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Wei Li Thyroid Cancer Research Laboratory, Thyroid Oncology Program, Medical Service, Veterans Affairs Medical Center, Lexington, Kentucky 40511, USA
Thyroid Cancer Research Laboratory, Thyroid Oncology Program, Medical Service, Veterans Affairs Medical Center, Lexington, Kentucky 40511, USA

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Kenneth B Ain Thyroid Cancer Research Laboratory, Thyroid Oncology Program, Medical Service, Veterans Affairs Medical Center, Lexington, Kentucky 40511, USA
Thyroid Cancer Research Laboratory, Thyroid Oncology Program, Medical Service, Veterans Affairs Medical Center, Lexington, Kentucky 40511, USA

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3: 20× Probe A, lane 4: AP-1, lane 5: AP-2, lane 6: CREB, lane 7: Pax8, lane 8: Sp1, lane 9: TTF-1/Pax8, lane 10: TTF-2, lane 11: Comp-1, and lane 12: Comp-2). In (D), EMSA results of KAK-1 nuclear extract that was examined with Probe A in lanes 2

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Fidéline Bonnet-Serrano Institut Cochin, INSERM U1016, CNRS UMR8104, Paris Descartes University, Paris, France
Hormonal Biology Laboratory, Assistance Publique Hôpitaux de Paris, Hôpital Cochin, Paris, France

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Jérôme Bertherat Institut Cochin, INSERM U1016, CNRS UMR8104, Paris Descartes University, Paris, France
Department of Endocrinology, Assistance Publique Hôpitaux de Paris, Hôpital Cochin, Paris, France

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, including the transcription factor CREB (cAMP response element-binding protein), responsible for the stimulation of cAMP-dependent genes transcription. Phosphodiesterases, involved in cAMP degradation, act as negative regulators of this pathway. ACTH is

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Y Zhou
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S Eppenberger-Castori
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U Eppenberger
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C C Benz
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tethering and coactivation of other DNA-bound transcription factor complexes such as AP-1, Sp1, C/EBPβ and CREB) gene induction. Importantly, the net transcriptional effect of crosstalk that phosphorylates ER and its many transcriptional coregulators

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M Muşat
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M Korbonits
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B Kola
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N Borboli
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M R Hanson
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A M Nanzer
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J Grigson
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S Jordan
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D G Morris
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M Gueorguiev
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M Coculescu
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S Basuand
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A B Grossman
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has a number of downstream substrates that may contribute to malignant transformation: these include apoptotic factor Bad, procaspase-9, inhibitor of nuclear factor kappa B kinase (IKK), cAMP-response-element-binding protein (CREB), the forkhead family

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Peng Hou Laboratory for Cellular and Molecular Thyroid Research, Division of Endocrinology and Metabolism, The Johns Hopkins University School of Medicine, 1830 East Monument Street, Suite 333, Baltimore, Maryland 21287, USA

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Dingxie Liu Laboratory for Cellular and Molecular Thyroid Research, Division of Endocrinology and Metabolism, The Johns Hopkins University School of Medicine, 1830 East Monument Street, Suite 333, Baltimore, Maryland 21287, USA

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Mingzhao Xing Laboratory for Cellular and Molecular Thyroid Research, Division of Endocrinology and Metabolism, The Johns Hopkins University School of Medicine, 1830 East Monument Street, Suite 333, Baltimore, Maryland 21287, USA

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, APOLD1 , APP, ATP9A , CD5L, CPEB1 , CREB1, Cu+, CYP26A1 , DUSP14, FSH, GM10681, GTPASE, hCG, hydrogen peroxide, KIAA0247 , MAP3K5 (includes EG: 293015), MCL1, NOS3, NOX5, octopamine, PAPD7, PCNA, POLD4, POLE, POLI , POLK, POLM, POLQ, PTPase, SFRS13

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Fabio R Faucz Section on Endocrinology & Genetics, Program on Developmental Endocrinology & Genetics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland, United States of America

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Anelia D Horvath Department of Pharmacology and Physiology, School of Medicine and Health Sciences, The George Washington University, Washington, District of Columbia, United States of America

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Guillaume Assié Université Paris Cité, CNRS UMR8104, INSERM U1016, Institut Cochin, Paris, France
Endocrine Department, Center for Rare Adrenal Diseases, AP-HP, Hôpital Cochin, Paris, France

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Madson Q Almeida Section on Endocrinology & Genetics, Program on Developmental Endocrinology & Genetics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland, United States of America
Adrenal Unit, Laboratory of Molecular and Cellular Endocrinology LIM/25, Division of Endocrinology and Metabolism, University of Sao Paulo Medical School, São Paulo, Brasil

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Eva Szarek Section on Endocrinology & Genetics, Program on Developmental Endocrinology & Genetics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland, United States of America

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Sosipatros Boikos Section on Endocrinology & Genetics, Program on Developmental Endocrinology & Genetics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland, United States of America

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Anna Angelousi Section on Endocrinology & Genetics, Program on Developmental Endocrinology & Genetics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland, United States of America

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Isaac Levy Section on Endocrinology & Genetics, Program on Developmental Endocrinology & Genetics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland, United States of America

