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

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

Nuclear Compartmentalization of N-CoR and Its Interactions with Steroid Receptors

Wu, Y., Kawate, H., Ohnaka, K., Nawata, H., & Takayanagi, R. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01534-05 · Cited by 36

From milliseconds to lifetimes: tracking the dynamic behavior of transcription factors in gene networks

Li, Y., Varala, K., & Coruzzi, G. M. (2015) · Trends in Genetics · doi:10.1016/j.tig.2015.05.005 · Cited by 38

Stable Chromatin Binding Prevents FoxA Acetylation, Preserving FoxA Chromatin Remodeling

Kohler, S., & Cirillo, L. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.063149 · Cited by 37

Retinoblastoma Tumor Suppressor: Analyses of Dynamic Behavior in Living Cells Reveal Multiple Modes of Regulation

Angus, S. P., Solomon, D. A., Kuschel, L., Hennigan, R. F., & Knudsen, E. S. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.22.8172-8188.2003 · Cited by 35

Transcriptional Control: An Activating Role for Arginine Methylation

Davie, J. K., & Dent, S. (2002) · Current Biology · doi:10.1016/s0960-9822(01)00674-1 · Cited by 35

Genomes, proteomes, and dynamic networks in the cell nucleus

Roix, J. J., & Misteli, T. (2002) · Histochemistry and Cell Biology · doi:10.1007/s00418-002-0446-7 · Cited by 35

Quantification of Protein–Protein and Protein–DNA Interactions In Vivo, Using Fluorescence Recovery after Photobleaching

Carrero, G., Crawford, E., Th'ng, J. P. H., de Vries, G., & Hendzel, M. J. (2003) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(03)75026-5 · Cited by 34

Nuclear receptor coactivators: the key to unlock chromatin

Xu, W. (2005) · Biochemistry and Cell Biology · doi:10.1139/o05-057 · Cited by 34

Glucocorticoid Receptor Mutants Demonstrate Increased Motility Inside the Nucleus of Living Cells: Time of Fluorescence Recovery After Photobleaching (FRAP) Is an Integrated Measure of Receptor Function

Kino, T., Liou, S.-H., Charmandari, E., & Chrousos, G. P. (2004) · Molecular Medicine · doi:10.2119/2005-00026.kino · Cited by 34

Formation of higher-order secondary and tertiary chromatin structures by genomic mouse mammary tumor virus promotersPreprint

Georgel, P. T., Fletcher, T. M., Hager, G. L., & Hansen, J. C. (2003) · Genes & Development · doi:10.1101/gad.1097603 · Cited by 34

Transcription dynamics and genome organization in the mammalian nucleus: Recent advances

Wagh, K., Stavreva, D. A., & Hager, G. L. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.09.022 · Cited by 32

Progestin withdrawal at parturition in the mare

Legacki, E. L., Corbin, C. J., Ball, B. A., Wynn, M. A. A., Loux, S. C., Stanley, S. D., & Conley, A. J. (2016) · Reproduction · doi:10.1530/rep-16-0227 · Cited by 33

Proteomic identification of glucocorticoid receptor interacting proteins

Hedman, E., Widén, C., Asadi, A., Dinnetz, I., Schröder, W. P., Gustafsson, J.-Å., & Wikström, A. (2006) · PROTEOMICS · doi:10.1002/pmic.200500266 · Cited by 33

“On the move”ments of nuclear components in living cells

Bubulya, P. A. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.03.018 · Cited by 33

Imaging Analysis of Subcellular Correlation of Androgen Receptor and Estrogen Receptor α in Single Living Cells Using Green Fluorescent Protein Color Variants

Ochiai, I., Matsuda, K., Nishi, M., Ozawa, H., & Kawata, M. (2003) · Molecular Endocrinology · doi:10.1210/me.2002-0262 · Cited by 33

In silico identification of metazoan transcriptional regulatory regions

Wasserman, W. W., & Krivan, W. (2003) · Die Naturwissenschaften · doi:10.1007/s00114-003-0409-4 · Cited by 33

