242 results on '"Freyssenet, Damien"'
Search Results
2. Myostatin gene invalidation does not prevent skeletal muscle mass loss during experimental sepsis in mice
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Morel, Jérome, primary, Pignard, Anne Sophie, additional, Castells, Josiane, additional, Allibert, Valentine, additional, Hatimi, Lahcène, additional, Buhot, Benjamin, additional, Velarde, Mathias, additional, Durieux, Anne Cécile, additional, and Freyssenet, Damien, additional
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- 2024
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3. Sarcopenia and serum biomarkers of oxidative stress after a 6-month physical activity intervention in women with metastatic breast cancer: results from the ABLE feasibility trial
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Delrieu, Lidia, Martin, Agnès, Touillaud, Marina, Pérol, Olivia, Morelle, Magali, Febvey-Combes, Olivia, Freyssenet, Damien, Friedenreich, Christine, Dufresne, Armelle, Bachelot, Thomas, Heudel, Pierre-Etienne, Trédan, Olivier, Crochet, Hugo, Bouhamama, Amine, Pilleul, Frank, Pialoux, Vincent, and Fervers, Béatrice
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- 2021
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4. Design and methods of a national, multicenter, randomized and controlled trial to assess the efficacy of a physical activity program to improve health-related quality of life and reduce fatigue in women with metastatic breast cancer: ABLE02 trial
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Delrieu, Lidia, Anota, Amélie, Trédan, Olivier, Freyssenet, Damien, Maire, Aurélia, Canada, Brice, Fournier, Baptiste, Febvey-Combes, Olivia, Pilleul, Frank, Bouhamama, Amine, Caux, Christophe, Joly, Florence, Fervers, Béatrice, Pialoux, Vincent, Pérol, David, and Pérol, Olivia
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- 2020
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5. Data from Myostatin Gene Inactivation Prevents Skeletal Muscle Wasting in Cancer
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Gallot, Yann S., primary, Durieux, Anne-Cécile, primary, Castells, Josiane, primary, Desgeorges, Marine M., primary, Vernus, Barbara, primary, Plantureux, Léa, primary, Rémond, Didier, primary, Jahnke, Vanessa E., primary, Lefai, Etienne, primary, Dardevet, Dominique, primary, Nemoz, Georges, primary, Schaeffer, Laurent, primary, Bonnieu, Anne, primary, and Freyssenet, Damien G., primary
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- 2023
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6. Supplementary Materials and Methods from Myostatin Gene Inactivation Prevents Skeletal Muscle Wasting in Cancer
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Gallot, Yann S., primary, Durieux, Anne-Cécile, primary, Castells, Josiane, primary, Desgeorges, Marine M., primary, Vernus, Barbara, primary, Plantureux, Léa, primary, Rémond, Didier, primary, Jahnke, Vanessa E., primary, Lefai, Etienne, primary, Dardevet, Dominique, primary, Nemoz, Georges, primary, Schaeffer, Laurent, primary, Bonnieu, Anne, primary, and Freyssenet, Damien G., primary
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- 2023
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7. Supplementary Figure S4 from Myostatin Gene Inactivation Prevents Skeletal Muscle Wasting in Cancer
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Gallot, Yann S., primary, Durieux, Anne-Cécile, primary, Castells, Josiane, primary, Desgeorges, Marine M., primary, Vernus, Barbara, primary, Plantureux, Léa, primary, Rémond, Didier, primary, Jahnke, Vanessa E., primary, Lefai, Etienne, primary, Dardevet, Dominique, primary, Nemoz, Georges, primary, Schaeffer, Laurent, primary, Bonnieu, Anne, primary, and Freyssenet, Damien G., primary
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- 2023
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8. Supplementary Figure Legend from Myostatin Gene Inactivation Prevents Skeletal Muscle Wasting in Cancer
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Gallot, Yann S., primary, Durieux, Anne-Cécile, primary, Castells, Josiane, primary, Desgeorges, Marine M., primary, Vernus, Barbara, primary, Plantureux, Léa, primary, Rémond, Didier, primary, Jahnke, Vanessa E., primary, Lefai, Etienne, primary, Dardevet, Dominique, primary, Nemoz, Georges, primary, Schaeffer, Laurent, primary, Bonnieu, Anne, primary, and Freyssenet, Damien G., primary
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- 2023
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9. Supplementary Table S1 from Myostatin Gene Inactivation Prevents Skeletal Muscle Wasting in Cancer
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Gallot, Yann S., primary, Durieux, Anne-Cécile, primary, Castells, Josiane, primary, Desgeorges, Marine M., primary, Vernus, Barbara, primary, Plantureux, Léa, primary, Rémond, Didier, primary, Jahnke, Vanessa E., primary, Lefai, Etienne, primary, Dardevet, Dominique, primary, Nemoz, Georges, primary, Schaeffer, Laurent, primary, Bonnieu, Anne, primary, and Freyssenet, Damien G., primary
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- 2023
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10. Molecular mechanisms of cancer cachexia‐related loss of skeletal muscle mass: data analysis from preclinical and clinical studies
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Martin, Agnès, primary, Gallot, Yann S., additional, and Freyssenet, Damien, additional
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- 2023
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11. Glucocorticoid-dependent REDD1 expression reduces muscle metabolism to enable adaptation under energetic stress
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Britto, Florian A., Cortade, Fabienne, Belloum, Yassine, Blaquière, Marine, Gallot, Yann S., Docquier, Aurélie, Pagano, Allan F., Jublanc, Elodie, Bendridi, Nadia, Koechlin-Ramonatxo, Christelle, Chabi, Béatrice, Francaux, Marc, Casas, François, Freyssenet, Damien, Rieusset, Jennifer, Giorgetti-Peraldi, Sophie, Carnac, Gilles, Ollendorff, Vincent, and Favier, François B.
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- 2018
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12. Activity energy expenditure is a major determinant of dietary fat oxidation and trafficking, but the deleterious effect of detraining is more marked than the beneficial effect of training at current recommendations
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Bergouignan, Audrey, Momken, Iman, Lefai, Etienne, Antoun, Edwina, Schoeller, Dale A, Platat, Carine, Chery, Isabelle, Zahariev, Alexandre, Vidal, Hubert, Gabert, Laure, Normand, Sylvie, Freyssenet, Damien, Laville, Martine, Simon, Chantal, and Blanc, Stephane
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- 2013
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13. Hypothalamic–pituitary–adrenal axis activation and glucocorticoid‐responsive gene expression in skeletal muscle and liver of Apc mice
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Martin, Agnès, primary, Castells, Josiane, additional, Allibert, Valentine, additional, Emerit, Andréa, additional, Zolotoff, Cindy, additional, Cardot‐Ruffino, Victoire, additional, Gallot, Yann S., additional, Vernus, Barbara, additional, Chauvet, Véronique, additional, Bartholin, Laurent, additional, Schaeffer, Laurent, additional, Durieux, Anne‐Cécile, additional, Hourdé, Christophe, additional, Favier, François B., additional, Mazelin, Laetitia, additional, and Freyssenet, Damien, additional
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- 2022
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14. Does high mitochondrial efficiency carry an oxidative cost? The case of the African pygmy mouse (Mus mattheyi)
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Boël, Mélanie, primary, Veyrunes, Frédéric, additional, Durieux, Anne-Cécile, additional, Freyssenet, Damien, additional, Voituron, Yann, additional, and Roussel, Damien, additional
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- 2022
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15. Early Deconditioning of Human Skeletal Muscles and the Effects of a Thigh Cuff Countermeasure
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Fovet, Théo, primary, Guilhot, Corentin, additional, Stevens, Laurence, additional, Montel, Valérie, additional, Delobel, Pierre, additional, Roumanille, Rémi, additional, Semporé, Michel-Yves, additional, Freyssenet, Damien, additional, Py, Guillaume, additional, Brioche, Thomas, additional, and Chopard, Angèle, additional
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- 2021
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16. Inactivation of myostatin: a potential therapeutic tool against autosomal dominant centronuclear myopathy: YPO.043
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Arnould, David, Freyssenet, Damien, and Durieux, Anne-Cécile
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- 2016
17. Molecular Mechanisms of Skeletal Muscle Atrophy in a Mouse Model of Cerebral Ischemia
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Desgeorges, Marine Maud, Devillard, Xavier, Toutain, Jérome, Divoux, Didier, Castells, Josiane, Bernaudin, Myriam, Touzani, Omar, and Freyssenet, Damien Gilles
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- 2015
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18. Activité physique et maladies chroniques : quels effets et dans quel cadre ?
