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

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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

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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.

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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).

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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

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

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