Gene expression within a dynamic nuclear landscape

Shav‐Tal, Y., Darzacq, X., & Singer, R. H. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601226 · Cited by 33

Hormonal Regulation of Oxidative Phosphorylation in the Brain in Health and Disease

Głombik, K., Detka, J., & Budziszewska, B. (2021) · Cells · doi:10.3390/cells10112937 · Cited by 34

The multivalency of the glucocorticoid receptor ligand-binding domain explains its manifold physiological activities

Jiménez‐Panizo, A., Alegre‐Martí, A., Tettey, T. T., Fettweis, G., Abella, M., Antón, R. I., Johnson, T. A., Kim, S., Schiltz, R. L., Barrios-Núñez, I., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac1119 · Cited by 32

HLA-DM mediates peptide exchange by interacting transiently and repeatedly with HLA-DR1

Narayan, K., Su, K. W., Chou, C.-L., Khoruzhenko, S., & Sadegh‐Nasseri, S. (2009) · Molecular Immunology · doi:10.1016/j.molimm.2009.07.001 · Cited by 32

In vitro FRAP reveals the ATP-dependent nuclear mobilization of the exon junction complex protein SRm160

Wagner, S., Chiosea, S. I., Ivshina, M. P., & Nickerson, J. A. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200307002 · Cited by 32

Agonist-mediated docking of androgen receptor onto the mitotic chromatin platform discriminates intrinsic mode of action of prostate cancer drugs

Kumar, S., Chaturvedi, N. K., Kumar, S., & Tyagi, R. K. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.11.002 · Cited by 31

Modulation of aryl hydrocarbon receptor (AHR)-dependent signaling by peroxisome proliferator-activated receptor β/δ (PPARβ/δ) in keratinocytes

Borland, M. G., Krishnan, P., Lee, C., Albrecht, P. P., Shan, W., Bility, M. T., Marcus, C. B., Lin, J.-M., Amin, S., Gonzalez, F. J., et al. (2014) · Carcinogenesis · doi:10.1093/carcin/bgu067 · Cited by 31

Organization of chromatin and histone modifications at a transcription site

Müller, W. G., Rieder, D., Karpova, T., John, S., Trajanoski, Z., & McNally, J. G. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200703157 · Cited by 31

Intranuclear Trafficking: Organization and Assembly of Regulatory Machinery for Combinatorial Biological Control

Zaidi, S. K., Young, D. W., Choi, J., Pratap, J., Javed, A., Montecino, M. A., Stein, J. L., Lian, J. B., van Wijnen, A. J., & Stein, G. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.r400020200 · Cited by 30

Effects of the heterogeneous nuclear ribonucleoprotein U (hnRNP U/SAF-A) on glucocorticoid-dependent transcription in vivo

Eggert, H., Schulz, M. M., Fackelmayer, F. O., Renkawitz, R., & Eggert, M. (2001) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(01)00074-7 · Cited by 30

Combinatorial probabilistic chromatin interactions produce transcriptional heterogeneity

Voss, T. C., Schiltz, R. L., Sung, M., Johnson, T. A., John, S., & Hager, G. L. (2009) · Journal of Cell Science · doi:10.1242/jcs.035865 · Cited by 29

Erk signaling and chromatin remodeling in MMTV promoter activation by progestins

Vicent, G. P., Zaurín, R., Ballaré, C., Nacht, A. S., & Beato, M. (2009) · Nuclear Receptor Signaling · doi:10.1621/nrs.07008 · Cited by 29

Hormone Binding and Co-regulator Binding to the Glucocorticoid Receptor are Allosterically Coupled

Pfaff, S. J., & Fletterick, R. J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.108118 · Cited by 30

Activation of Estrogen Receptor-α by E2 or EGF Induces Temporally Distinct Patterns of Large-Scale Chromatin Modification and mRNA Transcription

Berno, V., Amazit, L., Hinojos, C. A., Zhong, J., Mancini, M. G., Sharp, Z. D., & Mancini, M. A. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002286 · Cited by 29

