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Cristina Velasco Laboratorio de Fisioloxía Animal, Departamento de Fisiología de Peces y Biotecnología, Departamento de Bioloxía Funcional e Ciencias da Saúde, Facultade de Bioloxía, Universidade de Vigo, 36310 Vigo, Spain

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Marta Librán-Pérez Laboratorio de Fisioloxía Animal, Departamento de Fisiología de Peces y Biotecnología, Departamento de Bioloxía Funcional e Ciencias da Saúde, Facultade de Bioloxía, Universidade de Vigo, 36310 Vigo, Spain

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Cristina Otero-Rodiño Laboratorio de Fisioloxía Animal, Departamento de Fisiología de Peces y Biotecnología, Departamento de Bioloxía Funcional e Ciencias da Saúde, Facultade de Bioloxía, Universidade de Vigo, 36310 Vigo, Spain

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Marcos A López-Patiño Laboratorio de Fisioloxía Animal, Departamento de Fisiología de Peces y Biotecnología, Departamento de Bioloxía Funcional e Ciencias da Saúde, Facultade de Bioloxía, Universidade de Vigo, 36310 Vigo, Spain

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Jesús M Míguez Laboratorio de Fisioloxía Animal, Departamento de Fisiología de Peces y Biotecnología, Departamento de Bioloxía Funcional e Ciencias da Saúde, Facultade de Bioloxía, Universidade de Vigo, 36310 Vigo, Spain

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José Miguel Cerdá-Reverter Laboratorio de Fisioloxía Animal, Departamento de Fisiología de Peces y Biotecnología, Departamento de Bioloxía Funcional e Ciencias da Saúde, Facultade de Bioloxía, Universidade de Vigo, 36310 Vigo, Spain

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José L Soengas Laboratorio de Fisioloxía Animal, Departamento de Fisiología de Peces y Biotecnología, Departamento de Bioloxía Funcional e Ciencias da Saúde, Facultade de Bioloxía, Universidade de Vigo, 36310 Vigo, Spain

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with changes in the activity of integrative sensors like 5′-AMP-activated protein kinase (AMPK) and sirtuin 1 (SIRT1), is associated with the inhibition of the orexigenic factors AgRP and NPY and the enhancement of the anorexigenic factors POMC and CART

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Pouneh K Fazeli Neuroendocrine Unit, Massachusetts General Hospital, 55 Fruit Street, Bulfinch 457, Boston, Massachusetts 02114, USA

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Anne Klibanski Neuroendocrine Unit, Massachusetts General Hospital, 55 Fruit Street, Bulfinch 457, Boston, Massachusetts 02114, USA

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resistance in starvation may result from a decrease in STAT5 phosphorylation, mediated by fibroblast growth factor 21 (FGF21) and/or Sirtuin 1 (SIRT1). States of malnutrition A number of models of malnutrition have been studied to better understand the state

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Ricardo J Samms School of Life Sciences, Lilly Research Laboratories, Chemistry Department, Queen's Medical Centre, University of Nottingham, Nottingham NG7 2UH, UK

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Michelle Murphy School of Life Sciences, Lilly Research Laboratories, Chemistry Department, Queen's Medical Centre, University of Nottingham, Nottingham NG7 2UH, UK

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Maxine J Fowler School of Life Sciences, Lilly Research Laboratories, Chemistry Department, Queen's Medical Centre, University of Nottingham, Nottingham NG7 2UH, UK

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Scott Cooper School of Life Sciences, Lilly Research Laboratories, Chemistry Department, Queen's Medical Centre, University of Nottingham, Nottingham NG7 2UH, UK

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Paul Emmerson School of Life Sciences, Lilly Research Laboratories, Chemistry Department, Queen's Medical Centre, University of Nottingham, Nottingham NG7 2UH, UK

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Tamer Coskun School of Life Sciences, Lilly Research Laboratories, Chemistry Department, Queen's Medical Centre, University of Nottingham, Nottingham NG7 2UH, UK

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Andrew C Adams School of Life Sciences, Lilly Research Laboratories, Chemistry Department, Queen's Medical Centre, University of Nottingham, Nottingham NG7 2UH, UK

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Alexei Kharitonenkov School of Life Sciences, Lilly Research Laboratories, Chemistry Department, Queen's Medical Centre, University of Nottingham, Nottingham NG7 2UH, UK

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Francis J P Ebling School of Life Sciences, Lilly Research Laboratories, Chemistry Department, Queen's Medical Centre, University of Nottingham, Nottingham NG7 2UH, UK

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Kostas Tsintzas School of Life Sciences, Lilly Research Laboratories, Chemistry Department, Queen's Medical Centre, University of Nottingham, Nottingham NG7 2UH, UK

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, Danvers, MA, USA, #3661), PGC1α (Calbiochem, Billerica, MA, USA, #516557), PPARα (Abcam, Cambridge, UK, #8934), sirtuin-1 (SIRT1) (Cell Signalling, #2310) and housekeeping protein cyclophilin-B (Abcam, #74173) were diluted in Tris-buffered saline (TBS) and

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Haiyong Chen Li Ka Sing Faculty of Medicine, Department of Medicine and Therapeutics, Centre for Biosystems and Genome Network Medicine, Department of Clinical Oncology, School of Chinese Medicine, The University of Hong Kong, Pok Fu Lam, Hong Kong

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Hui-Yao Lan Li Ka Sing Faculty of Medicine, Department of Medicine and Therapeutics, Centre for Biosystems and Genome Network Medicine, Department of Clinical Oncology, School of Chinese Medicine, The University of Hong Kong, Pok Fu Lam, Hong Kong

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Dimitrios H Roukos Li Ka Sing Faculty of Medicine, Department of Medicine and Therapeutics, Centre for Biosystems and Genome Network Medicine, Department of Clinical Oncology, School of Chinese Medicine, The University of Hong Kong, Pok Fu Lam, Hong Kong

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William C Cho Li Ka Sing Faculty of Medicine, Department of Medicine and Therapeutics, Centre for Biosystems and Genome Network Medicine, Department of Clinical Oncology, School of Chinese Medicine, The University of Hong Kong, Pok Fu Lam, Hong Kong

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death 4; PDK1, phosphoinositide-dependent protein kinase 1; Rab27a, member RAS oncogene family; Sirt1, sirtuin (silent mating type information regulation 2 homolog) 1; Vamp2, vesicle-associated membrane protein 2; UCP2, uncoupling protein 2. miRNAs alter

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Ralf Baumeister Bio 3, Bioinformatics and Molecular Genetics, University of Freiburg, Germany
ZBSA – Freiburg Center for Systems Biology, University of Freiburg, Germany
Renal Division, University Hospital Freiburg, Germany

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Elke Schaffitzel Bio 3, Bioinformatics and Molecular Genetics, University of Freiburg, Germany
ZBSA – Freiburg Center for Systems Biology, University of Freiburg, Germany
Renal Division, University Hospital Freiburg, Germany

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Maren Hertweck Bio 3, Bioinformatics and Molecular Genetics, University of Freiburg, Germany
ZBSA – Freiburg Center for Systems Biology, University of Freiburg, Germany
Renal Division, University Hospital Freiburg, Germany

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worm, yet its similarity to the mammalian Homo sapiens SIRT-1 proteins suggests that it may involve deacetylation in Lys residues ( Daitoku et al. 2004 ). Indeed, transgenic expression of sir-2.1 increases the lifespan of C. elegans up to 50% in

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Shannon M Bailey Division of Molecular and Cellular Pathology, Division of Cardiovascular Diseases, Department of Pathology

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Uduak S Udoh Division of Molecular and Cellular Pathology, Division of Cardiovascular Diseases, Department of Pathology

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Martin E Young Division of Molecular and Cellular Pathology, Division of Cardiovascular Diseases, Department of Pathology

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interconverted between its oxidized (NAD + ) and reduced (NADH) forms. However, NAD + may also function as a cell signaling molecule via roles in PTMs; ADP-ribosylation and NAD + -dependent deacetylation. For example, NAD + activates sirtuin 1 (SIRT1

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Laura Marroqui Centro de Investigación Biomédica en Red de Diabetes y Enfermedades Metabólicas Asociadas (CIBERDEM) and Institute of Bioengineering, Miguel Hernández University of Elche, Alicante, Spain

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Eva Tudurí Centro de Investigación Biomédica en Red de Diabetes y Enfermedades Metabólicas Asociadas (CIBERDEM) and Institute of Bioengineering, Miguel Hernández University of Elche, Alicante, Spain

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Paloma Alonso-Magdalena Centro de Investigación Biomédica en Red de Diabetes y Enfermedades Metabólicas Asociadas (CIBERDEM) and Institute of Bioengineering, Miguel Hernández University of Elche, Alicante, Spain

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Iván Quesada Centro de Investigación Biomédica en Red de Diabetes y Enfermedades Metabólicas Asociadas (CIBERDEM) and Institute of Bioengineering, Miguel Hernández University of Elche, Alicante, Spain

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Ángel Nadal Centro de Investigación Biomédica en Red de Diabetes y Enfermedades Metabólicas Asociadas (CIBERDEM) and Institute of Bioengineering, Miguel Hernández University of Elche, Alicante, Spain

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Reinaldo Sousa dos Santos Centro de Investigación Biomédica en Red de Diabetes y Enfermedades Metabólicas Asociadas (CIBERDEM) and Institute of Bioengineering, Miguel Hernández University of Elche, Alicante, Spain

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( Zhang et al. 2015 b , Zhang & Choudhury 2017 ). Additionally, levels of sirtuins (SIRT) 1 and 3, two NAD + -dependent deacetylases with different roles in the control of mitochondrial biogenesis ( Nogueiras et al. 2012 ), were also decreased

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Zhongxiuzi Gao Department of Basic Medical Sciences, Medical College, Xiamen University, Xiamen, China

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Li Zhang Department of Basic Medical Sciences, Medical College, Xiamen University, Xiamen, China

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Wenting Xie Department of Basic Medical Sciences, Medical College, Xiamen University, Xiamen, China

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Siqi Wang Department of Basic Medical Sciences, Medical College, Xiamen University, Xiamen, China

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Xiaorui Bao Department of Basic Medical Sciences, Medical College, Xiamen University, Xiamen, China

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Yuli Guo Department of Basic Medical Sciences, Medical College, Xiamen University, Xiamen, China

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Houjian Zhang Department of Basic Medical Sciences, Medical College, Xiamen University, Xiamen, China

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Qingzhong Hu Department of Basic Medical Sciences, Medical College, Xiamen University, Xiamen, China

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Yi Chen Department of Basic Medical Sciences, Medical College, Xiamen University, Xiamen, China

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Zeen Wang Department of Basic Medical Sciences, Medical College, Xiamen University, Xiamen, China

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Maoqiang Xue Department of Basic Medical Sciences, Medical College, Xiamen University, Xiamen, China

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Guanghui Jin Department of Basic Medical Sciences, Medical College, Xiamen University, Xiamen, China

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53 1087 – 1097 . ( doi:10.1369/jhc.5C6684.2005 ) Cao Y Xue Y Xue L Jiang X Wang X Zhang Z Yang J Lu J Zhang C Wang W 2013 Hepatic menin recruits SIRT1 to control liver steatosis through histone

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Shaodong Guo Division of Molecular Cardiology, Department of Medicine, College of Medicine, Texas A&M University Health Science Center, Scott & White, Central Texas Veterans Health Care System, 1901 South 1st Street, Bldg. 205, Temple, Texas 76504, USA

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-phosphorylated and -regulated kinase 1A; Ub, ubiquitin; SIRT2, NAD + -dependent histone deacetylase silent information regulator 2; CBP, CREB-binding protein; p300, global transcription factor cofactor; P, phosphorylation; Me, methylation; G, glycosylation; Ac

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Jia Sun of Intensive Care Unit, The First Affiliated Hospital of Wenzhou Medical University, Wenzhou, China
School of Pharmaceutical Science, Wenzhou Medical University, Wenzhou, China

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Haiping Zhu of Intensive Care Unit, The First Affiliated Hospital of Wenzhou Medical University, Wenzhou, China

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Xiaorong Wang of Intensive Care Unit, The First Affiliated Hospital of Wenzhou Medical University, Wenzhou, China

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Qiuqi Gao of Intensive Care Unit, The First Affiliated Hospital of Wenzhou Medical University, Wenzhou, China

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Zhuoying Li of Intensive Care Unit, The First Affiliated Hospital of Wenzhou Medical University, Wenzhou, China

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Huiya Huang of Intensive Care Unit, The First Affiliated Hospital of Wenzhou Medical University, Wenzhou, China

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(version 6.0, Media Cybernetics). Luciferase assays of promoter activities for Nrf2/ARE, SIRT1 and PGC-1α Luciferase assays were performed as described elsewhere ( Lee et al. 2014 , Li et al. 2015 ). ARE- bla construct was used for Nrf2/ARE

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