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Maria Angela De Stefano Department of Public Health, University of Naples “Federico II”, Naples, Italy

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Tommaso Porcelli Department of Public Health, University of Naples “Federico II”, Naples, Italy

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Martin Schlumberger Department of Endocrine Oncology, Gustave Roussy and University Paris-Saclay, Villejuif, France

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Domenico Salvatore Department of Public Health, University of Naples “Federico II”, Naples, Italy
CEINGE Biotecnologie Avanzate Scarl, Naples, Italy

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',5'-cyclic adenosine monophosphate response element binding protein (CREB) is functionally reduced in human toxic thyroid adenomas . Endocrinology 141 722 – 730 . ( https://doi.org/10.1210/endo.141.2.7331 ) 10650954 Callebaut I Curcio-Morelli C Mornon

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Berna C Özdemir Department of Oncology, Centre Hospitalier Universitaire Vaudois, Lausanne, Switzerland
International Cancer Prevention Institute, Epalinges, Switzerland

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George Sflomos ISREC – Swiss Institute for Experimental Cancer Research, School of Life Sciences, Ecole polytechnique fédérale de Lausanne (EPFL), Lausanne, Switzerland

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Cathrin Brisken International Cancer Prevention Institute, Epalinges, Switzerland
ISREC – Swiss Institute for Experimental Cancer Research, School of Life Sciences, Ecole polytechnique fédérale de Lausanne (EPFL), Lausanne, Switzerland

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.1371/journal.pone.0088146 24523878 Quesada I Fuentes E Viso-Leon MC Soria B Ripoll C Nadal A 2002 Low doses of the endocrine disruptor bisphenol-A and the native hormone 17beta-estradiol rapidly activate transcription factor CREB . FASEB Journal 16

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Elizabeth Kopras
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Veena Potluri
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Mei-Ling Bermudez
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Karin Williams
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Scott Belcher Department of Environmental Heath, Department of Pharmacology and Cell Biophysics, University of Cincinnati, 3223 Eden Avenue, Cincinnati, Ohio 45267-0056, USA

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Susan Kasper
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-binding protein (CREB; Fritsche et al . 2005 ). Consequently, expression of stage-specific neuronal markers including nestin, neural cell adhesion molecule (NCAM), synaptophysin (SYP), 2-amino-3-(3-hydroxy-5-methyl-isoxazol-4-yl)propanoic acid (AMPA), and N

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N Burrows School of Pharmacy and Pharmaceutical Sciences, Department of Endocrinology, Department of Pathology, Experimental and Surgical Oncology, Academic Department of Radiation Oncology, University of Manchester, Wilmslow Road, Manchester M20 4BX, UK

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J Resch School of Pharmacy and Pharmaceutical Sciences, Department of Endocrinology, Department of Pathology, Experimental and Surgical Oncology, Academic Department of Radiation Oncology, University of Manchester, Wilmslow Road, Manchester M20 4BX, UK

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R L Cowen School of Pharmacy and Pharmaceutical Sciences, Department of Endocrinology, Department of Pathology, Experimental and Surgical Oncology, Academic Department of Radiation Oncology, University of Manchester, Wilmslow Road, Manchester M20 4BX, UK

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R von Wasielewski School of Pharmacy and Pharmaceutical Sciences, Department of Endocrinology, Department of Pathology, Experimental and Surgical Oncology, Academic Department of Radiation Oncology, University of Manchester, Wilmslow Road, Manchester M20 4BX, UK

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C Hoang-Vu School of Pharmacy and Pharmaceutical Sciences, Department of Endocrinology, Department of Pathology, Experimental and Surgical Oncology, Academic Department of Radiation Oncology, University of Manchester, Wilmslow Road, Manchester M20 4BX, UK

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C M West School of Pharmacy and Pharmaceutical Sciences, Department of Endocrinology, Department of Pathology, Experimental and Surgical Oncology, Academic Department of Radiation Oncology, University of Manchester, Wilmslow Road, Manchester M20 4BX, UK

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K J Williams School of Pharmacy and Pharmaceutical Sciences, Department of Endocrinology, Department of Pathology, Experimental and Surgical Oncology, Academic Department of Radiation Oncology, University of Manchester, Wilmslow Road, Manchester M20 4BX, UK

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G Brabant School of Pharmacy and Pharmaceutical Sciences, Department of Endocrinology, Department of Pathology, Experimental and Surgical Oncology, Academic Department of Radiation Oncology, University of Manchester, Wilmslow Road, Manchester M20 4BX, UK

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degraded in the proteasome via the ubiquitination pathway ( Pouyssegur et al . 2006 ). In hypoxia, HIF-1α is stabilized, translocates to the nucleus and, following heterodimerization with HIF-1β and cofactors like CREB-binding protein (CBP)/p300

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Stephen A Boorjian
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Hannelore V Heemers
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Igor Frank
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Sara A Farmer Department of Urology, Department of Health Sciences Research, Department of Laboratory Medicine and Pathology, Mayo Clinic, Guggenheim 1742, 200 First Street SW, Rochester, Minnesota 55905, USA

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Lucy J Schmidt
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Thomas J Sebo Department of Urology, Department of Health Sciences Research, Department of Laboratory Medicine and Pathology, Mayo Clinic, Guggenheim 1742, 200 First Street SW, Rochester, Minnesota 55905, USA

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Donald J Tindall
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OA 1998 CREB-binding protein in androgen receptor-mediated signaling . PNAS 95 2122 – 2127 . Agoulnik IU Vaid A Bingman WE III Erdeme H Frolov A Smith CL Ayala G Ittmann MM Weigel NL 2005 Role of SRC-1 in the promotion

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J Yang Department of Molecular Biology, Department of Endocrinology, Institute of Basic Medicine

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Y-L Zhao Department of Molecular Biology, Department of Endocrinology, Institute of Basic Medicine

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Z-Q Wu Department of Molecular Biology, Department of Endocrinology, Institute of Basic Medicine

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Y-L Si Department of Molecular Biology, Department of Endocrinology, Institute of Basic Medicine

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Y-G Meng Department of Molecular Biology, Department of Endocrinology, Institute of Basic Medicine

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X-B Fu Department of Molecular Biology, Department of Endocrinology, Institute of Basic Medicine

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Y-M Mu Department of Molecular Biology, Department of Endocrinology, Institute of Basic Medicine

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W-D Han Department of Molecular Biology, Department of Endocrinology, Institute of Basic Medicine

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( Bevan et al . 1999 , Powell et al . 2004 , Heemers & Tindall 2007 ). Moreover, SRC-1 functions as a scaffold protein that attracts additional coactivator proteins such as p300, the p300 homolog CREB-binding protein (CBP), and p300/CBP

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Carl Weidinger Division of Endocrinology and Diabetology, Department of Internal Medicine, University of Leipzig, Philipp-Rosenthal-Strasse 27, D-04103 Leipzig, Germany

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Kerstin Krause Division of Endocrinology and Diabetology, Department of Internal Medicine, University of Leipzig, Philipp-Rosenthal-Strasse 27, D-04103 Leipzig, Germany

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Antje Klagge Division of Endocrinology and Diabetology, Department of Internal Medicine, University of Leipzig, Philipp-Rosenthal-Strasse 27, D-04103 Leipzig, Germany

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Stefan Karger Division of Endocrinology and Diabetology, Department of Internal Medicine, University of Leipzig, Philipp-Rosenthal-Strasse 27, D-04103 Leipzig, Germany

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Dagmar Fuhrer Division of Endocrinology and Diabetology, Department of Internal Medicine, University of Leipzig, Philipp-Rosenthal-Strasse 27, D-04103 Leipzig, Germany

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, nuclear FOXO3a associates with the histone acetylase CREB-binding protein (CREBBP) and P300 ( Daitoku et al . 2004 , Perrot & Rechler 2005 ). This association is required for the assembly of an active initiation complex, responsible for FOXOs

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Carla S Verissimo
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Jan J Molenaar Division of Medical Pharmacology, Department of Human Genetics, Division of Toxicology, Leiden/Amsterdam Center for Drug Research, Gorlaeus Laboratories, Leiden, The Netherlands

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John Meerman Division of Medical Pharmacology, Department of Human Genetics, Division of Toxicology, Leiden/Amsterdam Center for Drug Research, Gorlaeus Laboratories, Leiden, The Netherlands

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Jordi Carreras Puigvert Division of Medical Pharmacology, Department of Human Genetics, Division of Toxicology, Leiden/Amsterdam Center for Drug Research, Gorlaeus Laboratories, Leiden, The Netherlands

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Fieke Lamers Division of Medical Pharmacology, Department of Human Genetics, Division of Toxicology, Leiden/Amsterdam Center for Drug Research, Gorlaeus Laboratories, Leiden, The Netherlands

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Jan Koster Division of Medical Pharmacology, Department of Human Genetics, Division of Toxicology, Leiden/Amsterdam Center for Drug Research, Gorlaeus Laboratories, Leiden, The Netherlands

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Erik H J Danen Division of Medical Pharmacology, Department of Human Genetics, Division of Toxicology, Leiden/Amsterdam Center for Drug Research, Gorlaeus Laboratories, Leiden, The Netherlands

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Bob van de Water Division of Medical Pharmacology, Department of Human Genetics, Division of Toxicology, Leiden/Amsterdam Center for Drug Research, Gorlaeus Laboratories, Leiden, The Netherlands

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Rogier Versteeg Division of Medical Pharmacology, Department of Human Genetics, Division of Toxicology, Leiden/Amsterdam Center for Drug Research, Gorlaeus Laboratories, Leiden, The Netherlands

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Carlos P Fitzsimons
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Erno Vreugdenhil
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expression via Nrf2 2.65×10 −5 Hmox1 (↑↓); Sirt7 (↑↑); Mapk1 (↓↓); Jun (↑↑); Atf4 (↓↓); Nfe2l2 (↓↓); Mafg (↑↑); Creb1 (↓↓); Cryz (↓↓); Keap1 (↑↓); Fos (↑↑); Prkcb1 (↓↓); Por (↑↑); Mapk14 (↓↓); Maff (↑↑); Mafk (↓↓) Cell cycle: G2/M checkpoint 3.10×10 −5 Ywhah

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Cassia Michael Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, New York, USA

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Juliana Moreira Mendonça-Gomes Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, New York, USA

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Clinton Walton DePaolo Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, New York, USA

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Antonio Di Cristofano Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, New York, USA
Department of Medicine (Oncology), Albert Einstein College of Medicine, Bronx, New York, USA
Montefiore-Einstein Comprehensive Cancer Research Center, Albert Einstein College of Medicine, Bronx, New York, USA
Cancer Dormancy Tumor Microenvironment Institute, Albert Einstein College of Medicine, Bronx, New York, USA

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Sofia de Oliveira Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, New York, USA
Montefiore-Einstein Comprehensive Cancer Research Center, Albert Einstein College of Medicine, Bronx, New York, USA
Cancer Dormancy Tumor Microenvironment Institute, Albert Einstein College of Medicine, Bronx, New York, USA
Department of Medicine (Hepatology), Albert Einstein College of Medicine, Bronx, New York, USA
Marion Bessin Liver Research Center, Albert Einstein College of Medicine and Montefiore Medical Center, Bronx, New York, USA

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Bao L Hu X Jin T Chen J Chen J Qian Y Lu X Li L , et al. 2022 CREB3L1 promotes tumor growth and metastasis of anaplastic thyroid carcinoma by remodeling the tumor microenvironment . Molecular Cancer 21 190 . ( https://doi.org/10

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Shyh-Han Tan Department of Cancer Biology, Kimmel Cancer Center, Thomas Jefferson University, 233 South 10th Street, BLSB 309, Philadelphia, Pennsylvania 19107, USA

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Marja T Nevalainen Department of Cancer Biology, Kimmel Cancer Center, Thomas Jefferson University, 233 South 10th Street, BLSB 309, Philadelphia, Pennsylvania 19107, USA

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–706 686–701 686–706 Transactivation domain 722–794 727–787 721–793 726–786 The glycosylation on threonine 92 of STAT5 is found to enhance interaction with the co-activator of transcription CREB-binding protein (CBP; Gewinner et al . 2004 ). Adjacent to

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