The neuroprotective and antiapoptotic effects of melatonin in cerebellar neurons involve glucocorticoid receptor and p130 signal pathways

Persengiev, S. P. (2001) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(01)00037-1 · Cited by 29

Identification of biomolecule mass transport and binding rate parameters in living cells by inverse modeling

Zadeh, K. S., Montas, H. J., & Shirmohammadi, A. (2006) · Theoretical Biology and Medical Modelling · doi:10.1186/1742-4682-3-36 · Cited by 29

The amazing complexity of transcription factories

Jackson, D. A. (2005) · Briefings in Functional Genomics and Proteomics · doi:10.1093/bfgp/4.2.143 · Cited by 29

Imaging transcription dynamics at endogenous genes in living Drosophila tissues

Yao, J., Zobeck, K. L., Lis, J. T., & Webb, W. W. (2008) · Methods · doi:10.1016/j.ymeth.2008.06.004 · Cited by 29

Nature of the Accessible Chromatin at a Glucocorticoid-Responsive Enhancer

Flavin, M., Cappabianca, L. A., Kress, C., Thomassin, H., & Grange, T. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.18.7891-7901.2004 · Cited by 29

A Glucocorticoid/Retinoic Acid Receptor Chimera That Displays Cytoplasmic/Nuclear Translocation in Response to Retinoic Acid

Mackem, S., Baumann, C. T., & Hager, G. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100269200 · Cited by 29

Different SP1 binding dynamics at individual genomic loci in human cells

Hasegawa, Y., & Struhl, K. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2113579118 · Cited by 29

Show and tell: visualizing gene expression in living cells

Rafalska-Metcalf, I. U., & Janicki, S. M. (2007) · Journal of Cell Science · doi:10.1242/jcs.008664 · Cited by 29

BCAS2 promotes prostate cancer cells proliferation by enhancing AR mRNA transcription and protein stability

Kuo, P.-C., Huang, C.-W., Lee, C.-I., Chang, H.-W., Hsieh, S.-W., Chung, Y.-P., Lee, M.-S., Huang, C.-S., Tsao, L.-P., Tsao, Y.-P., et al. (2014) · British Journal of Cancer · doi:10.1038/bjc.2014.603 · Cited by 28

Chromatin priming elements establish immunological memory in T cells without activating transcription

Bevington, S. L., Cauchy, P., & Cockerill, P. N. (2016) · BioEssays · doi:10.1002/bies.201600184 · Cited by 31

Dynamic Control of Nuclear Receptor Transcription

Fowler, A. M., & Alarid, E. T. (2004) · Science s STKE · doi:10.1126/stke.2562004pe51 · Cited by 28

Carboxyl Terminus of hVIP/mov34 Is Critical for HIV-1-Vpr Interaction and Glucocorticoid-mediated Signaling

Ramanathan, M. P., Curley, E., Su, M. S. S., Chambers, J. A., & Weiner, D. B. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203905200 · Cited by 28

Ligands Differentially Modify the Nuclear Mobility of Estrogen Receptors α and β

Damdimopoulos, A. E., Spyrou, G., & Gustafsson, J.-Α. (2007) · Endocrinology · doi:10.1210/en.2007-0198 · Cited by 28

Molecular dynamics and nuclear receptor function

Hinojos, C. A., Sharp, Z. D., & Mancini, M. A. (2004) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2004.11.006 · Cited by 28

Navigating the crowd: visualizing coordination between genome dynamics, structure, and transcription

Shaban, H. A., Barth, R., & Bystricky, K. (2020) · Genome biology · doi:10.1186/s13059-020-02185-y · Cited by 28

Altered Promoter Recycling Rates Contribute to Dominant-Negative Activity of Human Peroxisome Proliferator-Activated Receptor-γ Mutations Associated with Diabetes

Li, G., & Leff, T. (2007) · Molecular Endocrinology · doi:10.1210/me.2006-0401 · Cited by 27

Transcription Factor Oscillations Induce Differential Gene Expressions

Wee, K. B., Yio, W. K., Surana, U., & Chiam, K. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.04.023 · Cited by 27

Chapter 23 Modification of Androgen Receptor Function by Igf‐1 Signaling

Yanase, T., & Fan, W. (2009) · Vitamins and hormones · doi:10.1016/s0083-6729(08)00623-7 · Cited by 27

Differences in Nuclear Retention Characteristics of Agonist-Activated Glucocorticoid Receptor May Determine Specific Responses

Vicent, G. P., Pecci, A., Ghini, A. A., Piwien‐Pilipuk, G., & Galigniana, M. D. (2002) · Experimental Cell Research · doi:10.1006/excr.2002.5532 · Cited by 27

Chromatin-Mediated Restriction of Nuclear Factor 1/CTF Binding in a Repressed and Hormone-Activated Promoter In Vivo

Belikov, S. V., Åstrand, C., Holmqvist, P.-H., & Wränge, Ö. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.7.3036-3047.2004 · Cited by 27

Transcriptional enhancers at 40: evolution of a viral DNA element to nuclear architectural structures

Nair, S. J., Suter, T., Wang, S. S., Lu, Y., Yang, F., & Rosenfeld, M. G. (2022) · Trends in Genetics · doi:10.1016/j.tig.2022.05.015 · Cited by 27

Dynamic Interaction of HDAC1 with a Glucocorticoid Receptor-regulated Gene Is Modulated by the Activity State of the Promoter

Qiu, Y., Stavreva, D. A., Luo, Y., Indrawan, A., Chang, M., & Hager, G. L. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.185488 · Cited by 24

Transient Association of Ku with Nuclear Substrates Characterized Using Fluorescence Photobleaching

Rodgers, W., Jordan, S. J., & Capra, J. D. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.168.5.2348 · Cited by 26

Effects of acetylation, polymerase phosphorylation, and DNA unwinding in glucocorticoid receptor transactivation

Kim, Y. Y., Sun, Y., Chow, C. C., Pommier, Y. G., & Simons, S. S. (2006) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2006.03.003 · Cited by 26

Cell Cycle-dependent Expression of Thyroid Hormone Receptor-β Is a Mechanism for Variable Hormone Sensitivity

Maruvada, P., Dmitrieva, N. I., East-Palmer, J., & Yen, P. M. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-09-0636 · Cited by 26

Visualizing chromatin dynamics in intact cells

Voss, T. C., & Hager, G. L. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.06.022 · Cited by 27

Phosphorylation-Elicited Quaternary Changes of GA Binding Protein in Transcriptional Activation

Sunesen, M., Huchet, M., Christensen, M. O., & Changeux, J. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.22.8008-8018.2003 · Cited by 26

Trichostatin a inhibits β‐casein expression in mammary epithelial cells

Pujuguet, P., Radisky, D. C., Levy, D., Lacza, C. T., & Bissell, M. J. (2001) · Journal of Cellular Biochemistry · doi:10.1002/jcb.1260 · Cited by 25

AR-V7 exhibits non-canonical mechanisms of nuclear import and chromatin engagement in castrate-resistant prostate cancer

Kim, S., Au, C. C., Jamalruddin, M. A. B., Abou-Ghali, N. E., Mukhtar, E., Portella, L., Berger, A., Worroll, D., Vatsa, P., Rickman, D. S., et al. (2022) · eLife · doi:10.7554/elife.73396 · Cited by 25

FRAP and FRET Methods to Study Nuclear Receptors in Living Cells

van Royen, M. E., Dinant, C., Farla, P., Trapman, J., & Houtsmuller, A. B. (2009) · Methods in molecular biology · doi:10.1007/978-1-60327-575-0_5 · Cited by 25

Assaying epigenome functions of PRMTs and their substrates

Rakow, S., Pullamsetti, S. S., Bauer, U., & Bouchard, C. (2019) · Methods · doi:10.1016/j.ymeth.2019.09.014 · Cited by 24

A High-Content Glucocorticoid Receptor Translocation Assay for Compound Mechanism-of-Action Evaluation

Agler, M. L., Prack, M. M., Zhu, Y., Kolb, J. M., Nowak, K., Ryseck, R., Shen, D. R., Cvijic, M. E., Somerville, J. E., Nadler, S., et al. (2007) · SLAS DISCOVERY · doi:10.1177/1087057107309353 · Cited by 25

Dynamic Patterns of Growth Hormone Gene Transcription in Individual Living Pituitary Cells

Norris, A. J., Stirland, J. A., McFerran, D. W., Seymour, Z. C., Spiller, D. G., Loudon, A. S. I., White, M., & Davis, J. R. (2003) · Molecular Endocrinology · doi:10.1210/me.2002-0201 · Cited by 25

Translational applications of evaluating physiologic variability in human endotoxemia

Scheff, J. D., Mavroudis, P. D., Calvano, S. E., & Androulakis, I. P. (2012) · Journal of Clinical Monitoring and Computing · doi:10.1007/s10877-012-9418-1 · Cited by 24

Modeling Physiologic Variability in Human Endotoxemia

Scheff, J. D., Mavroudis, P. D., Foteinou, P. T., Calvano, S. E., & Androulakis, I. P. (2012) · Critical Reviews in Biomedical Engineering · doi:10.1615/critrevbiomedeng.v40.i4.60 · Cited by 24

Androgen receptor complexes probe DNA for recognition sequences by short random interactions

van Royen, M. E., van Cappellen, W. A., Geverts, B., Schmidt, T., Houtsmuller, A. B., & Schaaf, M. J. M. (2014) · Journal of Cell Science · doi:10.1242/jcs.135228 · Cited by 24

Development and Validation of a High-Content Screening Assay to Identify Inhibitors of Cytoplasmic Dynein-Mediated Transport of Glucocorticoid Receptor to the Nucleus

Johnston, P. A., Shinde, S. N., Hua, Y., Shun, T. Y., Lazo, J. S., & Day, B. W. (2012) · Assay and Drug Development Technologies · doi:10.1089/adt.2012.456 · Cited by 24

Genome-wide Regulatory Roles of the C2H2-type Zinc Finger Protein ZNF764 on the Glucocorticoid Receptor

Fadda, A., Syed, N., Mackeh, R., Papadopoulou, A., Suzuki, S., Jithesh, P., & Kino, T. (2017) · Scientific Reports · doi:10.1038/srep41598 · Cited by 23

Conformational profiling of a G-rich sequence within the c-KIT promoter

Rigo, R., Dean, W. L., Gray, R. D., Chaires, J. B., & Sissi, C. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx983 · Cited by 24

Mutual transactivational repression of Runx2 and the androgen receptor by an impairment of their normal compartmentalization

Kawate, H., Wu, Y., Ohnaka, K., & Takayanagi, R. (2007) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2006.11.020 · Cited by 24

Distinct Interaction of Cortivazol with the Ligand Binding Domain Confers Glucocorticoid Receptor Specificity

Yoshikawa, N., Makino, Y., Okamoto, K., Morimoto, C., Makino, I., & Tanaka, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107946200 · Cited by 25

Impaired Nuclear Translocation, Nuclear Matrix Targeting, and Intranuclear Mobility of Mutant Androgen Receptors Carrying Amino Acid Substitutions in the Deoxyribonucleic Acid-Binding Domain Derived from Androgen Insensitivity Syndrome Patients

Kawate, H., Wu, Y., Ohnaka, K., Tao, R.-H., Nakamura, K., Okabe, T., Yanase, T., Nawata, H., & Takayanagi, R. (2005) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2005-0179 · Cited by 24

High Mobility of Flap Endonuclease 1 and DNA Polymerase η Associated with Replication Foci in Mammalian S-Phase Nucleus

Solovjeva, L., Svetlova, M., Sasina, L., Tanaka, K., Saijo, M., Nazarov, I. B., Bradbury, M., & Tomilin, N. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-12-1066 · Cited by 23

