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Caiyan Mo Department of Endocrinology, Beijing Tiantan Hospital, Capital Medical University, Beijing, China

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Tao Tong Department of Endocrinology, Beijing Tiantan Hospital, Capital Medical University, Beijing, China

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Ying Guo Department of Endocrinology, Beijing Tiantan Hospital, Capital Medical University, Beijing, China

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Zheng Li Department of Endocrinology, Beijing Tiantan Hospital, Capital Medical University, Beijing, China

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Liyong Zhong Department of Endocrinology, Beijing Tiantan Hospital, Capital Medical University, Beijing, China

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ability of the patient's IgG to block TSH binding and induce the production of cyclic adenosine monophosphate (cAMP), and the activity index and symptom of GD improved after surgical remission of acromegaly, confirming the hypothesis that the GH−IGF-1 axis

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Bjørn O Åsvold Department of Endocrinology, Department of Public Health, Department of Cancer Research and Molecular Medicine, Department of Medical Biochemistry, St Olavs Hospital, Trondheim University Hospital, P O Box 3250 Sluppen, N-7006 Trondheim, Norway
Department of Endocrinology, Department of Public Health, Department of Cancer Research and Molecular Medicine, Department of Medical Biochemistry, St Olavs Hospital, Trondheim University Hospital, P O Box 3250 Sluppen, N-7006 Trondheim, Norway

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Valdemar Grill Department of Endocrinology, Department of Public Health, Department of Cancer Research and Molecular Medicine, Department of Medical Biochemistry, St Olavs Hospital, Trondheim University Hospital, P O Box 3250 Sluppen, N-7006 Trondheim, Norway
Department of Endocrinology, Department of Public Health, Department of Cancer Research and Molecular Medicine, Department of Medical Biochemistry, St Olavs Hospital, Trondheim University Hospital, P O Box 3250 Sluppen, N-7006 Trondheim, Norway

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Ketil Thorstensen Department of Endocrinology, Department of Public Health, Department of Cancer Research and Molecular Medicine, Department of Medical Biochemistry, St Olavs Hospital, Trondheim University Hospital, P O Box 3250 Sluppen, N-7006 Trondheim, Norway

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Marit R Bjørgaas Department of Endocrinology, Department of Public Health, Department of Cancer Research and Molecular Medicine, Department of Medical Biochemistry, St Olavs Hospital, Trondheim University Hospital, P O Box 3250 Sluppen, N-7006 Trondheim, Norway
Department of Endocrinology, Department of Public Health, Department of Cancer Research and Molecular Medicine, Department of Medical Biochemistry, St Olavs Hospital, Trondheim University Hospital, P O Box 3250 Sluppen, N-7006 Trondheim, Norway

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1 nmol/l, and these were assigned the half value of the minimal detection limit. Plasma dexamethasone was measured during March 2010 using the direct RIA from IgG Corporation (Nashville, TN, USA) as described by Ritchie et al . (7, 8) , with minor

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Yiqiong Ma Division of Nephrology, Renmin Hospital of Wuhan University, Wuhan, Hubei, People’s Republic of China

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Zhaowei Chen Division of Nephrology, Renmin Hospital of Wuhan University, Wuhan, Hubei, People’s Republic of China

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Yu Tao Division of Nephrology, Renmin Hospital of Wuhan University, Wuhan, Hubei, People’s Republic of China

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Jili Zhu Division of Nephrology, Renmin Hospital of Wuhan University, Wuhan, Hubei, People’s Republic of China

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Hongxia Yang Division of Nephrology, Renmin Hospital of Wuhan University, Wuhan, Hubei, People’s Republic of China

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Wei Liang Division of Nephrology, Renmin Hospital of Wuhan University, Wuhan, Hubei, People’s Republic of China

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Guohua Ding Division of Nephrology, Renmin Hospital of Wuhan University, Wuhan, Hubei, People’s Republic of China

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Technology; Drp1 rabbit monoclonal antibody, 1:100, Abcam) overnight at 4°C. FITC/TRITC-conjugated IgG was used as a secondary antibody and was incubated with the sections at 37°C for 90 min in the dark. All microscopic images were recorded using a confocal

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Marko Stojanovic Neuroendocrinology Department, Clinic for Endocrinology, Diabetes and Metabolic Diseases, Clinical Centre of Serbia, Belgrade, Serbia
University of Belgrade, Medical Faculty, Belgrade, Serbia

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Zida Wu Department of Medicine for Endocrinology, Diabetes and Nutritional Medicine, Charité Universitätsmedizin, Campus Mitte, Berlin, Germany

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Craig E Stiles Centre for Endocrinology, William Harvey Research Institute, Barts and the London School of Medicine and Dentistry, Queen Mary University of London, London, UK

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Dragana Miljic Neuroendocrinology Department, Clinic for Endocrinology, Diabetes and Metabolic Diseases, Clinical Centre of Serbia, Belgrade, Serbia
University of Belgrade, Medical Faculty, Belgrade, Serbia

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Ivan Soldatovic University of Belgrade, Medical Faculty, Belgrade, Serbia
Insitute of Medical Statistics and Informatics, Belgrade, Serbia

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Sandra Pekic Neuroendocrinology Department, Clinic for Endocrinology, Diabetes and Metabolic Diseases, Clinical Centre of Serbia, Belgrade, Serbia
University of Belgrade, Medical Faculty, Belgrade, Serbia

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Mirjana Doknic Neuroendocrinology Department, Clinic for Endocrinology, Diabetes and Metabolic Diseases, Clinical Centre of Serbia, Belgrade, Serbia
University of Belgrade, Medical Faculty, Belgrade, Serbia

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Milan Petakov Neuroendocrinology Department, Clinic for Endocrinology, Diabetes and Metabolic Diseases, Clinical Centre of Serbia, Belgrade, Serbia
University of Belgrade, Medical Faculty, Belgrade, Serbia

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Vera Popovic University of Belgrade, Medical Faculty, Belgrade, Serbia

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Christian Strasburger Department of Medicine for Endocrinology, Diabetes and Nutritional Medicine, Charité Universitätsmedizin, Campus Mitte, Berlin, Germany

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Márta Korbonits Centre for Endocrinology, William Harvey Research Institute, Barts and the London School of Medicine and Dentistry, Queen Mary University of London, London, UK

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were screened for anti-AIP activity after 10–12 days of culture using biotinylated AIP. Hybridoma cells corresponding to the highest signals of supernatants were cloned at least twice by limiting dilution. The IgG subclass of the monoclonal antibodies

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Clarissa Souza Barthem Laboratório de Adaptações Metabólicas, Programa de Bioquímica e Biofísica Celular, Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil

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Camila Lüdke Rossetti Laboratório de Adaptações Metabólicas, Programa de Bioquímica e Biofísica Celular, Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil
Laboratório de Fisiologia Endócrina Doris Rosenthal, Instituto de Biofísica Carlos Chagas Filho, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil

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Denise P Carvalho Laboratório de Fisiologia Endócrina Doris Rosenthal, Instituto de Biofísica Carlos Chagas Filho, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil

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Wagner Seixas da-Silva Laboratório de Adaptações Metabólicas, Programa de Bioquímica e Biofísica Celular, Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil

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-acetyl-CoA carboxylase (Ser79) #3661 (Cell Signaling) 1:2500 Acetyl-CoA carboxylase #3662 (Cell Signaling) 1:2500 Monoclonal anti-α-tubulin T5168 (Sigma) 1:25,000 Anti-rabbit IgG A0545 (Sigma) 1:2500 Anti-mouse IgG A3673 (Sigma

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Caio Jordão Teixeira Department of Pharmacology, Faculty of Medical Sciences, State University of Campinas, Campinas, Brazil

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Junia Carolina Santos-Silva Department of Pharmacology, Faculty of Medical Sciences, State University of Campinas, Campinas, Brazil

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Dailson Nogueira de Souza Department of Pharmacology, Faculty of Medical Sciences, State University of Campinas, Campinas, Brazil

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Alex Rafacho Department of Physiological Sciences, Center of Biological Sciences, Federal University of Santa Catarina, Florianópolis, Brazil

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Gabriel Forato Anhe Department of Pharmacology, Faculty of Medical Sciences, State University of Campinas, Campinas, Brazil

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Silvana Bordin Department of Physiology and Biophysics, Institute of Biomedical Sciences, University of Sao Paulo, Sao Paulo, Brazil

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diluted in TBS containing 3% BSA overnight at 4°C. Subsequently, sections were washed with TBS and incubated either with HRP-conjugated anti-guinea-pig IgG (1:1000; Invitrogen; cat. no. 614620) or HRP-conjugated anti-rabbit IgG (Nichirei Bioscience, Tokyo

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Melissa Braga Department of Internal Medicine, Charles R. Drew University of Medicine and Science, Los Angeles, California, USA

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Zena Simmons Department of Health & Life Sciences, Charles R. Drew University of Medicine and Science, Los Angeles, California, USA

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Keith C Norris Department of Medicine, David Geffen School of Medicine at UCLA, Los Angeles, California, USA

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Monica G Ferrini Department of Internal Medicine, Charles R. Drew University of Medicine and Science, Los Angeles, California, USA
Department of Health & Life Sciences, Charles R. Drew University of Medicine and Science, Los Angeles, California, USA
Department of Medicine, David Geffen School of Medicine at UCLA, Los Angeles, California, USA

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Jorge N Artaza Department of Internal Medicine, Charles R. Drew University of Medicine and Science, Los Angeles, California, USA
Department of Health & Life Sciences, Charles R. Drew University of Medicine and Science, Los Angeles, California, USA
Department of Medicine, David Geffen School of Medicine at UCLA, Los Angeles, California, USA

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, we either omitted the first antibody or replaced it with a rabbit IgG isotype antibody ( 11 ). Double labeling immunofluorescence detection of PAX7 and VDR The double localization of PAX7 and VDR was carried out on 2% p -formaldehyde

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Satoshi Inoue Department of Pathology & Laboratory Medicine, University of Rochester Medical Center, Rochester, New York, USA
James P. Wilmot Cancer Institute, University of Rochester Medical Center, Rochester, New York, USA
Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA
James Buchanan Brady Urological Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA

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Taichi Mizushima Department of Pathology & Laboratory Medicine, University of Rochester Medical Center, Rochester, New York, USA
James P. Wilmot Cancer Institute, University of Rochester Medical Center, Rochester, New York, USA
Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA
James Buchanan Brady Urological Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA

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Hiroki Ide Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA
James Buchanan Brady Urological Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA

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Guiyang Jiang Department of Pathology & Laboratory Medicine, University of Rochester Medical Center, Rochester, New York, USA
James P. Wilmot Cancer Institute, University of Rochester Medical Center, Rochester, New York, USA

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Takuro Goto Department of Pathology & Laboratory Medicine, University of Rochester Medical Center, Rochester, New York, USA
James P. Wilmot Cancer Institute, University of Rochester Medical Center, Rochester, New York, USA

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Yujiro Nagata Department of Pathology & Laboratory Medicine, University of Rochester Medical Center, Rochester, New York, USA
James P. Wilmot Cancer Institute, University of Rochester Medical Center, Rochester, New York, USA

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George J Netto Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA
James Buchanan Brady Urological Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA
Department of Pathology, University of Alabama at Birmingham, Birmingham, Alabama, USA

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Hiroshi Miyamoto Department of Pathology & Laboratory Medicine, University of Rochester Medical Center, Rochester, New York, USA
James P. Wilmot Cancer Institute, University of Rochester Medical Center, Rochester, New York, USA
Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA
James Buchanan Brady Urological Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA
Department of Urology, University of Rochester Medical Center, Rochester, New York, USA

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PVDF membrane electronically, blocked and incubated with an appropriate dilution of each specific antibody and a secondary antibody (anti-mouse IgG HRP-linked antibody or anti-rabbit IgG HRP-linked antibody; Cell Signaling Technology) followed by

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Marra Jai Aghajani Ingham Institute for Applied Medical Research, Liverpool, New South Wales, Australia
School of Medicine, Western Sydney University, Campbelltown, New South Wales, Australia

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Tao Yang School of Medicine, Western Sydney University, Campbelltown, New South Wales, Australia
Saint Vincent’s Clinical School, UNSW Sydney, Sydney, Australia
SydPath, Saint Vincent’s Hospital, Sydney, Australia

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Ulf Schmitz Computational BioMedicine Laboratory Centenary Institute, The University of Sydney, Camperdown, New South Wales, Australia
Gene & Stem Cell Therapy Program Centenary Institute, The University of Sydney, Camperdown, New South Wales, Australia
Faculty of Medicine & Health, The University of Sydney, Camperdown, New South Wales, Australia

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Alexander James Ingham Institute for Applied Medical Research, Liverpool, New South Wales, Australia

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Charles Eugenio McCafferty Ingham Institute for Applied Medical Research, Liverpool, New South Wales, Australia
School of Medicine, Western Sydney University, Campbelltown, New South Wales, Australia

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Paul de Souza Ingham Institute for Applied Medical Research, Liverpool, New South Wales, Australia
School of Medicine, Western Sydney University, Campbelltown, New South Wales, Australia
School of Medicine, University of Wollongong, New South Wales, Australia

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Navin Niles Ingham Institute for Applied Medical Research, Liverpool, New South Wales, Australia
School of Medicine, Western Sydney University, Campbelltown, New South Wales, Australia
Department of Head & Neck Surgery, Liverpool Hospital, Liverpool, New South Wales, Australia
Department of Clinical Medicine, Faculty of Medicine and Health Sciences, Macquarie University, Sydney, Australia

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Tara L Roberts Ingham Institute for Applied Medical Research, Liverpool, New South Wales, Australia
School of Medicine, Western Sydney University, Campbelltown, New South Wales, Australia
South West Sydney Clinical School, UNSW Sydney, Sydney, Australia

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-vimentin (ab92547) (Abcam) and β-actin (Cell Signaling Technology), which was used as an endogenous protein for normalisation. Blots were then washed and incubated with a 1:1000 dilution of anti-Rabbit IgG H&L (HRP)-conjugated secondary (Cell Signaling

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Lianghui You Women’s Hospital of Nanjing Medical University, Nanjing Maternity and Child Health Care Hospital, Nanjing, China
Institute of Pediatrics, Nanjing Medical University, Nanjing, China

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Yan Wang Women’s Hospital of Nanjing Medical University, Nanjing Maternity and Child Health Care Hospital, Nanjing, China
Institute of Pediatrics, Nanjing Medical University, Nanjing, China

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Yao Gao Department of Endocrinology, Children’s Hospital of Nanjing Medical University, Nanjing, China

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Xingyun Wang Women’s Hospital of Nanjing Medical University, Nanjing Maternity and Child Health Care Hospital, Nanjing, China

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Xianwei Cui Women’s Hospital of Nanjing Medical University, Nanjing Maternity and Child Health Care Hospital, Nanjing, China

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Yanyan Zhang Beijing Chaoyang Distirct Maternal and Child Health Care Hospital, Beijing, China

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Lingxia Pang Women’s Hospital of Nanjing Medical University, Nanjing Maternity and Child Health Care Hospital, Nanjing, China

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Chenbo Ji Women’s Hospital of Nanjing Medical University, Nanjing Maternity and Child Health Care Hospital, Nanjing, China
Institute of Pediatrics, Nanjing Medical University, Nanjing, China

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Xirong Guo Tongren Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China

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Xia Chi Women’s Hospital of Nanjing Medical University, Nanjing Maternity and Child Health Care Hospital, Nanjing, China
Institute of Pediatrics, Nanjing Medical University, Nanjing, China

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secondary antibodies were horse radish peroxidase-conjugated goat anti-rabbit IgG and goat anti-mouse IgG from Beijing Zhong Shan Biotechnology CO (Beijing, China). Measurement of oxygen consumption and lipolysis capacity Mouse brown pre

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