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

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 101–200 of 799

Rapid Switching of TFIIH between RNA Polymerase I and II Transcription and DNA Repair In Vivo
Hoogstraten, D., Nigg, A. L., Heath, H., Mullenders, L. H. F., DRIEL, R. V., Hoeijmakers, J. H. J., Vermeulen, W., & Houtsmuller, A. B. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00709-8 · Cited by 191
Dynamics of heat shock factor association with native gene loci in living cells
Yao, J., Munson, K. M., Webb, W. W., & Lis, J. T. (2006) · Nature · doi:10.1038/nature05025 · Cited by 192
Enhancer selectivity in space and time: from enhancer–promoter interactions to promoter activation
Yang, J. H., & Hansen, A. S. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00710-6 · Cited by 191
Concise Review: Epigenetic Mechanisms Contribute to Pluripotency and Cell Lineage Determination of Embryonic Stem Cells
Gan, Q., Yoshida, T., McDonald, O. G., & Owens, G. K. (2006) · Stem Cells · doi:10.1634/stemcells.2006-0383 · Cited by 192
DNA binding domains in diverse nuclear receptors function as nuclear export signals
Black, B. E., Holaska, J. M., Rastinejad, F., & Paschal, B. M. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00537-1 · Cited by 189
Visualizing transcription factor dynamics in living cells
Liu, Z. J., & Tjian, R. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201710038 · Cited by 192
Large-scale chromatin decondensation and recondensation regulated by transcription from a natural promoter
Müller, W. G., Walker, D. A., Hager, G. L., & McNally, J. G. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200011069 · Cited by 183
Dynamic Shuttling and Intranuclear Mobility of Nuclear Hormone Receptors
Maruvada, P., Baumann, C. T., Hager, G. L., & Yen, P. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m202752200 · Cited by 185
Mechanisms of endometrial progesterone resistance
Al-Sabbagh, M., Lam, E. W.-F., & Brosens, J. J. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.10.035 · Cited by 183
HDAC1 Acetylation Is Linked to Progressive Modulation of Steroid Receptor-Induced Gene Transcription
Qiu, Y., Zhao, Y., Becker, M., John, S., Parekh, B. S., Huang, S., Hendarwanto, A., Martinez, E. D., Chen, Y., Lu, H., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.04.019 · Cited by 162
Transcription Dynamics in Living Cells
Lenstra, T. L., Rodriguez, J., Chen, H., & Larson, D. R. (2016) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-062215-010838 · Cited by 186
The Search for Safer Glucocorticoid Receptor Ligands
Rosen, J., & Miner, J. N. (2005) · Endocrine Reviews · doi:10.1210/er.2005-0002 · Cited by 187
A single molecule view of gene expression
Larson, D. R., Singer, R. H., & Zenklusen, D. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.08.008 · Cited by 177
Arkadia Activates Smad3/Smad4-Dependent Transcription by Triggering Signal-Induced SnoN Degradation
Lévy, L., Howell, M. T., Das, D., Harkin, S., Episkopou, V., & Hill, C. S. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00664-07 · Cited by 177
Dynamic Remodeling of Transcription Complexes by Molecular Chaperones
Morimoto, R. I. (2002) · Cell · doi:10.1016/s0092-8674(02)00860-7 · Cited by 177
Synergy among Nuclear Receptor Coactivators: Selective Requirement for Protein Methyltransferase and Acetyltransferase Activities
Lee, Y., Koh, S. S., Zhang, X., Cheng, X., & Stallcup, M. R. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.11.3621-3632.2002 · Cited by 181
Dissecting the Contribution of Diffusion and Interactions to the Mobility of Nuclear Proteins
Beaudouin, J., Mora‐Bermúdez, F., Klee, T., Daigle, N., & Ellenberg, J. (2005) · Biophysical Journal · doi:10.1529/biophysj.105.071241 · Cited by 175
Macromolecular dynamics in living cell nuclei revealed by fluorescence redistribution after photobleaching
Houtsmuller, A. B., & Vermeulen, W. (2000) · Histochemistry and Cell Biology · doi:10.1007/s004180000234 · Cited by 173
Molecular Determinants of Glucocorticoid Receptor Mobility in Living Cells: the Importance of Ligand Affinity
Schaaf, M. J. M., & Cidlowski, J. A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.6.1922-1934.2003 · Cited by 173
Compartmentalization of androgen receptor protein–protein interactions in living cells
van Royen, M. E., Cunha, S. M. P. R. M., Brink, M. C., Mattern, K. A., Nigg, A. L., Dubbink, H. J., Verschure, P. J., Trapman, J., & Houtsmuller, A. B. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200609178 · Cited by 170
Single-molecule analysis of transcription factor binding at transcription sites in live cells
Morisaki, T., Müller, W. G., Golob, N., Mazza, D., & McNally, J. G. (2014) · Nature Communications · doi:10.1038/ncomms5456 · Cited by 166
DNA damage stabilizes interaction of CSB with the transcription elongation machinery
van den Boom, V., Citterio, E., Hoogstraten, D., Zotter, A., Egly, J., van Cappellen, W. A., Hoeijmakers, J. H. J., Houtsmuller, A. B., & Vermeulen, W. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200401056 · Cited by 166
Glucocorticoid receptor action in beneficial and side effects of steroid therapy: lessons from conditional knockout mice
Kleiman, A., & Tuckermann, J. P. (2007) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2007.05.009 · Cited by 165
Proteasomal inhibition enhances glucocorticoid receptor transactivation and alters its subnuclear trafficking
Deroo, B. J., Rentsch, C., Sampath, S., Young, J., DeFranco, D. B., & Archer, T. K. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.12.4113-4123.2002 · Cited by 164
DNase Footprint Signatures Are Dictated by Factor Dynamics and DNA Sequence
Sung, M., Guertin, M. J., Baek, S., & Hager, G. L. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.08.016 · Cited by 160
The glucocorticoid receptor dimer interface allosterically transmits sequence-specific DNA signals
Watson, L. C., Kuchenbecker, K. M., Schiller, B., Gross, J., Pufall, M., & Yamamoto, K. R. (2013) · Nature Structural &Molecular Biology · doi:10.1038/nsmb.2595 · Cited by 161
DNA binding controls inactivation and nuclear accumulation of the transcription factor Stat1
Meyer, T., Marg, A., Lemke, P., Wiesner, B., & Vinkemeier, U. (2003) · Genes & Development · doi:10.1101/gad.268003 · Cited by 161
Nucleosome remodeling at the IL-12 p40 promoter is a TLR-dependent, Rel-independent event
Weinmann, A. S., Mitchell, D. M., Sanjabi, S., Bradley, M. N., Hoffmann, A., Liou, H.-C., & Smale, S. T. (2001) · Nature Immunology · doi:10.1038/83168 · Cited by 161
Ordered recruitment of histone acetyltransferases and the TRAP/Mediator complex to thyroid hormone-responsive promoters in vivo
Sharma, D., & Fondell, J. D. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.122004799 · Cited by 160
Glucocorticoids: Effects on Gene Transcription
Adcock, I. M., Ito, K., & Barnes, P. J. (2004) · Proceedings of the American Thoracic Society · doi:10.1513/pats.200402-001ms · Cited by 160
Potentiation of glucocorticoid receptor transcriptional activity by sumoylation
Le Drean, Y., Mincheneau, N., Le Goff, P., & Michel, D. (2002) · Endocrinology · doi:10.1210/en.2002-220135 · Cited by 159
Higher order chromatin architecture in the cell nucleus: on the way from structure to function
Cremer, T. J., Küpper, K., Dietzel, S., & Fakan, S. (2004) · Biology of the Cell · doi:10.1016/j.biolcel.2004.07.002 · Cited by 159
Direct observation of frequency modulated transcription in single cells using light activation
Larson, D. R., Fritzsch, C., Sun, L. D., Meng, X., Lawrence, D. S., & Singer, R. H. (2013) · eLife · doi:10.7554/elife.00750 · Cited by 147
Dynamic Shuttling of Nuclear Factor κB between the Nucleus and Cytoplasm as a Consequence of Inhibitor Dissociation
Carlotti, F., Dower, S., & Qwarnström, E. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006179200 · Cited by 154
Retinoid X Receptor Dominates the Nuclear Import and Export of the Unliganded Vitamin D Receptor
Prüfer, K., & Bársony, J. (2002) · Molecular Endocrinology · doi:10.1210/me.2001-0345 · Cited by 153
Analysis of computational footprinting methods for DNase sequencing experiments
Gusmao, E. G., Allhoff, M., Zenke, M., & Costa, I. G. (2016) · Nature Methods · doi:10.1038/nmeth.3772 · Cited by 152
Single-Molecule Nanoscopy Elucidates RNA Polymerase II Transcription at Single Genes in Live Cells
Li, J., Dong, A., Saydaminova, K., Chang, H., Wang, G., Ochiai, H., Yamamoto, T., & Pertsinidis, A. (2019) · Cell · doi:10.1016/j.cell.2019.05.029 · Cited by 152
Ligand-Mediated Assembly and Real-Time Cellular Dynamics of Estrogen Receptor α-Coactivator Complexes in Living Cells
Stenoien, D. L., Nye, A. C., Mancini, M. G., Patel, K. N., Dutertre, M., O’Malley, B. W., Smith, C. L., Belmont, A. S., & Mancini, M. A. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.13.4404-4412.2001 · Cited by 148
Nuclear Cytoplasmic Shuttling by Thyroid Hormone Receptors
Baumann, C. T., Maruvada, P., Hager, G. L., & Yen, P. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011112200 · Cited by 147
Stimulus-induced modulation of transcriptional bursting in a single mammalian gene
Molina, N., Suter, D. M., Cannavò, R., Zoller, B., Gotić, I., & Naef, F. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1312310110 · Cited by 143
The circadian clock and glucocorticoids – interactions across many time scales
Dickmeis, T., Weger, B. D., & Weger, M. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.05.012 · Cited by 144
Molecular chaperones function as steroid receptor nuclear mobility factors
Elbi, C., Walker, D. A., Romero, G. G., Sullivan, W. P., Toft, D. O., Hager, G. L., & DeFranco, D. B. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400116101 · Cited by 144
Development of the HPA axis: Where and when do sex differences manifest?
Panagiotakopoulos, L., & Neigh, G. N. (2014) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2014.03.002 · Cited by 148
“Structure”-function relationships in eukaryotic transcription factors: The role of intrinsically disordered regions in gene regulation
Ferrie, J. J., Karr, J. P., Tjian, R., & Darzacq, X. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.09.021 · Cited by 142
Dynamic regulation of glucocorticoid signalling in health and disease
Biddie, S. C., Conway-Campbell, B. L., & Lightman, S. L. (2012) · Rheumatology · doi:10.1093/rheumatology/ker215 · Cited by 143
DNA binding triggers tetramerization of the glucocorticoid receptor in live cells
Presman, D. M., Ganguly, S., Schiltz, R. L., Johnson, T. A., Karpova, T., & Hager, G. L. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1606774113 · Cited by 142
Nuclear receptors: from molecular mechanisms to therapeutics
Frigo, D. E., Bondesson, M., & Williams, C. (2021) · Essays in Biochemistry · doi:10.1042/ebc20210020 · Cited by 138
Modern fluorescent proteins and imaging technologies to study gene expression, nuclear localization, and dynamics
Wu, B., Piatkevich, K. D., Lionnet, T., Singer, R. H., & Verkhusha, V. V. (2011) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.12.004 · Cited by 138
Single-molecule analysis of steroid receptor and cofactor action in living cells
Paakinaho, V., Presman, D. M., Ball, D. A., Johnson, T. A., Schiltz, R. L., Levitt, P. S., Mazza, D., Morisaki, T., Karpova, T., & Hager, G. L. (2017) · Nature Communications · doi:10.1038/ncomms15896 · Cited by 139
Live Cell Imaging Unveils Multiple Domain Requirements for In Vivo Dimerization of the Glucocorticoid Receptor
Presman, D. M., Ogara, M. F., Stortz, M., Álvarez, L. D., Pooley, J. R., Schiltz, R. L., Grøntved, L., Johnson, T. A., Mittelstadt, P. R., Ashwell, J. D., et al. (2014) · PLoS Biology · doi:10.1371/journal.pbio.1001813 · Cited by 138
Analysis of Smad nucleocytoplasmic shuttling in living cells
Nicolás, F. J., Bosscher, K. D., Schmierer, B., & Hill, C. S. (2004) · Journal of Cell Science · doi:10.1242/jcs.01289 · Cited by 138
ATP-Dependent Mobilization of the Glucocorticoid Receptor during Chromatin Remodeling
Fletcher, T. M., Xiao, N., Mautino, G., Baumann, C. T., Wolford, R. G., Warren, B. S., & Hager, G. L. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.10.3255-3263.2002 · Cited by 138
Allosteric Modulators of Steroid Hormone Receptors: Structural Dynamics and Gene Regulation
Kumar, R., & McEwan, I. J. (2012) · Endocrine Reviews · doi:10.1210/er.2011-1033 · Cited by 135
Interaction of Glucocorticoid Receptor (GR) with Estrogen Receptor (ER) α and Activator Protein 1 (AP1) in Dexamethasone-mediated Interference of ERα Activity
Karmakar, S., Jin, Y., & Nagaich, A. K. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.473819 · Cited by 137
Trafficking of nuclear receptors in living cells
Hager, G. L., Lim, C. S., Elbi, C., & Baumann, C. T. (2000) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(00)00100-x · Cited by 137
Androgen receptor phosphorylation: biological context and functional consequences
Koryakina, Y. A., Ta, H. Q., & Gioeli, D. G. (2014) · Endocrine Related Cancer · doi:10.1530/erc-13-0472 · Cited by 136
Concurrent Fast and Slow Cycling of a Transcriptional Activator at an Endogenous Promoter
Karpova, T., Kim, M. J., Spriet, C., Nalley, K., Stasevich, T. J., Kherrouche, Z., Héliot, L., & McNally, J. G. (2008) · Science · doi:10.1126/science.1150559 · Cited by 136
Direct Measurement of Association and Dissociation Rates of DNA Binding in Live Cells by Fluorescence Correlation Spectroscopy
Michelman‐Ribeiro, A., Mazza, D., Rosales, T., Stasevich, T. J., Boukari, H., Rishi, V., Vinson, C., Knutson, J. R., & McNally, J. G. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2009.04.027 · Cited by 134
Polycomb group protein complexes exchange rapidly in living Drosophila
Ficz, G., Heintzmann, R., & Arndt‐Jovin, D. J. (2005) · Development · doi:10.1242/dev.01950 · Cited by 136
Recruitment of Distinct Chromatin-modifying Complexes by Tamoxifen-complexed Estrogen Receptor at Natural Target Gene Promoters in Vivo*
Liu, X.-F., & Bagchi, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311932200 · Cited by 147
Microenvironment and Effect of Energy Depletion in the Nucleus Analyzed by Mobility of Multiple Oligomeric EGFPs
Pack, C., Saito, K., Tamura, M., & Kinjo, M. (2006) · Biophysical Journal · doi:10.1529/biophysj.105.079467 · Cited by 133
Ligand-Specific Dynamics of the Androgen Receptor at Its Response Element in Living Cells
Klokk, T. I., Kurys, P., Elbi, C., Nagaich, A. K., Hendarwanto, A., Slagsvold, T., Chang, C., Hager, G. L., & Saatcioglu, F. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01297-06 · Cited by 132
Fluorescence Imaging Reveals the Nuclear Behavior of Peroxisome Proliferator-activated Receptor/Retinoid X Receptor Heterodimers in the Absence and Presence of Ligand*♦
Feige, J. N., Gelman, L., Tudor, C., Engelborghs, Y., Wahli, W., & Desvergne, B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500786200 · Cited by 125
Reciprocal Recruitment of DRIP/Mediator and p160 Coactivator Complexes in Vivo by Estrogen Receptor
Burakov, D., Crofts, L. A., Chang, C.-P. B., & Freedman, L. P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200099200 · Cited by 127
Nucleosomes accelerate transcription factor dissociation
Luo, Y., North, J. A., Rose, S., & Poirier, M. G. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1319 · Cited by 125
Tissue-specific splicing of a ubiquitously expressed transcription factor is essential for muscle differentiationPreprint
Sebastian, S., Faralli, H., Yao, Z., Rakopoulos, P., Palii, C. G., Cao, Y., Singh, K., Liu, Q.-C., Chu, A., Aziz, A., et al. (2013) · Genes & Development · doi:10.1101/gad.215400.113 · Cited by 124
Transcriptional Activities of Retinoic Acid Receptors
Lefèbvre, P., Martin, P. J., Flajollet, S., Dedieu, S., Billaut, X., & Lefebvre, B. (2005) · Vitamins and hormones · doi:10.1016/s0083-6729(05)70007-8 · Cited by 129
Transcription factor assisted loading and enhancer dynamics dictate the hepatic fasting response
Goldstein, I., Baek, S., Presman, D. M., Paakinaho, V., Swinstead, E. E., & Hager, G. L. (2017) · Genome Research · doi:10.1101/gr.212175.116 · Cited by 121
Self-citation
MAP kinases couple multiple functions of human progesterone receptors: degradation, transcriptional synergy, and nuclear association
Qiu, M., & Lange, C. A. (2003) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(03)00221-8 · Cited by 119
Optimized glucocorticoid therapy: teaching old drugs new tricks
Strehl, C., & Buttgereit, F. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.01.026 · Cited by 118
Imaging Transcription in Living Cells
Darzacq, X., Yao, J., Larson, D. R., Causse, S., Bosanac, L., de Turris, V., Ruda, V. M., Lionnet, T., Zenklusen, D., Guglielmi, B., et al. (2009) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.050708.133728 · Cited by 120
Power-law behavior of transcription factor dynamics at the single-molecule level implies a continuum affinity model
Garcia, D. A., Fettweis, G., Presman, D. M., Paakinaho, V., Jarzynski, C., Upadhyaya, A., & Hager, G. L. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab072 · Cited by 119
Circadian Dbp Transcription Relies on Highly Dynamic BMAL1-CLOCK Interaction with E Boxes and Requires the Proteasome
Stratmann, M., Suter, D. M., Molina, N., Naef, F., & Schibler, U. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.08.012 · Cited by 119
Changes in the Distributions and Dynamics of Polycomb Repressive Complexes during Embryonic Stem Cell Differentiation
Ren, X., Vincenz, C., & Kerppola, T. K. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00949-07 · Cited by 119
GR and HMGB1 Interact Only within Chromatin and Influence Each Other’s Residence Time
Agresti, A., Scaffidi, P., Riva, A., Caiolfa, V. R., & Bianchi, M. E. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.03.005 · Cited by 114
Nuclear Ubiquitin Ligases, NF-κB Degradation, and the Control of Inflammation
Natoli, G., & Chiocca, S. (2008) · Science Signaling · doi:10.1126/stke.11pe1 · Cited by 114
Antiandrogens prevent stable DNA-binding of the androgen receptor
Farla, P., Hersmus, R., Trapman, J., & Houtsmuller, A. B. (2005) · Journal of Cell Science · doi:10.1242/jcs.02546 · Cited by 114
Sustained activation of STAT5 is essential for chromatin remodeling and maintenance of mammary-specific function
Xu, R., Nelson, C. M., Muschler, J. L., Veiseh, M., Vonderhaar, B. K., & Bissell, M. J. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200807021 · Cited by 118
Correlative cryo-light microscopy and cryo-electron tomography: from cellular territories to molecular landscapes
Plitzko, J. M., Rigort, A., & Leis, A. P. (2009) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2009.03.008 · Cited by 111
Interleukin-10 Inhibits Interleukin-12 p40 Gene Transcription by Targeting a Late Event in the Activation Pathway
Zhou, L., Nazarian, A. A., & Smale, S. T. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.6.2385-2396.2004 · Cited by 111
Ca2+-Dependent Nuclear Export Mediated by Calreticulin
Holaska, J. M., Black, B. E., Rastinejad, F., & Paschal, B. M. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.17.6286-6297.2002 · Cited by 113
Role of glucocorticoids and the glucocorticoid receptor in metabolism: Insights from genetic manipulations
Rose, A. J., Vegiopoulos, A., & Herzig, S. (2010) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.02.010 · Cited by 110
Site-specific Androgen Receptor Serine Phosphorylation Linked to Epidermal Growth Factor-dependent Growth of Castration-recurrent Prostate Cancer
Ponguta, L. A., Gregory, C. W., French, F. S., & Wilson, E. M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802392200 · Cited by 112
Ligand-Specific Dynamics of the Progesterone Receptor in Living Cells and during Chromatin Remodeling In Vitro
Rayasam, G. V., Elbi, C., Walker, D. A., Wolford, R. G., Fletcher, T. M., Edwards, D. P., & Hager, G. L. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.6.2406-2418.2005 · Cited by 111
Navigating Steroid Hormone Receptors through the Nuclear Compartment
DeFranco, D. B. (2002) · Molecular Endocrinology · doi:10.1210/mend.16.7.0880 · Cited by 110
Dynamic Changes in Subcellular Localization of Mineralocorticoid Receptor in Living Cells: In Comparison with Glucocorticoid Receptor using Dual-Color Labeling with Green Fluorescent Protein Spectral Variants
Nishi, M., Ogawa, H., Ito, T., Matsuda, K., & Kawata, M. (2001) · Molecular Endocrinology · doi:10.1210/mend.15.7.0659 · Cited by 108
Integration of Transcriptional Repression and Polycomb-Mediated Silencing of WUSCHEL in Floral Meristems
Sun, B., Zhou, Y., Cai, J., Shang, E., Yamaguchi, N., Xiao, J. Y., Looi, L., Wee, W.-Y., Gao, X., Wagner, D., et al. (2019) · The Plant Cell · doi:10.1105/tpc.18.00450 · Cited by 104
Chromatin remodeling by nuclear receptors
Hebbar, P. B., & Archer, T. (2003) · Chromosoma · doi:10.1007/s00412-003-0232-x · Cited by 106
What do expression dynamics tell us about the mechanism of transcription?
Larson, D. R. (2011) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2011.07.010 · Cited by 104
Imaging gene expression in single living cells
Shav‐Tal, Y., Singer, R. H., & Darzacq, X. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1494 · Cited by 104
Analysis of Binding at a Single Spatially Localized Cluster of Binding Sites by Fluorescence Recovery after Photobleaching
Sprague, B. L., Mueller, F., Pego, R. L., Bungay, P. M., Stavreva, D. A., & McNally, J. G. (2006) · Biophysical Journal · doi:10.1529/biophysj.105.073676 · Cited by 104
Estrogen-receptor-α exchange and chromatin dynamics are ligand- and domain-dependent
Sharp, Z. D., Mancini, M. G., Hinojos, C. A., Dai, F., Berno, V., Szafran, A. T., Smith, K. P., Lele, T. T., Ingber, D. E., & Mancini, M. A. (2006) · Journal of Cell Science · doi:10.1242/jcs.03161 · Cited by 103
Protein Mobility within the Nucleus—What Are the Right Moves?
Pederson, T. (2001) · Cell · doi:10.1016/s0092-8674(01)00258-6 · Cited by 103
Kinetic Complexity of the Global Response to Glucocorticoid Receptor Action
John, S., Johnson, T. A., Sung, M., Biddie, S. C., Trump, S., Koch-Paiz, C. A., Davis, S. R., Walker, R. L., Meltzer, P. S., & Hager, G. L. (2009) · Endocrinology · doi:10.1210/en.2008-0863 · Cited by 101
Visualizing the action of steroid hormone receptors in living cells
Griekspoor, A., Zwart, W. T., Neefjes, J., & Michalides, R. J. A. M. (2007) · Nuclear Receptor Signaling · doi:10.1621/nrs.05003 · Cited by 102
Quantifying transcription factor binding dynamics at the single-molecule level in live cells
Presman, D. M., Ball, D. A., Paakinaho, V., Grimm, J. B., Lavis, L. D., Karpova, T., & Hager, G. L. (2017) · Methods · doi:10.1016/j.ymeth.2017.03.014 · Cited by 102
UTF1 is a chromatin-associated protein involved in ES cell differentiation
van den Boom, V., Kooistra, S. M., Boesjes, M., Geverts, B., Houtsmuller, A. B., Monzen, K., Komuro, I., Essers, J., Drenth-Diephuis, L. J., & Eggen, B. J. L. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200702058 · Cited by 102
Physiological importance of RNA and protein mobility in the cell nucleus
Misteli, T. (2007) · Histochemistry and Cell Biology · doi:10.1007/s00418-007-0355-x · Cited by 101
The RNA polymerase II transcription cycle: cycling through chromatin
Svejstrup, J. Q. (2003) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/j.bbaexp.2003.10.012 · Cited by 99
Mitotic chromosome binding predicts transcription factor properties in interphase
Raccaud, M., Friman, E. T., Alber, A. B., Agarwal, H., Deluz, C., Kuhn, T., Gebhardt, J. C. M., & Suter, D. M. (2019) · Nature Communications · doi:10.1038/s41467-019-08417-5 · Cited by 98

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