Dynamic enhancer function in the chromatin context

Goldstein, I., & Hager, G. L. (2018) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1390 · Cited by 25

Ep300 sequestration to functionally distinct glucocorticoid receptor binding loci underlie rapid gene activation and repression

Sarusi-Portuguez, A., Grbeša, I., Tal, M., Deitch, R., Raz, D., Kliker, L., Weismann, R., Schwartz, M., Loza, O., Cohen, L., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac488 · Cited by 29

Quantifying transcription factor–DNA binding in single cells in vivo with photoactivatable fluorescence correlation spectroscopy

Zhao, Z., White, M. D., Álvarez, Y. D., Zenker, J., Bissière, S., & Plachta, N. (2017) · Nature Protocols · doi:10.1038/nprot.2017.051 · Cited by 23

Intranuclear mobility of estrogen receptor α and progesterone receptors in association with nuclear matrix dynamics

Matsuda, K., Nishi, M., Takaya, H., Kaku, N., & Kawata, M. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21393 · Cited by 23

Glucocorticoid receptor binding to chromatin is selectively controlled by the coregulator Hic-5 and chromatin remodeling enzymes

Lee, B. H., & Stallcup, M. R. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.782607 · Cited by 23

Chromatin reprogramming in breast cancer

Swinstead, E. E., Paakinaho, V., & Hager, G. L. (2018) · Endocrine Related Cancer · doi:10.1530/erc-18-0033 · Cited by 24

Frontiers in fluorescence microscopy

Rino, J., Braga, J., Henriques, R., & Carmo‐Fonseca, M. (2009) · The International Journal of Developmental Biology · doi:10.1387/ijdb.072351jr · Cited by 23

Oncogenic conversion of the thyroid hormone receptor by altered nuclear transport

Bonamy, G. M. C., & Allison, L. A. (2006) · Nuclear Receptor Signaling · doi:10.1621/nrs.04008 · Cited by 23

Dynamics of Leptomycin B‐Sensitive Nucleocytoplasmic Flux of Parathyroid Hormone‐Related Protein

Lam, M. H. C., Henderson, B. R., Gillespie, M. T., & Jans, D. A. (2001) · Traffic · doi:10.1034/j.1600-0854.2001.21110.x · Cited by 23

Nuclear structure-associated TIF2 recruits glucocorticoid receptor and its target DNA

Ogawa, H., Yu, R. T., Haraguchi, T., Hiraoka, Y., Nakatani, Y., Morohashi, K.-I., & Umesono, K. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.05.161 · Cited by 23

DNA methylation, nuclear structure, gene expression and cancer

Heinrich, L., & Cardoso, M. C. (2000) · Journal of Cellular Biochemistry · doi:10.1002/1097-4644(2000)79:35+ · Cited by 97

Taking into account nucleosomes for predicting gene expression

Teif, V. B., Erdel, F., Beshnova, D. A., Vainshtein, Y., Mallm, J., & Rippe, K. (2013) · Methods · doi:10.1016/j.ymeth.2013.03.011 · Cited by 22

Agonist-controlled competition of RAR and VDR nuclear receptors for heterodimerization with RXR is manifested in their DNA binding

Rehó, B., Fadel, L., Brázda, P., Benziane, A., Hegedüs, É., Sen, P., Gadella, T. W. J., Tóth, K., Nagy, L., & Vámosi, G. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.102896 · Cited by 26

Biochemical observation of the rapid mobility of nuclear HMGB1

Sapojnikova, N. A., Maman, J. D., Myers, F. A., Thorne, A. W., Vorobyev, V. I., & Crane‐Robinson, C. (2005) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/j.bbaexp.2005.03.002 · Cited by 22

Impact of chromatin structure on PR signaling: Transition from local to global analysis

Grøntved, L., & Hager, G. L. (2011) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.09.006 · Cited by 22

Current Major Advances in the Regulation of Milk Protein Gene Expression

Qian, X., & Zhao, F. (2014) · Critical Reviews in Eukaryotic Gene Expression · doi:10.1615/critreveukaryotgeneexpr.2014012215 · Cited by 25

Perspective on unraveling the versatility of ‘co-repressor’ complexes

Baymaz, H. I., Karemaker, I. D., & Vermeulen, M. (2015) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2015.06.012 · Cited by 22

Photo-caged agonists of the nuclear receptors RARγ and TRβ provide unique time-dependent gene expression profiles for light-activated gene patterning

Link, K. H., Cruz, F. G., Ye, H., O'Reilly, K. E., Dowdell, S. E., & Koh, J. T. (2004) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2004.08.022 · Cited by 22

An estrogen receptor chimera senses ligands by nuclear translocation

Martinez, E. D., Rayasam, G. V., Dull, A. B., Walker, D. A., & Hager, G. L. (2005) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2005.06.033 · Cited by 22

Real-time imaging of gene promoter activity using an adenoviral reporter construct demonstrates transcriptional dynamics in normal anterior pituitary cells

Stirland, J. A., Seymour, Z. C., Windeatt, S., Norris, A., Stanley, P., Castro, M. G., Loudon, A. S. I., White, M., & Davis, J. R. (2003) · Journal of Endocrinology · doi:10.1677/joe.0.1780061 · Cited by 22

Genomic Approaches for Reconstructing Gene Networks

Lee, N. H. (2005) · Pharmacogenomics · doi:10.1517/14622416.6.3.245 · Cited by 21

Live cell imaging of the cancer‐related transcription factor RUNX2 during mitotic progression

Pockwinse, S. M., Kota, K. P., Quaresma, A. J. C., Imbalzano, A. N., Lian, J. B., van Wijnen, A. J., Stein, J. L., Stein, G. S., & Nickerson, J. A. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22465 · Cited by 21

Transcription Factor Interactions in Genomic Nuclear Receptor Function

George, C. L., Lightman, S. L., & Biddie, S. C. (2011) · Epigenomics · doi:10.2217/epi.11.66 · Cited by 21

High-Content Positional Biosensor Screening Assay for Compounds to Prevent or Disrupt Androgen Receptor and Transcriptional Intermediary Factor 2 Protein–Protein Interactions

Hua, Y., Tong, Y.-S., Strock, C., & Johnston, P. (2014) · Assay and drug development technologies · doi:10.1089/adt.2014.594 · Cited by 20

Nuclear Organisation and Subnuclear Bodies

Platani, M., & Lamond, A. I. (2007) · Progress in molecular and subcellular biology · doi:10.1007/978-3-540-74266-1_1 · Cited by 21

Scaffold attachment factor B (SAFB)1 and SAFB2 cooperatively inhibit the intranuclear mobility and function of ERα

Hashimoto, T., Matsuda, K., & Kawata, M. (2012) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24182 · Cited by 21

Chromatin structure and gene regulation: a dynamic view of enhancer function

Stavreva, D. A., & Hager, G. L. (2015) · Nucleus · doi:10.1080/19491034.2015.1107689 · Cited by 24

Steroid Receptors Hit and Run

(2000) · Science s STKE · doi:10.1126/stke.2000.20.tw3

Glucocorticoid receptor dynamics and gene regulation

Biddie, S. C., & Hager, G. L. (2008) · Stress · doi:10.1080/10253890802506409 · Cited by 72

Nuclear Receptor Mobility on Gene Targets

(2003) · Hormone and Metabolic Research · doi:10.1055/s-2003-43512-3

Subnuclear Trafficking and Gene Targeting by Steroid Receptors

Nagaich, A. K., Rayasam, G. V., Martinez, E. D., BECKER, M., Qiu, Y., Johnson, T. A., Elbi, C., Fletcher, T. M., John, S., & Hager, G. L. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1321.002 · Cited by 48

Nuclear Mechanisms of Glucocorticoid Action

Hager, G. L., Stavreva, D. A., & Voss, T. C. (2009) · Elsevier eBooks · doi:10.1016/b978-008088783-8.00040-1