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Andrea G Maria Section on Endocrinology & Genetics, Program on Developmental Endocrinology & Genetics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland, United States of America

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Ajay Chitnis Laboratory of Molecular Genetics, Section on Neural Developmental Dynamics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland, United States of America

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Cristina R Antonescu Department of Pathology, Memorial Sloan-Kettering Cancer Center, New York, New York, United States of America

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Rainer Claus Hematology and Oncology, Medical Faculty, University of Augsburg, Augsburg, Germany

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Jérôme Bertherat Université Paris Cité, CNRS UMR8104, INSERM U1016, Institut Cochin, Paris, France
Endocrine Department, Center for Rare Adrenal Diseases, AP-HP, Hôpital Cochin, Paris, France

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Christoph Plass Division of Cancer Epigenomics, German Cancer Research Center, Heidelberg, Germany

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Charis Eng Genomic Medicine Institute, Lerner Research Institute, and Taussig Cancer Institute, Cleveland Clinic, Cleveland, Ohio, United States of America

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Constantine A Stratakis Section on Endocrinology & Genetics, Program on Developmental Endocrinology & Genetics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland, United States of America
Human Genetics & Precision Medicine, IMBB, Foundation for Research & Technology Hellas, Heraklion, Crete, Greece
Research Institute, ELPEN, Pikermi, Athens, Greece

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vitro determination of the role of DNA methylation on transcription factor binding using AlphaScreen(R) analysis: focus on CREB1 binding at hBDNF promoter IV . Journal of Neuroscience Methods 341 108720 . ( https://doi.org/10.1016/j.jneumeth.2020

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Yulia Koryakina Department of Microbiology Immunology, and Cancer Biology

UVA Cancer Center University of Virginia, PO Box 800734, Charlottesville, Virginia 22908, USA

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Huy Q Ta Department of Microbiology Immunology, and Cancer Biology

UVA Cancer Center University of Virginia, PO Box 800734, Charlottesville, Virginia 22908, USA

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Daniel Gioeli Department of Microbiology Immunology, and Cancer Biology

UVA Cancer Center University of Virginia, PO Box 800734, Charlottesville, Virginia 22908, USA
Department of Microbiology Immunology, and Cancer Biology

UVA Cancer Center University of Virginia, PO Box 800734, Charlottesville, Virginia 22908, USA

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critical reading of the manuscript. References Aarnisalo P Palvimo JJ Janne OA 1998 CREB-binding protein in androgen receptor-mediated signaling . PNAS 95 2122 – 2127 . ( doi:10.1073/pnas.95.5.2122 ). Aho TL Sandholm J Peltola KJ

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Alistair Ring Academic Department of Biochemistry, Royal Marsden Hospital, Fulham Rd, London. SW3 6JJ, UK

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Mitch Dowsett Academic Department of Biochemistry, Royal Marsden Hospital, Fulham Rd, London. SW3 6JJ, UK

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, CREB-binding protein (CBP), p300/CBP-associated factor (PCAF), and the TRAP/DRIP/SMCC complex ( Chen et al. 1997 , Sudarsanam & Winston 2000 , Ito & Roeder 2001 , Vo & Goodman 2001 ). These proteins associate with each other and the general

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Willem-Jan Welboren
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Fred C G J Sweep Department of Molecular Biology, Radiation Oncology, Faculty of Science, Nijmegen Centre for Molecular Life Sciences, Radboud University Nijmegen, PO Box 9101, HB Nijmegen, The Netherlands Departments of

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Paul N Span Department of Molecular Biology, Radiation Oncology, Faculty of Science, Nijmegen Centre for Molecular Life Sciences, Radboud University Nijmegen, PO Box 9101, HB Nijmegen, The Netherlands Departments of
Department of Molecular Biology, Radiation Oncology, Faculty of Science, Nijmegen Centre for Molecular Life Sciences, Radboud University Nijmegen, PO Box 9101, HB Nijmegen, The Netherlands Departments of

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Hendrik G Stunnenberg
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-box) motif, which facilitates the interaction of the cofactor with the AF-2 domain of the ERα. One function of these cofactors is to recruit other proteins such as CREB-binding protein (CBP)/p300 and pCAF that have HAT activity. The CBP is a not only a

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Marc Lacroix Laboratoire Jean-Claude Heuson de Cancérologie Mammaire, Institut Jules Bordet – Université Libre de Bruxelles, 127 boulevard de Waterloo, B-1000 Bruxelles, Belgium

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Robert-Alain Toillon Laboratoire Jean-Claude Heuson de Cancérologie Mammaire, Institut Jules Bordet – Université Libre de Bruxelles, 127 boulevard de Waterloo, B-1000 Bruxelles, Belgium

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Guy Leclercq Laboratoire Jean-Claude Heuson de Cancérologie Mammaire, Institut Jules Bordet – Université Libre de Bruxelles, 127 boulevard de Waterloo, B-1000 Bruxelles, Belgium

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CHK1 and CHK2), Ser366 (by CHK2 only) and Thr387 (by CHK1 only). These events may alter the pattern of acetylation at Lys373 and Lys382, but not at Lys320, thus distinguishing between P300/CREB-binding protein (CBP) and P300/CBP-associated factor (PCAF

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