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Carré, François, primary, Grémy, Isabelle, additional, Duclos, Martine, additional, Moro, Cédric, additional, Freyssenet, Damien, additional, Boiché, Julie, additional, Vuillemin, Anne, additional, Perrier, Clément, additional, Perrin, Claire, additional, Cha, Sophie, additional, and Lucia, Valérie, additional
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- 2021
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19. Downregulation of Akt/mammalian target of rapamycin pathway in skeletal muscle is associated with increased REDD1 expression in response to chronic hypoxia
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Favier, Francois B., Costes, Frederic, Defour, Aurelia, Bonnefoy, Regis, Lefai, Etienne, Bauge, Stephane, Peinnequin, Andre, Benoit, Henri, and Freyssenet, Damien
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Lung diseases, Obstructive -- Research ,Lung diseases, Obstructive -- Genetic aspects ,Gene expression -- Research ,Muscles -- Physiological aspects ,Muscles -- Genetic aspects ,Muscles -- Research ,Ubiquitin-proteasome system -- Physiological aspects ,Ubiquitin-proteasome system -- Genetic aspects ,Ubiquitin-proteasome system -- Research ,Biological sciences - Abstract
Although it is well established that chronic hypoxia leads to an inexorable loss of skeletal muscle mass in healthy subjects, the underlying molecular mechanisms involved in this process are currently unknown. Skeletal muscle atrophy is also an important systemic consequence of chronic obstructive pulmonary disease (COPD), but the role of hypoxemia in this regulation is still debated. Our general aim was to determine the molecular mechanisms involved in the regulation of skeletal muscle mass after exposure to chronic hypoxia and to test the biological relevance of our findings into the clinical context of COPD. Expression of positive and negative regulators of skeletal muscle mass were explored 1) in the soleus muscle of rats exposed to severe hypoxia (6,300 m) for 3 wk and 2) in vastus lateralis muscle of nonhypoxemic and hypoxemic COPD patients. In rodents, we observed a marked inhibition of the mammalian target of rapamycin (mTOR) pathway together with a strong increase in regulated in development and DNA damage response 1 (REDD1) expression and in its association with 14-3-3, a mechanism known to downregulate the mTOR pathway. Importantly, REDD1 overexpression in vivo was sufficient to cause skeletal muscle fiber atrophy in normoxia. Finally, the comparative analysis of skeletal muscle in hypoxemic vs. nonhypoxemic COPD patients confirms that hypoxia causes an inhibition of the mTOR signaling pathway. We thus identify REDD1 as a negative regulator of skeletal muscle mass during chronic hypoxia. Translation of this fundamental knowledge into the clinical investigation of COPD shows the interest to develop therapeutic strategies aimed at inhibiting REDD1. 14-3-3; proteasome; muscle atrophy; AMPK doi: 10.1152/ajpregu.00550.2009.
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- 2010
20. Mechano-transduction to muscle protein synthesis is modulated by FAK
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Klossner, Stephan, Durieux, Anne-Cecile, Freyssenet, Damien, and Flueck, Martin
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- 2009
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21. Muscle inactivation of mTOR causes metabolic and dystrophin defects leading to severe myopathy
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Risson, Valerie, Mazelin, Laetitia, Roceri, Mila, Sanchez, Herve, Moncollin, Vincent, Corneloup, Claudine, Richard-Bulteau, Helene, Vignaud, Alban, Baas, Dominique, Defour, Aurelia, Freyssenet, Damien, Tanti, Jean-Francois, Le-Marchand-Brustel, Yannick, Ferrier, Bernard, Conjard-Duplany, Agnes, Romanino, Klaas, Bauche, Stephanie, Hantai, Daniel, Mueller, Matthias, Kozma, Sara C., Thomas, George, Ruegg, Markus A., Ferry, Arnaud, Pende, Mario, Bigard, Xavier, Koulmann, Nathalie, Schaeffer, Laurent, and Gangloff, Yann-Gael
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Glucose metabolism -- Physiological aspects ,Utrophin -- Physiological aspects ,Dextrose -- Physiological aspects ,Glucose -- Physiological aspects ,Glycogen -- Physiological aspects ,Dystrophin -- Physiological aspects ,Biological sciences - Abstract
Mammalian target of rapamycin (mTOR) is a key regulator of cell growth that associates with raptor and rictor to form the mTOR complex 1 (mTORC1) and mTORC2, respectively. Raptor is required for oxidative muscle integrity, whereas rictor is dispensable. In this study, we show that muscle-specific inactivation of mTOR leads to severe myopathy, resulting in premature death, mTOR-deficient muscles display metabolic changes similar to those observed in muscles lacking raptor, including impaired oxidative metabolism, altered mitochondrial regulation, and glycogen accumulation associated with protein kinase B/Akt hyperactivation. In addition, mTOR-deficient muscles exhibit increased basal glucose uptake, whereas whole body glucose homeostasis is essentially maintained. Importantly, loss of mTOR exacerbates the myopathic features in both slow oxidative and fast glycolytic muscles. Moreover, mTOR but not raptor and rictor deficiency leads to reduced muscle dystrophin content. We provide evidence that mTOR controls dystrophin transcription in a cell-autonomous, rapamycin-resistant, and kinase-independent manner. Collectively, our results demonstrate that mTOR acts mainly via mTORC1, whereas regulation of dystrophin is raptor and rictor independent. /doi/ 10.1083/jcb.200903131
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- 2009
22. Control of mitochondrial biogenesis, ROS level, and cytosolic [Ca.sup.2+] concentration during the cell cycle and the onset of differentiation in L6E9 myoblasts
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Jahnke, Vanessa E., Sabido, Odile, and Freyssenet, Damien
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Mitochondria -- Physiological aspects ,Mitochondria -- Research ,Muscle cells -- Physiological aspects ,Muscle cells -- Research ,Gene expression -- Research ,Biological sciences - Abstract
Mitochondria can sense signals linked to changes in energy demand to affect nuclear gene expression. This retrograde signaling pathway is presumed to be involved in the regulation of myoblast proliferation and differentiation. We have investigated the regulation of mitochondrial biogenesis and production of putative retrograde signaling agents [hydrogen peroxide ([H.sub.2][O.sub.2]) and [Ca.sup.2+]] during the cell cycle and the onset of differentiation in L6E9 muscle cells. The biosynthesis of cardiolipin and mitochondrial proteins was mainly achieved in S phase, whereas the expression of mitochondrial biogenesis factors [peroxisome proliferator-activated receptor (PPAR)-[alpha], PPAR-[delta], and neuronal nitric oxide synthase 1] was regularly increased from [G.sub.1] to [G.sub.2]M phase. In agreement with the increase in mitochondrial membrane potential, mitochondria in S and [G.sub.2]M phases have a significantly higher [H.sub.2][O.sub.2] level when compared with [G.sub.1] phase. By contrast, the onset of differentiation was characterized by a marked reduction in mitochondrial protein expression and mitochondrial [H.sub.2][O.sub.2] level. The capacity of mitochondria to release [Ca.sup.2+] in response to a metabolic challenge was significantly decreased at the onset of differentiation. Finally, an increase in calmodulin expression in S and [G.sub.2]M phases and a transitory increase in phosphorylated nuclear factor of activated T cells (NFAT) c3 in S phase was observed. NFATc3 phosphorylation was markedly decreased at the onset of differentiation. Our data point to functional links between the control of mitochondrial biogenesis and the regulation of the level of retrograde signaling agents during the cell cycle and the onset of differentiation in L6E9 muscle cells. mitochondria; myogenesis; reactive oxygen species; skeletal muscle
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- 2009
23. Cellular and molecular events controlling skeletal muscle mass in response to altered use
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Favier, François B., Benoit, Henri, and Freyssenet, Damien
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- 2008
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24. Phenotypic features of cancer cachexia‐related loss of skeletal muscle mass and function: lessons from human and animal studies
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Martin, Agnès, primary and Freyssenet, Damien, additional
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- 2021
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25. Calcineurin A and CaMKIV transactivate PGC-1α promoter, but differentially regulate cytochrome c promoter in rat skeletal muscle
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Guerfali, Ibtissem, Manissolle, Chloé, Durieux, Anne-Cécile, Bonnefoy, Régis, Bartegi, Aghleb, and Freyssenet, Damien
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- 2007
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26. Calcium-regulated changes in mitochondrial phenotype in skeletal muscle cells
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Freyssenet, Damien, Irrcher, Isabella, Connor, Michael K., Di Carlo, Martino, and Hood, David A.
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Oxidoreductases -- Research ,Biological sciences - Abstract
Cytochrome c expression and mitochondrial biogenesis can be invoked by elevated intracellular [Ca.sup.2+] in muscle cells. To characterize the potential role of [Ca.sup.2+] as a messenger involved in mitochondrial biogenesis in muscle, we determined the effects of the [Ca.sup.2+] ionophore A-23187 on the expression of nuclear- and mitochondrially encoded genes. Treatment of myotubes with 1 [micro]M A-23187 for 48-96 h increased nuclear-encoded [beta]-subunit [F.sub.1]ATPase and malate dehydrogenase (MDH) mRNA levels by 50-100% (P < 0.05) but decreased mRNA levels of glutamate dehydrogenase (GDH) by 19% (P < 0.05). mRNA levels of the cytochrome c oxidase (COX) nuclear-encoded subunits IV, Vb, and VIc were unchanged, whereas the mitochondrially encoded subunits COX II and COX III were decreased by 30 and 70%, respectively (P < 0.05). This was paralleled by a 20% decrease (P < 0.05) in COX activity. These data suggest that cytoplasmic [Ca.sup.2+] differentially regulates the mRNA level of nuclear and mitochondrial genes. The decline in COX II and III mRNA may be mediated by Tfam, because A-23187 modestly reduced Tfam levels by 48 h. A-23187 induced time-dependent increases in Egr-1 mRNA, along with the activation of ERK1/2 and AMP-activated protein kinase. MEK inhibition with PD-98059 attenuated the increase in Egr-1 mRNA. A-23187 also increased Egr-1, serum response factor, and Sp1 protein expression, transcription factors implicated in mitochondrial biogenesis. Egr-1 overexpression increased nuclear-encoded cytochrome c transcriptional activation by 1.5-fold (P < 0.05) and reduced GDH mRNA by 37% (P < 0.05) but had no effect on MDH or [beta]-subunit [F.sub.1]ATPase mRNA. These results indicate that changes in intracellular [Ca.sup.2+] can modify mitochondrial phenotype, in part via the involvement of Egr-1. mitochondrial biogenesis; malate dehydrogenase; cytochrome c oxidase mitochondrial transcription factor-A; early growth response gene-1; glutamate dehydrogenase
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- 2004
27. Myogenic and nonmyogenic cells differentially express proteinases, Hsc/Hsp70, and BAG-1 during skeletal muscle regeneration
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Duguez, Stephanie, Le Bihan, Marie-Catherine, Gouttefangeas, Dominique, Feasson, Leonard, and Freyssenet, Damien
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Muscles -- Research ,Biological sciences - Abstract
Skeletal muscle has a remarkable capacity to regenerate after injury. To determine whether changes in the expression of proteinases, 73-kDa constitutive heat shock cognate protein (Hsc70) and stress-inducible 72-kDa heat shock protein (Hsp70) (Hsc/Hsp70), and Bcl-2-associated gene product-1 (BAG-1) contribute to the remodeling response of muscle tissue, tibialis anterior muscles of male Spragne-Dawley rats were injected with 0.75% bupivacaine and removed at 3, 5, 7, 10, 14, 21, or 35 days postinjection (n = 5-7/group). The immunohistochemical analysis of desmin, [alpha]-actin, and developmental/neonatal myosin heavy chain expressions indicated the presence of myoblasts (days 3-7), inflammatory cells (days 3-7), degenerating myofibers (days 3-7), regenerating myofibers (days 5-10), and growing mature myofibers (days 10-21) in regenerating muscles. Our biochemical analysis documented profound adaptations in proteolytic metabolism characterized by significant increases in the enzyme activities of matrix metalloproteinases 2 and 9 and plasminogen activators (days 3-14), calpains 1 and 2 (days 3-7), cathepsins B and L (days 3-10), and proteasome (days 3-14). Proteasome activity was strongly correlated with proliferating cell nuclear antigen protein level, suggesting that proteasome played a key role in myoblast proliferation. The expression pattern of BAG-1, a regulatory cofactor of Hsc/Hsp70 at the interface between protein folding and proteasomal proteolysis, did not corroborate the changes in proteasome enzyme activity, suggesting that BAG-1 may promote other functions, such as the folding capacity of Hsc/Hsp70. Altogether, the diversity of functions attributed to proteinases in the present study was strongly supported by the relative changes in the proportion of myogenic and nonmyogenic cells over the time course of regeneration. heat shock cognate protein 70; heat shock protein 70; Bcl-2-associated gene product-1; chaperone; immunohistochemistry; matrix metalloproteinases; myogenesis; proliferating cell nuclear antigen
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- 2003
28. Mitochondrial biogenesis during skeletal muscle regeneration
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Duguez, Stephanie, Feasson, Leonard, Denis, Christian, and Freyssenet, Damien
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Physiology -- Research ,Myogenesis -- Research ,Mitochondria -- Physiological aspects ,Striated muscle -- Physiological aspects ,Rats -- Physiological aspects ,Cell differentiation -- Physiological aspects ,Peroxisomes -- Physiological aspects ,Genetic transcription -- Research ,Biological sciences - Abstract
Myogenesis requires energy production for the execution of a number of regulatory and biosynthesis events. We hypothesized that mitochondrial biogenesis would be stimulated during skeletal muscle regeneration. Tibialis anterior muscles of male Sprague-Dawley rats were injected with 0.75% bupivacaine and removed at 3, 5, 7, 10, 14, 21, or 35 days after injection (n = 5-7/group). Two main periods emerged from the histochemical analyses of muscle sections and the expression of proliferating cell nuclear antigen, desmin, and creatine phosphokinase: 1) activation/proliferation of satellite cells (days 3-14) and 2) differentiation into muscle fibers (days 5-35). The onset of muscle differentiation was accompanied by a marked stimulation of mitochondrial biogenesis, as indicated by a nearly fivefold increase in citrate synthase activity and state 3 rate of respiration between days 5 and 10. Peroxisome proliferator-activated receptor-[gamma] coactivator-1 (PGC-1) mRNA level and mitochondrial transcription factor A (mtTFA) protein level peaked on day 10 concurrently with the state 3 rate of respiration. Therefore, transcriptional activation by PGC-1 and mtTFA may be one of the mechanisms regulating mitochondrial biogenesis in regenerating skeletal muscle. Taken together, our results suggest that mitochondrial biogenesis may be an important regulatory event during muscle regeneration. mitochondrial respiration; muscle precursor cells; myogenesis; peroxisome proliferator-activated receptor-[gamma] coactivator-1; mitochondrial transcription factor A
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- 2002
29. A Centronuclear Myopathy – Dynamin 2 Mutation Impairs Autophagy in Mice
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Durieux, Anne-Cécile, Vassilopoulos, Stéphane, Lainé, Jeanne, Fraysse, Bodvaël, Briñas, Laura, Prudhon, Bernard, Castells, Josiane, Freyssenet, Damien, Bonne, Gisèle, Guicheney, Pascale, and Bitoun, Marc
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- 2012
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30. L’activité physique adaptée comme stratégie de prévention et de traitement des maladies chroniques : les cas du diabète de type II et de la dépression
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Boiche, Julie, primary, Carré, François, additional, Fervers, Béatrice, additional, Freyssenet, Damien, additional, Gremy, Isabelle, additional, Guiraud, Thibaut, additional, Moro, Cédric, additional, Nguyen, Christelle, additional, Poiraudeau, Serge, additional, Ninot, Grégory, additional, Perrin, Claire, additional, Varray, Alain, additional, Vinet, Agnès, additional, and Walther, Guillaume, additional
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- 2020
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31. Cytochrome c transcriptional activation and mRNA stability during contractile activity in skeletal muscle
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Freyssenet, Damien, Connor, Michael K., Takahashi, Mark, and Hood, David A.
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Cytochrome c -- Genetic aspects ,Messenger RNA -- Research ,Genetic transcription -- Research ,Muscles -- Genetic aspects ,Biological sciences - Abstract
Unilateral chronic stimulation has been done on the rat tibialis anterior (TA) to study the transcriptional activation and mRNA stability of cytochrome c. The stimulation had a duration of 3 hours for 1, 2, 3, 4, 5 and 7 days at 10 Hz. Direct plasmid DNA injection into the TA with a chloramphenicol acetyltransferase reporter gene linked to 326 bp of the cytochrome c promoter was used in assessing transcriptional activation. Results indicate that cytochrome c mRNA increased by 1.3 to 1.7-fold above control between 1 and 7 days. The mRNA stability was higher in stimulated TA than in control between 2 and 4 days.
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- 1999
32. Focal adhesion kinase is a load-dependent governor of the slow contractile and oxidative muscle phenotype
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Durieux, Anne-Cécile, DʼAntona, Giuseppe, Desplanches, Dominique, Freyssenet, Damien, Klossner, Stephan, Bottinelli, Roberto, and Flück, Martin
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- 2009
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33. Down-Regulation of Akt/Mammalian Target of Rapamycin Signaling Pathway in Response to Myostatin Overexpression in Skeletal Muscle
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Amirouche, Adel, Durieux, Anne-Cécile, Banzet, Sébastien, Koulmann, Nathalie, Bonnefoy, Régis, Mouret, Catherine, Bigard, Xavier, Peinnequin, André, and Freyssenet, Damien
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- 2009
34. Ectopic Expression of Myostatin Induces Atrophy of Adult Skeletal Muscle by Decreasing Muscle Gene Expression
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Durieux, Anne-Cécile, Amirouche, Adel, Banzet, Sébastien, Koulmann, Nathalie, Bonnefoy, Régis, Pasdeloup, Marielle, Mouret, Catherine, Bigard, Xavier, Peinnequin, André, and Freyssenet, Damien
- Published
- 2007
35. Contractile activity-induced adaptations in the mitochondrial protein import system
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Takahashi, Mark, Chesley, Alan, Freyssenet, Damien, and Hood, David A.
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Contractility (Biology) -- Research ,Mitochondrial DNA -- Research ,Biological sciences - Abstract
Research was conducted to examine the contractile activity-induced adaptations in the protein import system during mitochondrial biogenesis. The skeletal muscle was chosen for the experimental model which has shown itself to be effective in eliciting mitochondrial biogenesis. Evidence shows that chronic contractile activity modifies the extra- and intramitochondrial environments in a manner that hastens precursor protein import into the matrix of the organelle.
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- 1998
36. Mitochondrial-dependent regulation of myoblast proliferation
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Duguez, Stéphanie, Sabido, Odile, and Freyssenet, Damien
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- 2004
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37. Mitotic activity of rat muscle satellite cells in response to serum stimulation: relation with cellular metabolism
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Barani, Aude E, Sabido, Odile, and Freyssenet, Damien
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- 2003
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38. Zidovudine (AZT) induced alterations in mitochondrial biogenesis in rat striated muscles
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Freyssenet, Damien, DiCarlo, Martino, Escobar, Patricia, Grey, Janice, Schneider, Jeremy, and Hood, David A
- Published
- 1999
39. Additional file 1: of Glucocorticoid-dependent REDD1 expression reduces muscle metabolism to enable adaptation under energetic stress
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Britto, Florian, Cortade, Fabienne, Belloum, Yassine, Blaquière, Marine, Gallot, Yann, Docquier, Aurélie, Pagano, Allan, Jublanc, Elodie, Bendridi, Nadia, Koechlin-Ramonatxo, Christelle, Chabi, Béatrice, Francaux, Marc, Casas, François, Freyssenet, Damien, Rieusset, Jennifer, Giorgetti-Peraldi, Sophie, Carnac, Gilles, Ollendorff, Vincent, and Favier, François
- Abstract
Table S1. Classical markers of hypoxia exposure. Table S2. List of antibodies. Table S3. Primers used for real-time qPCR. (DOCX 17 kb)
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- 2018
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40. Additional file 2: of Glucocorticoid-dependent REDD1 expression reduces muscle metabolism to enable adaptation under energetic stress
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Britto, Florian, Cortade, Fabienne, Belloum, Yassine, Blaquière, Marine, Gallot, Yann, Docquier, Aurélie, Pagano, Allan, Jublanc, Elodie, Bendridi, Nadia, Koechlin-Ramonatxo, Christelle, Chabi, Béatrice, Francaux, Marc, Casas, François, Freyssenet, Damien, Rieusset, Jennifer, Giorgetti-Peraldi, Sophie, Carnac, Gilles, Ollendorff, Vincent, and Favier, François
- Abstract
Figure S1. Same as Fig. 1 with all raw data. Figure S2. Atrophying program in REDD1 KO muscles after hypoxia exposure. Figure S3. REDD1 deletion did not disrupt redox status of skeletal muscle in normoxic or hypoxic mice. Figure S4. REDD1 KO mice display an attenuated decrease in Akt/mTOR phosphorylation under energetic stress. Figure S5. REDD1 localizes in crude mitochondria after running exercise. Figure S6. REDD1 deletion does not alter the respiration capacity of isolated mitochondria. Figure S7. REDD1 overexpression does not alter citrate synthase protein expression. Figure S8. PRAS40 and mTOR localize in the crude mitochondrial fraction from skeletal muscle. Figure S9. Protein synthesis under energetic stress in human myoblasts depleted for REDD1. Figure S10. mTOR and HKII activity correlates with basal O2 consumption of myoblasts. Figure S11. Increase in mitophagy markers following intense running exercise in REDD1 KO mice. (PPTX 11020 kb)
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- 2018
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41. Glucocorticoid-dependent REDD1 expression reduces muscle metabolism to enable adaptation under energetic stress
- Author
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Britto, Florian, Cortade, Fabienne, Belloum, Yassine, Blaquière, Marine, Gallot, Yann S., Docquier, Aurélie, Pagano, Allan, Jublanc, Elodie, Bendridi, Nadia, Ramonatxo, Christelle, Chabi, Beatrice, Francaux , Marc, Casas, Francois, Freyssenet, Damien, Rieusset, Jennifer, Giorgetti-Peraldi, Sophie, Carnac, Gilles, Ollendorff, Vincent, and Favier, François
- Subjects
skeletal muscle ,metabolism ,hypoxia ,fasting ,exercise ,mitochondria ,mams ,energy expenditure ,mtor ,Médecine humaine et pathologie ,Human health and pathology - Abstract
Background: Skeletal muscle atrophy is a common feature of numerous chronic pathologies and is correlated with patient mortality. The REDD1 protein is currently recognized as a negative regulator of muscle mass through inhibition of the Akt/mTORC1 signaling pathway. REDD1 expression is notably induced following glucocorticoid secretion, which is a component of energy stress responses. Results: Unexpectedly, we show here that REDD1 instead limits muscle loss during energetic stresses such as hypoxia and fasting by reducing glycogen depletion and AMPK activation. Indeed, we demonstrate that REDD1 is required to decrease O2 and ATP consumption in skeletal muscle via reduction of the extent of mitochondrial-associated endoplasmic reticulum membranes (MAMs), a central hub connecting energy production by mitochondria and anabolic processes. In fact, REDD1 inhibits ATP-demanding processes such as glycogen storage and protein synthesis through disruption of the Akt/Hexokinase II and PRAS40/mTORC1 signaling pathways in MAMs. Our results uncover a new REDD1-dependent mechanism coupling mitochondrial respiration and anabolic processes during hypoxia, fasting, and exercise. Conclusions: Therefore, REDD1 is a crucial negative regulator of energy expenditure that is necessary for muscle adaptation during energetic stresses. This present study could shed new light on the role of REDD1 in several pathologies associated with energetic metabolism alteration, such as cancer, diabetes, and Parkinson’s disease.
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- 2018
42. Glucocorticoid-dependent REDD1 expression reduces muscle metabolism to enable adaptation under energetic stress
- Author
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UCL - SSS/IONS/CEMO - Pôle Cellulaire et moléculaire, Britto, Florian, Cortade, Fabienne, Belloum, Yassine, Blaquière, Marine, Gallot, Yann S., Docquier, Aurélie, Pagano, Allan F., Jublanc, Elodie, Bendridi, Nadia, Koechlin-Ramonatxo, Christelle, Chabi, Béatrice, Francaux, Marc, Casas, François, Freyssenet, Damien, Rieusset, Jennifer, Giorgetti-Peraldi, Sophie, Carnac, Gilles, Ollendorff, Vincent, Favier, François B., UCL - SSS/IONS/CEMO - Pôle Cellulaire et moléculaire, Britto, Florian, Cortade, Fabienne, Belloum, Yassine, Blaquière, Marine, Gallot, Yann S., Docquier, Aurélie, Pagano, Allan F., Jublanc, Elodie, Bendridi, Nadia, Koechlin-Ramonatxo, Christelle, Chabi, Béatrice, Francaux, Marc, Casas, François, Freyssenet, Damien, Rieusset, Jennifer, Giorgetti-Peraldi, Sophie, Carnac, Gilles, Ollendorff, Vincent, and Favier, François B.
- Abstract
Background: Skeletal muscle atrophy is a common feature of numerous chronic pathologies and is correlated with patient mortality. The REDD1 protein is currently recognized as a negative regulator of muscle mass through inhibition of the Akt/mTORC1 signaling pathway. REDD1 expression is notably induced following glucocorticoid secretion, which is a component of energy stress responses. Results: Unexpectedly, we show here that REDD1 instead limits muscle loss during energetic stresses such as hypoxia and fasting by reducing glycogen depletion and AMPK activation. Indeed, we demonstrate that REDD1 is required to decrease O2 and ATP consumption in skeletal muscle via reduction of the extent of mitochondrialassociated endoplasmic reticulum membranes (MAMs), a central hub connecting energy production by mitochondria and anabolic processes. In fact, REDD1 inhibits ATP-demanding processes such as glycogen storage and protein synthesis through disruption of the Akt/Hexokinase II and PRAS40/mTORC1 signaling pathways in MAMs. Our results uncover a new REDD1-dependent mechanism coupling mitochondrial respiration and anabolic processes during hypoxia, fasting, and exercise. Conclusions: Therefore, REDD1 is a crucial negative regulator of energy expenditure that is necessary for muscle adaptation during energetic stresses. This present study could shed new light on the role of REDD1 in several pathologies associated with energetic metabolism alteration, such as cancer, diabetes, and Parkinson’s disease.
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- 2018
43. Mechano-transduction to muscle protein synthesis is modulated by FAK
- Author
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Klossner, Stephan, Durieux, Anne-Cecile, Freyssenet, Damien, Flueck, Martin, Klossner, Stephan, Durieux, Anne-Cecile, Freyssenet, Damien, and Flueck, Martin
- Abstract
We examined the involvement of focal adhesion kinase (FAK) in mechano-regulated signalling to protein synthesis by combining muscle-targeted transgenesis with a physiological model for un- and reloading of hindlimbs. Transfections of mouse tibialis anterior muscle with a FAK expression construct increased FAK protein 1.6-fold versus empty transfection in the contralateral leg and elevated FAK concentration at the sarcolemma. Altered activation status of phosphotransfer enzymes and downstream translation factors showed that FAK overexpression was functionally important. FAK auto-phosphorylation on Y397 was enhanced between 1 and 6h of reloading and preceded the activation of p70S6K after 24h of reloading. Akt and translation initiation factors 4E-BP1 and 2A, which reside up- or downstream of p70S6K, respectively, showed no FAK-modulated regulation. The findings identify FAK as an upstream element of the mechano-sensory pathway of p70S6K activation whose Akt-independent regulation intervenes in control of muscle mass by mechanical stimuli in humans
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- 2018
44. REDD1 Reduces Muscle Metabolism to Foster Adaptation under Fasting
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FAVIER, Francois, primary, Britto, Florian, additional, Belloum, Yassine, additional, Gallot, Yann, additional, Cortade, Fabienne, additional, Chabi, Beatrice, additional, Freyssenet, Damien, additional, Carnac, Gilles, additional, Rieusset, Jennifer, additional, Giorgetti‐Peraldi, Sophie, additional, and Ollendorff, Vincent, additional
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- 2018
- Full Text
- View/download PDF
45. Pharmacological inhibition of myostatin improves skeletal muscle mass and function in a mouse model of stroke
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Desgeorges, Marine Maud, primary, Devillard, Xavier, additional, Toutain, Jérome, additional, Castells, Josiane, additional, Divoux, Didier, additional, Arnould, David Frédéric, additional, Haqq, Christopher, additional, Bernaudin, Myriam, additional, Durieux, Anne-Cécile, additional, Touzani, Omar, additional, and Freyssenet, Damien Gilles, additional
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- 2017
- Full Text
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46. Regulation of Akt-mTOR, ubiquitin-proteasome and autophagy-lysosome pathways in locomotor and respiratory muscles during experimental sepsis in mice
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Morel, Jérome, primary, Palao, Jean-Charles, additional, Castells, Josiane, additional, Desgeorges, Marine, additional, Busso, Thierry, additional, Molliex, Serge, additional, Jahnke, Vanessa, additional, Del Carmine, Peggy, additional, Gondin, Julien, additional, Arnould, David, additional, Durieux, Anne Cécile, additional, and Freyssenet, Damien, additional
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- 2017
- Full Text
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47. Fibroblast growth factor 19 regulates skeletal muscle mass and ameliorates muscle wasting in mice
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Benoit, Bérengère, primary, Meugnier, Emmanuelle, additional, Castelli, Martina, additional, Chanon, Stéphanie, additional, Vieille-Marchiset, Aurélie, additional, Durand, Christine, additional, Bendridi, Nadia, additional, Pesenti, Sandra, additional, Monternier, Pierre-Axel, additional, Durieux, Anne-Cécile, additional, Freyssenet, Damien, additional, Rieusset, Jennifer, additional, Lefai, Etienne, additional, Vidal, Hubert, additional, and Ruzzin, Jérôme, additional
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- 2017
- Full Text
- View/download PDF
48. High intensity aerobic exercise training improves chronic intermittent hypoxia-induced insulin resistance without basal autophagy modulation
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Pauly, Marion, primary, Assense, Allan, additional, Rondon, Aurélie, additional, Thomas, Amandine, additional, Dubouchaud, Hervé, additional, Freyssenet, Damien, additional, Benoit, Henri, additional, Castells, Josiane, additional, and Flore, Patrice, additional
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- 2017
- Full Text
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49. Muscle-specific microRNA-206 targets multiple components in dystrophic skeletal muscle representing beneficial adaptations
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Amirouche, Adel, primary, Jahnke, Vanessa E., additional, Lunde, John A., additional, Koulmann, Nathalie, additional, Freyssenet, Damien G., additional, and Jasmin, Bernard J., additional
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- 2017
- Full Text
- View/download PDF
50. Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)
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Mark, Coppens, Isabelle, Corasaniti, Maria Tiziana, Corazzari, Marco, Corbalan, Ramon, Corcelle-Termeau, Elisabeth, Cordero, Mario D., Corral-Ramos, Cristina, Corti, Olga, Cossarizza, Andrea, Costelli, Paola, Costes, Safia, Coto-Montes, Ana, Cottet, Sandra, Couve, Eduardo, Covey, Lori R., Cowart, L. Ashley, Cox, Jeffery S., Coxon, Fraser P., Coyne, Carolyn B., Cragg, Mark S., Craven, Rolf J., Crepaldi, Tiziana, Crespo, Jose L., Criollo, Alfredo, Crippa, Valeria, Cruz, Maria Teresa, Cuervo, Ana Maria, Cuezva, Jose M., Cui, Taixing, Cutillas, Pedro R., Czaja, Mark J., Czyzyk-Krzeska, Maria F., Dagda, Ruben K., Dahmen, Uta, Dai, Chunsun, Dai, Wenjie, Dai, Yun, Dalby, Kevin N., Valle, Luisa Dalla, Dalmasso, Guillaume, D'Amelio, Marcello, Damme, Markus, Darfeuille-Michaud, Arlette, Dargemont, Catherine, Darley-Usmar, Victor M., Dasarathy, Srinivasan, Dasgupta, Biplab, Dash, Srikanta, Dass, Crispin R., Davey, Hazel Marie, Davids, Lester M., Davila, David, Davis, Roger J., Dawson, Ted M., Dawson, Valina L., Daza, Paula, de Belleroche, Jackie, de Figueiredo, Paul, Bressan Queiroz de Figueiredo, Regina Celia, de la Fuente, Jose, De Martino, Luisa, De Matteis, Antonella, De Meyer, Guido R. Y., De Milito, Angelo, De Santi, Mauro, de Souza, Wanderley, De Tata, Vincenzo, De Zio, Daniela, Debnath, Jayanta, Dechant, Reinhard, Decuypere, Jean-Paul, Deegan, Shane, Dehay, Benjamin, Del Bello, Barbara, Del Re, Dominic P., Delage-Mourroux, Regis, Delbridge, Lea M. D., Deldicque, Louise, Delorme-Axford, Elizabeth, Deng, Yizhen, Dengjel, Joern, Denizot, Melanie, Dent, Paul, Der, Channing J., Deretic, Vojo, Derrien, Benoit, Deutsch, Eric, Devarenne, Timothy P., Devenish, Rodney J., Di Bartolomeo, Sabrina, Di Daniele, Nicola, Di Domenico, Fabio, Di Nardo, Alessia, Di Paola, Simone, Di Pietro, Antonio, Di Renzo, Livia, DiAntonio, Aaron, Diaz-Araya, Guillermo, Diaz-Laviada, Ines, Diaz-Meco, Maria T., Diaz-Nido, Javier, Dickey, Chad A., Dickson, Robert C., Diederich, Marc, Digard, Paul, Dikic, Ivan, Dinesh-Kumar, Savithrama P., Ding, Chan, Ding, Wen-Xing, Ding, Zufeng, Dini, Luciana, Distler, Joerg H. W., Diwan, Abhinav, Djavaheri-Mergny, Mojgan, Dmytruk, Kostyantyn, Dobson, Renwick C. J., Doetsch, Volker, Dokladny, Karol, Dokudovskaya, Svetlana, Donadelli, Massimo, Dong, X. Charlie, Dong, Xiaonan, Dong, Zheng, Donohue, Terrence M., Jr., Doran, Kelly S., D'Orazi, Gabriella, Dorn, Gerald W., II, Dosenko, Victor, Dridi, Sami, Drucker, Liat, Du, Jie, Du, Li-Lin, Du, Lihuan, du Toit, Andre, Dua, Priyamvada, Duan, Lei, Duann, Pu, Dubey, Vikash Kumar, Duchen, Michael R., Duchosal, Michel A., Duez, Helene, Dugail, Isabelle, Dumit, Veronica I., Duncan, Mara C., Dunlop, Elaine A., Dunn, William A., Jr., Dupont, Nicolas, Dupuis, Luc, Duran, Raul V., Durcan, Thomas M., Duvezin-Caubet, Stephane, Duvvuri, Umamaheswar, Eapen, Vinay, Ebrahimi-Fakhari, Darius, Echard, Arnaud, Eckhart, Leopold, Edelstein, Charles L., Edinger, Aimee L., Eichinger, Ludwig, Eisenberg, Tobias, Eisenberg-Lerner, Avital, Eissa, N. Tony, El-Deiry, Wafik S., El-Khoury, Victoria, Elazar, Zvulun, Eldar-Finkelman, Hagit, Elliott, Chris J. H., Emanuele, Enzo, Emmenegger, Urban, Engedal, Nikolai, Engelbrecht, Anna-Mart, Engelender, Simone, Enserink, Jorrit M., Erdmann, Ralf, Erenpreisa, Jekaterina, Eri, Rajaraman, Eriksen, Jason L., Erman, Andreja, Escalante, Ricardo, Eskelinen, Eeva-Liisa, Espert, Lucile, Esteban-Martinez, Lorena, Evans, Thomas J., Fabri, Mario, Fabrias, Gemma, Fabrizi, Cinzia, Facchiano, Antonio, Faergeman, Nils J., Faggioni, Alberto, Fairlie, W. Douglas, Fan, Chunhai, Fan, Daping, Fan, Jie, Fang, Shengyun, Fanto, Manolis, Fanzani, Alessandro, Farkas, Thomas, Faure, Mathias, Favier, Francois B., Fearnhead, Howard, Federici, Massimo, Fei, Erkang, Felizardo, Tania C., Feng, Hua, Feng, Yibin, Feng, Yuchen, Ferguson, Thomas A., Fernandez, Alvaro F., Fernandez-Barrena, Maite G., Fernandez-Checa, Jose C., Fernandez-Lopez, Arsenio, Fernandez-Zapico, Martin E., Feron, Olivier, Ferraro, Elisabetta, Ferreira-Halder, Carmen Verissima, Fesus, Laszlo, Feuer, Ralph, Fiesel, Fabienne C., Filippi-Chiela, Eduardo C., Filomeni, Giuseppe, Fimia, Gian Maria, Fingert, John H., Finkbeiner, Steven, Finkel, Toren, Fiorito, Filomena, Fisher, Paul B., Flajolet, Marc, Flamigni, Flavio, Florey, Oliver, Florio, Salvatore, Floto, R. Andres, Folini, Marco, Follo, Carlo, Fon, Edward A., Fornai, Francesco, Fortunato, Franco, Fraldi, Alessandro, Franco, Rodrigo, Francois, Arnaud, Francois, Aurelie, Frankel, Lisa B., Fraser, Iain D. C., Frey, Norbert, Freyssenet, Damien G., Frezza, Christian, Friedman, Scott L., Frigo, Daniel E., Fu, Dongxu, Fuentes, Jose M., Fueyo, Juan, Fujitani, Yoshio, Fujiwara, Yuuki, Fujiya, Mikihiro, Fukuda, Mitsunori, Fulda, Simone, Fusco, Carmela, Gabryel, Bozena, Gaestel, Matthias, Gailly, Philippe, Gajewska, Malgorzata, Galadari, Sehamuddin, Galili, Gad, Galindo, Inmaculada, Galindo, Maria F., Galliciotti, Giovanna, Galluzzi, Lorenzo, Galluzzi, Luca, Galy, Vincent, Gammoh, Noor, Gandy, Sam, Ganesan, Anand K., Ganesan, Swamynathan, Ganley, Ian G., Gannage, Monique, Gao, Fen-Biao, Gao, Feng, Gao, Jian-Xin, Garcia Nannig, Lorena, Vescovi, Eleonora Garcia, Garcia-Macia, Marina, Garcia-Ruiz, Carmen, Garg, Abhishek D., Garg, Pramod Kumar, Gargini, Ricardo, Gassen, Nils Christian, Gatica, Damian, Gatti, Evelina, Gavard, Julie, Gavathiotis, Evripidis, Ge, Liang, Ge, Pengfei, Ge, Shengfang, Gean, Po-Wu, Gelmetti, Vania, Genazzani, Armando A., Geng, Jiefei, Genschik, Pascal, Gerner, Lisa, Gestwicki, Jason E., Gewirtz, David A., Ghavami, Saeid, Ghigo, Eric, Ghosh, Debabrata, Giammarioli, Anna Maria, Giampieri, Francesca, Giampietri, Claudia, Giatromanolaki, Alexandra, Gibbings, Derrick J., Gibellini, Lara, Gibson, Spencer B., Ginet, Vanessa, Giordano, Antonio, Giorgini, Flaviano, Giovannetti, Elisa, Girardin, Stephen E., Gispert, Suzana, Giuliano, Sandy, Gladson, Candece L., Glavic, Alvaro, Gleave, Martin, Godefroy, Nelly, Gogal, Robert M., Jr., Gokulan, Kuppan, Goldman, Gustavo H., Goletti, Delia, Goligorsky, Michael S., Gomes, Aldrin V., Gomes, Ligia C., Gomez, Hernando, Gomez-Manzano, Candelaria, Gomez-Sanchez, Ruben, Goncalves, Dawit A. P., Goncu, Ebru, Gong, Qingqiu, Gongora, Celine, Gonzalez, Carlos B., Gonzalez-Alegre, Pedro, Gonzalez-Cabo, Pilar, Ana Gonzalez-Polo, Rosa, Goping, Ing Swie, Gorbea, Carlos, Gorbunov, Nikolai V., Goring, Daphne R., Gorman, Adrienne M., Gorski, Sharon M., Goruppi, Sandro, Goto-Yamada, Shino, Gotor, Cecilia, Gottlieb, Roberta A., Gozes, Illana, Gozuacik, Devrim, Graba, Yacine, Graef, Martin, Granato, Giovanna E., Grant, Gary Dean, Grant, Steven, Gravina, Giovanni Luca, Green, Douglas R., Greenhough, Alexander, Greenwood, Michael T., Grimaldi, Benedetto, Gros, Frederic, Grose, Charles, Groulx, Jean-Francois, Gruber, Florian, Grumati, Paolo, Grune, Tilman, Guan, Jun-Lin, Guan, Kun-Liang, Guerra, Barbara, Guillen, Carlos, Gulshan, Kailash, Gunst, Jan, Guo, Chuanyong, Guo, Lei, Guo, Ming, Guo, Wenjie, Guo, Xu-Guang, Gust, Andrea A., Gustafsson, Asa B., Gutierrez, Elaine, Gutierrez, Maximiliano G., Gwak, Ho-Shin, Haas, Albert, Haber, James E., Hadano, Shinji, Hagedorn, Monica, Hahn, David R., Halayko, Andrew J., Hamacher-Brady, Anne, Hamada, Kozo, Hamai, Ahmed, Hamann, Andrea, Hamasaki, Maho, Hamer, Isabelle, Hamid, Qutayba, Hammond, Ester M., Han, Feng, Han, Weidong, Handa, James T., Hanover, John A., Hansen, Malene, Harada, Masaru, Harhaji-Trajkovic, Ljubica, Harper, J. Wade, Harrath, Abdel Halim, Harris, Adrian L., Harris, James, Hasler, Udo, Hasselblatt, Peter, Hasui, Kazuhisa, Hawley, Robert G., Hawley, Teresa S., He, Congcong, He, Cynthia Y., He, Fengtian, He, Gu, He, Rong-Rong, He, Xian-Hui, He, You-Wen, He, Yu-Ying, Heath, Joan K., Hebert, Marie-Josee, Heinzen, Robert A., Helgason, Gudmundur Vignir, Hensel, Michael, Henske, Elizabeth P., Her, Chengtao, Herman, Paul K., Hernandez, Agustin, Hernandez, Carlos, Hernandez-Tiedra, Sonia, Hetz, Claudio, Hiesinger, P. Robin, Higaki, Katsumi, Hilfiker, Sabine, Hill, Bradford G., Hill, Joseph A., Hill, William D., Hino, Keisuke, Hofius, Daniel, Hofman, Paul, Hoeglinger, Guenter U., Hoehfeld, Joerg, Holz, Marina K., Hong, Yonggeun, Hood, David A., Hoozemans, Jeroen J. M., Hoppe, Thorsten, Hsu, Chin, Hsu, Chin-Yuan, Hsu, Li-Chung, Hu, Dong, Hu, Guochang, Hu, Hong-Ming, Hu, Hongbo, Hu, Ming Chang, Hu, Yu-Chen, Hu, Zhuo-Wei, Hua, Fang, Hua, Ya, Huang, Canhua, Huang, Huey-Lan, Huang, Kuo-How, Huang, Kuo-Yang, Huang, Shile, Huang, Shiqian, Huang, Wei-Pang, Huang, Yi-Ran, Huang, Yong, Huang, Yunfei, Huber, Tobias B., Huebbe, Patricia, Huh, Won-Ki, Hulmi, Juha J., Hur, Gang Min, Hurley, James H., Husak, Zvenyslava, Hussain, Sabah N. A., Hussain, Salik, Hwang, Jung Jin, Hwang, Seungmin, Hwang, Thomas I. S., Ichihara, Atsuhiro, Imai, Yuzuru, Imbriano, Carol, Inomata, Megumi, Into, Takeshi, Iovane, Valentina, Iovanna, Juan L., Iozzo, Renato V., Ip, Nancy Y., Irazoqui, Javier E., Iribarren, Pablo, Isaka, Yoshitaka, Isakovic, Aleksandra J., Ischiropoulos, Harry, Isenberg, Jeffrey S., Ishaq, Mohammad, Ishida, Hiroyuki, Ishii, Isao, Ishmael, Jane E., Isidoro, Ciro, Isobe, Ken-ichi, Isono, Erika, Issazadeh-Navikas, Shohreh, Itahana, Koji, Itakura, Eisuke, Ivanov, Andrei I., Iyer, Anand Krishnan V., Izquierdo, Jose M., Izumi, Yotaro, Izzo, Valentina, Jaeaettelae, Marja, Jaber, Nadia, Jackson, Daniel John, Jackson, William T., Jacob, Tony George, Jacques, Thomas S., Jagannath, Chinnaswamy, Jain, Ashish, Jana, Nihar Ranjan, Jang, Byoung Kuk, Jani, Alkesh, Janji, Bassam, Jannig, Paulo Roberto, Jansson, Patric J., Jean, Steve, Jendrach, Marina, Jeon, Ju-Hong, Jessen, Niels, Jeung, Eui-Bae, Jia, Kailiang, Jia, Lijun, Jiang, Hong, Jiang, Hongchi, Jiang, Liwen, Jiang, Teng, Jiang, Xiaoyan, Jiang, Xuejun, Jiang, Ying, Jiang, Yongjun, Jimenez, Alberto, Jin, Cheng, Jin, Hongchuan, Jin, Lei, Jin, Meiyan, Jin, Shengkan, Jinwal, Umesh Kumar, Jo, Eun-Kyeong, Johansen, Terje, Johnson, Daniel E., Johnson, Gail V. W., Johnson, James D., Jonasch, Eric, Jones, Chris, Joosten, Leo A. B., Jordan, Joaquin, Joseph, Anna-Maria, Joseph, Bertrand, Joubert, Annie M., Ju, Dianwen, Ju, Jingfang, Juan, Hsueh-Fen, Juenemann, Katrin, Juhasz, Gabor, Jung, Hye Seung, Jung, Jae U., Jung, Yong-Keun, Jungbluth, Heinz, Justice, Matthew J., Jutten, Barry, Kaakoush, Nadeem O., Kaarniranta, Kai, Kaasik, Allen, Kabuta, Tomohiro, Kaeffer, Bertrand, Kagedal, Katarina, Kahana, Alon, Kajimura, Shingo, Kakhlon, Or, Kalia, Manjula, Kalvakolanu, Dhan V., Kamada, Yoshiaki, Kambas, Konstantinos, Kaminskyy, Vitaliy O., Kampinga, Harm H., Kandouz, Mustapha, Kang, Chanhee, Kang, Rui, Kang, Tae-Cheon, Kanki, Tomotake, Kanneganti, Thirumala-Devi, Kanno, Haruo, Kanthasamy, Anumantha G., Kantorow, Marc, Kaparakis-Liaskos, Maria, Kapuy, Orsolya, Karantza, Vassiliki, Karim, Md Razaul, Karmakar, Parimal, Kaser, Arthur, Kaushik, Susmita, Kawula, Thomas, Kaynar, A. Murat, Ke, Po-Yuan, Ke, Zun-Ji, Kehrl, John H., Keller, Kate E., Kemper, Jongsook Kim, Kenworthy, Anne K., Kepp, Oliver, Kern, Andreas, Kesari, Santosh, Kessel, David, Ketteler, Robin, Kettelhut, Isis do Carmo, Khambu, Bilon, Khan, Muzamil Majid, Khandelwal, Vinoth K. M., Khare, Sangeeta, Kiang, Juliann G., Kiger, Amy A., Kihara, Akio, Kim, Arianna L., Kim, Cheol Hyeon, Kim, Deok Ryong, Kim, Do-Hyung, Kim, Eung Kweon, Kim, Hye Young, Kim, Hyung-Ryong, Kim, Jae-Sung, Kim, Jeong Hun, Kim, Jin Cheon, Kim, Jin Hyoung, Kim, Kwang Woon, Kim, Michael D., Kim, Moon-Moo, Kim, Peter K., Kim, Seong Who, Kim, Soo-Youl, Kim, Yong-Sun, Kim, Yonghyun, Kimchi, Adi, Kimmelman, Alec C., Kimura, Tomonori, King, Jason S., Kirkegaard, Karla, Kirkin, Vladimir, Kirshenbaum, Lorrie A., Kishi, Shuji, Kitajima, Yasuo, Kitamoto, Katsuhiko, Kitaoka, Yasushi, Kitazato, Kaio, Kley, Rudolf A., Klimecki, Walter T., Klinkenberg, Michael, Klucken, Jochen, Knaevelsrud, Helene, Knecht, Erwin, Knuppertz, Laura, Ko, Jiunn-Liang, Kobayashi, Satoru, Koch, Jan C., Koechlin-Ramonatxo, Christelle, Koenig, Ulrich, Ko, Young Ho, Koehler, Katja, Kohlwein, Sepp D., Koike, Masato, Komatsu, Masaaki, Kominami, Eiki, Kong, Dexin, Kong, Hee Jeong, Konstantakou, Eumorphia G., Kopp, Benjamin T., Korcsmaros, Tamas, Korhonen, Laura, Korolchuk, Viktor I., Koshkina, Nadya V., Kou, Yanjun, Koukourakis, Michael I., Koumenis, Constantinos, Kovacs, Attila L., Kovacs, Tibor, Kovacs, Werner J., Koya, Daisuke, Kraft, Claudine, Krainc, Dimitri, Kramer, Helmut, Kravic-Stevovic, Tamara, Krek, Wilhelm, Kretz-Remy, Carole, Krick, Roswitha, Krishnamurthy, Malathi, Kriston-Vizi, Janos, Kroemer, Guido, Kruer, Michael C., Kruger, Rejko, Ktistakis, Nicholas T., Kuchitsu, Kazuyuki, Kuhn, Christian, Kumar, Addanki Pratap, Kumar, Anuj, Kumar, Ashok, Kumar, Deepak, Kumar, Dhiraj, Kumar, Rakesh, Kumar, Sharad, Kundu, Mondira, Kung, Hsing-Jien, Kuno, Atsushi, Kuo, Sheng-Han, Kuret, Jeff, Kurz, Tino, Kwok, Terry, Kwon, Taeg Kyu, Kwon, Yong Tae, Kyrmizi, Irene, La Spada, Albert R., Lafont, Frank, Lahm, Tim, Lakkaraju, Aparna, Lam, Truong, Lamark, Trond, Lancel, Steve, Landowski, Terry H., Lane, Darius J. R., Lane, Jon D., Lanzi, Cinzia, Lapaquette, Pierre, Lapierre, Louis R., Laporte, Jocelyn, Laukkarinen, Johanna, Laurie, Gordon W., Lavandero, Sergio, Lavie, Lena, LaVoie, Matthew J., Law, Betty Yuen Kwan, Law, Helen Ka-wai, Law, Kelsey B., Layfield, Robert, Lazo, Pedro A., Le Cam, Laurent, Le Roch, Karine G., Le Stunff, Herve, Leardkamolkarn, Vijittra, Lecuit, Marc, Lee, Byung-Hoon, Lee, Che-Hsin, Lee, Erinna F., Lee, Gyun Min, Lee, He-Jin, Lee, Hsinyu, Lee, Jae Keun, Lee, Jongdae, Lee, Ju-Hyun, Lee, Jun Hee, Lee, Michael, Lee, Myung-Shik, Lee, Patty J., Lee, Sam W., Lee, Seung-Jae, Lee, Shiow-Ju, Lee, Stella Y., Lee, Sug Hyung, Lee, Sung Sik, Lee, Sung-Joon, Lee, Sunhee, Lee, Ying-Ray, Lee, Yong J., Lee, Young H., Leeuwenburgh, Christiaan, Lefort, Sylvain, Legouis, Renaud, Lei, Jinzhi, Lei, Qun-Ying, Leib, David A., Leibowitz, Gil, Lekli, Istvan, Lemaire, Stephane D., Lemasters, John J., Lemberg, Marius K., Lemoine, Antoinette, Leng, Shuilong, Lenz, Guido, Lenzi, Paola, Lerman, Lilach O., Barbato, Daniele Lettieri, Leu, Julia I-Ju, Leung, Hing Y., Levine, Beth, Lewis, Patrick A., Lezoualc'h, Frank, Li, Chi, Li, Faqiang, Li, Feng-Jun, Li, Jun, Li, Ke, Li, Lian, Li, Min, Li, Qiang, Li, Rui, Li, Sheng, Li, Wei, Li, Xiaotao, Li, Yumin, Lian, Jiqin, Liang, Chengyu, Liang, Qiangrong, Liao, Yulin, Liberal, Joana, Liberski, Pawel P., Lie, Pearl, Lieberman, Andrew P., Lim, Hyunjung Jade, Lim, Kah-Leong, Lim, Kyu, Lima, Raquel T., Lin, Chang-Shen, Lin, Chiou-Feng, Lin, Fang, Lin, Fangming, Lin, Fu-Cheng, Lin, Kui, Lin, Kwang-Huei, Lin, Pei-Hui, Lin, Tianwei, Lin, Wan-Wan, Lin, Yee-Shin, Lin, Yong, Linden, Rafael, Lindholm, Dan, Lindqvist, Lisa M., Lingor, Paul, Linkermann, Andreas, Liotta, Lance A., Lipinski, Marta M., Lira, Vitor A., Lisanti, Michael P., Liton, Paloma B., Liu, Bo, Liu, Chong, Liu, Chun-Feng, Liu, Fei, Liu, Hung-Jen, Liu, Jianxun, Liu, Jing-Jing, Liu, Jing-Lan, Liu, Ke, Liu, Leyuan, Liu, Liang, Liu, Quentin, Liu, Rong-Yu, Liu, Shiming, Liu, Shuwen, Liu, Wei, Liu, Xian-De, Liu, Xiangguo, Liu, Xiao-Hong, Liu, Xinfeng, Liu, Xu, Liu, Xueqin, Liu, Yang, Liu, Yule, Liu, Zexian, Liu, Zhe, Liuzzi, Juan P., Lizard, Gerard, Ljujic, Mila, Lodhi, Irfan J., Logue, Susan E., Lokeshwar, Bal L., Long, Yun Chau, Lonial, Sagar, Loos, Benjamin, Lopez-Otin, Carlos, Lopez-Vicario, Cristina, Lorente, Mar, Lorenzi, Philip L., Lorincz, Peter, Los, Marek, Lotze, Michael T., Lovat, Penny E., Lu, Binfeng, Lu, Bo, Lu, Jiahong, Lu, Qing, Lu, She-Min, Lu, Shuyan, Lu, Yingying, Luciano, Federic, Luckhart, Shirley, Lucocq, John Milton, Ludovico, Paula, Lugea, Aurelia, Lukacs, Nicholas W., Lum, Julian J., Lund, Anders H., Luo, Honglin, Luo, Jia, Luo, Shouqing, Luparello, Claudio, Lyons, Timothy, Ma, Jianjie, Ma, Yi, Ma, Yong, Ma, Zhenyi, Machado, Juliano, Machado-Santelli, Glaucia M., Macian, Fernando, MacIntosh, Gustavo C., MacKeigan, Jeffrey P., Macleod, Kay F., MacMicking, John D., MacMillan-Crow, Lee Ann, Madeo, