligase
Wang, X., & DeFranco, D. B. (2005) · Molecular Endocrinology · doi:10.1210/me.2004-0383 · Cited by 77
Corepressor Recruitment by Agonist-Bound Nuclear Receptors
White, J. H., Fernandes, I., Mader, S., & Yang, X. (2004) · Vitamins and hormones · doi:10.1016/s0083-6729(04)68004-6 · Cited by 85
Clusters of regulatory signals for RNA polymerase II transcription associated with Alu family repeats and CpG islands in human promoters
Sl, O., Babich, V., Kazakov, V. I., Usmanova, N. M., Kropotov, A., & Tomilin, N. (2003) · Genomics · doi:10.1016/j.ygeno.2003.11.001 · Cited by 77
Dynamic chromatin technologies: from individual molecules to epigenomic regulation in cells
Cuvier, O., & Fierz, B. (2017) · Nature Reviews Genetics · doi:10.1038/nrg.2017.28 · Cited by 77
Proteolytic turnover of the Gal4 transcription factor is not required for function in vivo
Nalley, K., Johnston, S. A., & Kodadek, T. (2006) · Nature · doi:10.1038/nature05067 · Cited by 82
Changes in Attitude, Changes in Latitude: Nuclear Receptors Remodeling Chromatin to Regulate Transcription
Chen, J., Kinyamu, H. K., & Archer, T. (2005) · Molecular Endocrinology · doi:10.1210/me.2005-0192 · Cited by 76
Nuclear receptors, coactivators and chromatin: new approaches, new insights
Lee, K. C., & Kraus, W. L. (2001) · Trends in Endocrinology and Metabolism · doi:10.1016/s1043-2760(01)00392-7 · Cited by 76
Glucocorticoid Receptor Activation of the Ciz1-Lcn2 Locus by Long Range Interactions
Hakim, O., John, S., Ling, J. Q., Biddie, S. C., Hoffman, A. R., & Hager, G. L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.c800212200 · Cited by 75
Endocrine disruptors of sex hormone activities
Varticovski, L., Stavreva, D. A., McGowan, A., Raziuddin, R., & Hager, G. L. (2021) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2021.111415 · Cited by 75
Coactivators and nuclear receptor transactivation
Wolf, I. M., Heitzer, M. D., Grubisha, M. J., & DeFranco, D. B. (2008) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21755 · Cited by 73
Glucocorticoid receptor dynamics and gene regulation
Biddie, S. C., & Hager, G. L. (2008) · Stress · doi:10.1080/10253890802506409 · Cited by 72
The Presence of Both the Amino- and Carboxyl-Terminal Domains in the AR Is Essential for the Completion of a Transcriptionally Active Form with Coactivators and Intranuclear Compartmentalization Common to the Steroid Hormone Receptors: A Three-Dimensional Imaging Study
Saitoh, M., Takayanagi, R., Goto, K., Fukamizu, A., Tomura, A., Yanase, T., & Nawata, H. (2002) · Molecular Endocrinology · doi:10.1210/me.16.4.694 · Cited by 73
Repression of transcription by the glucocorticoid receptor: A parsimonious model for the genomics era
Gerber, A. N., Newton, R. C., & Sasse, S. K. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100687 · Cited by 75
Intranuclear organization and function of the androgen receptor
Black, B. E., & Paschal, B. M. (2004) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2004.09.006 · Cited by 78
Cdt1 associates dynamically with chromatin throughout G1 and recruits Geminin onto chromatin
Xouri, G., Squire, A., Dimaki, M., Geverts, B., Verveer, P. J., Taraviras, S. L., Nishitani, H., Houtsmuller, A. B., Bastiaens, P. I. H., & Lygerou, Z. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601597 · Cited by 72
Genome-wide footprinting: ready for prime time?
Sung, M., Baek, S., & Hager, G. L. (2016) · Nature Methods · doi:10.1038/nmeth.3766 · Cited by 71
Fluorescence Recovery After Photobleaching (FRAP) to Study Nuclear Protein Dynamics in Living Cells
van Royen, M. E., Farla, P., Mattern, K. A., Geverts, B., Trapman, J., & Houtsmuller, A. B. (2008) · Methods in molecular biology · doi:10.1007/978-1-60327-461-6_20 · Cited by 73
Protein dynamics in the nuclear compartment
Hager, G. L., Elbi, C., & Becker, M. (2002) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(02)00278-2 · Cited by 72
Unraveling the molecular interactions involved in phase separation of glucocorticoid receptor
Stortz, M., Pecci, A., Presman, D. M., & Levi, V. (2020) · BMC Biology · doi:10.1186/s12915-020-00788-2 · Cited by 72
Fibroblast Growth Factor Receptor-1 (FGFR1) Nuclear Dynamics Reveal a Novel Mechanism in Transcription Control
Dunham-Ems, S. M., Lee, Y., Stachowiak, E. K., Pudavar, H. E., Claus, P., Prasad, P. N., & Stachowiak, M. K. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-06-0600 · Cited by 71
Protein 14-3-3σ Interacts with and Favors Cytoplasmic Subcellular Localization of the Glucocorticoid Receptor, Acting as a Negative Regulator of the Glucocorticoid Signaling Pathway
Kino, T., Souvatzoglou, E., Martino, M. U. D., Tsopanomihalu, M., Wan, Y., & Chrousos, G. P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302818200 · Cited by 71
Molecular Architecture of Transcription Factor Hotspots in Early Adipogenesis
Siersbæk, R., Baek, S., Rabiee, A., Nielsen, R., Traynor, S., Clark, N., Sandelin, A., Jensen, O. N., Sung, M., Hager, G. L., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.04.043 · Cited by 65
Molecular dynamics of ultradian glucocorticoid receptor action
Conway-Campbell, B. L., Pooley, J. R., Hager, G. L., & Lightman, S. L. (2011) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.08.014 · Cited by 67
New and improved glucocorticoid receptor ligands
Miner, J. N., Hong, M. H., & Negro-Vilar, A. F. (2005) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.14.12.1527 · Cited by 70
DNA damage repair: anytime, anywhere?
Essers, J., Vermeulen, W., & Houtsmuller, A. B. (2006) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2006.03.004 · Cited by 67
Complex genomic interactions in the dynamic regulation of transcription by the glucocorticoid receptor
Miranda, T. B., Morris, S. A., & Hager, G. L. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.03.002 · Cited by 69
Imaging in situ protein–DNA interactions in the cell nucleus using FRET–FLIM
Crémazy, F. G. E., Manders, E. M. M., Bastiaens, P. I. H., Kramer, G., Hager, G. L., VANMUNSTER, E., Verschure, P. J., Gadella, T. W. J., & VANDRIEL, R. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.06.007 · Cited by 67
Phosphorylation of Estrogen Receptor α at Serine 118 Directs Recruitment of Promoter Complexes and Gene-Specific Transcription
Duplessis, T., Williams, C. C., Hill, S. M., & Rowan, B. G. (2011) · Endocrinology · doi:10.1210/en.2010-1281 · Cited by 67
Phosphorylation of Activation Function-1 Regulates Proteasome-Dependent Nuclear Mobility and E6-Associated Protein Ubiquitin Ligase Recruitment to the Estrogen Receptor β
Picard, N., Charbonneau, C., Sanchez, M., Licznar, A., Busson, M., Lazennec, G., & Tremblay, A. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0281 · Cited by 70
Binding and interplay of HMG proteins on chromatin: Lessons from live cell imaging
Catez, F., & Hock, R. (2010) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2009.11.001 · Cited by 66
A ubiquitin-selective AAA-ATPase mediates transcriptional switching by remodelling a repressor–promoter DNA complex
Wilcox, A. J., & Laney, J. D. (2009) · Nature Cell Biology · doi:10.1038/ncb1997 · Cited by 67
Thyroid Hormone-Regulated Target Genes Have Distinct Patterns of Coactivator Recruitment and Histone Acetylation
Liu, Y., Xia, X., Fondell, J. D., & Yen, P. M. (2005) · Molecular Endocrinology · doi:10.1210/me.2005-0101 · Cited by 66
Glucocorticoid receptor quaternary structure drives chromatin occupancy and transcriptional outcomePreprint
Paakinaho, V., Johnson, T. A., Presman, D. M., & Hager, G. L. (2019) · Genome Research · doi:10.1101/gr.244814.118 · Cited by 70
Transcription Factor Dynamics: One Molecule at a Time
Wagh, K., Stavreva, D. A., Upadhyaya, A., & Hager, G. L. (2023) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-022823-013847 · Cited by 68
Marking time: The dynamic role of chromatin and covalent modification in transcription
Reid, G., Gallais, R., & Métivier, R. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.08.028 · Cited by 68
The HSP90 Molecular Chaperone Cycle Regulates Cyclical Transcriptional Dynamics of the Glucocorticoid Receptor and Its Coregulatory Molecules CBP/p300 During Ultradian Ligand Treatment
Conway-Campbell, B. L., George, C. L., Pooley, J. R., Knight, D. M., Norman, M. R., Hager, G. L., & Lightman, S. L. (2011) · Molecular Endocrinology · doi:10.1210/me.2010-0073 · Cited by 67
Quantitation of Glucocorticoid Receptor DNA-Binding Dynamics by Single-Molecule Microscopy and FRAP
Groeneweg, F. L., van Royen, M. E., Fenz, S. F., Keizer, V. I. P., Geverts, B., Prins, J., de Kloet, E. R., Houtsmuller, A. B., Schmidt, T. S., & Schaaf, M. J. M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0090532 · Cited by 63
Tuning Transcription Factor Availability through Acetylation-Mediated Genomic Redistribution
Louphrasitthiphol, P., Siddaway, R., Loffreda, A., Pogenberg, V., Friedrichsen, H. J., Schepsky, A., Zeng, Z., Lu, M. M., Strub, T., Freter, R., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.05.025 · Cited by 67
Following the tracks: How transcription factor binding dynamics control transcription
de Jonge, W. J., Patel, H., Meeussen, J. V. W., & Lenstra, T. L. (2022) · Biophysical Journal · doi:10.1016/j.bpj.2022.03.026 · Cited by 62
Transient, Ligand-Dependent Arrest of the Androgen Receptor in Subnuclear Foci Alters Phosphorylation and Coactivator Interactions
Black, B. E., Vitto, M. J., Gioeli, D. G., Spencer, A., Afshar, N., Conaway, M. R., Weber, M. J., & Paschal, B. M. (2003) · Molecular Endocrinology · doi:10.1210/me.2003-0145 · Cited by 63
Vitamin D receptor and retinoid X receptor interactions in motion
Bársony, J., & Prüfer, K. (2002) · Vitamins and hormones · doi:10.1016/s0083-6729(02)65071-x · Cited by 63
Chromatin dynamics and the evolution of alternate promoter states
Hager, G. L., Elbi, C., Johnson, T. A., Voss, T. C., Nagaich, A. K., Schiltz, R. L., Qiu, Y., & John, S. (2006) · Chromosome Research · doi:10.1007/s10577-006-1030-0 · Cited by 63
An Alternative Splicing Variant of the Selenoprotein Thioredoxin Reductase Is a Modulator of Estrogen Signaling
Damdimopoulos, A. E., Miranda‐Vizuete, A., Treuter, E., Gustafsson, J.-Α., & Spyrou, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402753200 · Cited by 63
A guide to changing paradigms of glucocorticoid receptor function—a model system for genome regulation and physiology
Vettorazzi, S., Nalbantoglu, D., Gebhardt, J. C. M., & Tuckermann, J. P. (2021) · FEBS Journal · doi:10.1111/febs.16100 · Cited by 62
Transcript elongation on a nucleoprotein template
Hartzog, G. A., Speer, J. L., & Lindstrom, D. L. (2002) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(02)00458-x · Cited by 62
Subnuclear Localization of C/EBPβ Is Regulated by Growth Hormone and Dependent on MAPK
Pilipuk, G. P., Galigniana, M. D., & Schwartz, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305182200 · Cited by 62
A Necessary Good: Nuclear Hormone Receptors and Their Chromatin Templates
Urnov, F. D., & Wolffe, A. P. (2001) · Molecular Endocrinology · doi:10.1210/mend.15.1.0589 · Cited by 62
Re-defining the chromatin loop domain
Heng, H. H., Krawetz, S. A., Lu, W., Bremer, S. W., Liu, G., & Ye, C. J. (2001) · Cytogenetic and Genome Research · doi:10.1159/000056977 · Cited by 61
Engineered chromosome regions with altered sequence composition demonstrate hierarchical large-scale folding within metaphase chromosomes
Strukov, Y. G., Wang, Y., & Belmont, A. S. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200303098 · Cited by 60
The neuroendocrine control of the innate immune system in health and brain diseases
Bellavance, M., & Rivest, S. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01129.x · Cited by 61
Single-molecule imaging correlates decreasing nuclear volume with increasing TF-chromatin associations during zebrafish development
Reisser, M., Palmer, A., Popp, A. P., Jahn, C., Weidinger, G., & Gebhardt, J. C. M. (2018) · Nature Communications · doi:10.1038/s41467-018-07731-8 · Cited by 60
Dissociation of Steroid Receptor Coactivator 1 and Nuclear Receptor Corepressor Recruitment to the Human Glucocorticoid Receptor by Modification of the Ligand-Receptor Interface: The Role of Tyrosine 735
Stevens, A., Garside, H., Berry, A. A., Waters, C. E., White, A. E., & Ray, D. W. (2003) · Molecular Endocrinology · doi:10.1210/me.2002-0320 · Cited by 60
Structural and molecular determinants of mineralocorticoid receptor signalling
Großmann, C., Almeida‐Prieto, B., Nolze, A., & de la Rosa, D. Á. (2021) · British Journal of Pharmacology · doi:10.1111/bph.15746 · Cited by 64
High Mobility Group B Proteins Facilitate Strong Estrogen Receptor Binding to Classical and Half-Site Estrogen Response Elements and Relax Binding Selectivity
Das, D., Peterson, R. C., & Scovell, W. M. (2004) · Molecular Endocrinology · doi:10.1210/me.2004-0125 · Cited by 59

Authors: McNally, J. G., Müller, W. G., Walker, D., Wolford, R., & Hager, G. L.
Affiliations: National Institutes of Health (US)
Laboratory of Receptor Biology and Gene Expression, Building 41, Room B602, National Cancer Institute, Bethesda, MD 20892–5055, USA.
Corresponding author: McNally, James G.
Hager, Gordon L.
ORCID: McNally, James G.
Hager, Gordon L.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2000-02-18
Volume: 287
Issue: 5456
Pages: 1262-1265
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.287.5456.1262
OpenAlex: W2096594220
Cited by: 802
References: 32
Citations by year: 2026: 17 · 2025: 13 · 2024: 11 · 2023: 13 · 2022: 16 · 2021: 21 · 2020: 17 · 2019: 13 · 2018: 15 · 2017: 24 · 2016: 28 · 2015: 27 · 2014: 29 · 2013: 31 · 2012: 20
FWCI: 35.70
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Estrogen and related hormone effects
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Diffusion and Search Dynamics
Keywords: glucocorticoid receptor, chromatin, response elements, nucleoplasm, photobleaching, green fluorescent protein tagging, chromatin dynamics, transcriptional regulation
MeSH terms: Animals, Binding Sites, Cell Line, Transformed, Cell Nucleus, Chromatin, Dexamethasone, Ligands, Luminescent Proteins, Mammary Tumor Virus, Mouse, Microscopy, Fluorescence, Nucleosomes, Receptors, Glucocorticoid, In Situ Hybridization, Fluorescence, Microscopy, Confocal, Terminal Repeat Sequences, Response Elements, Green Fluorescent Proteins, Mice

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

The Glucocorticoid Receptor: Rapid Exchange with Regulatory Sites in Living Cells

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks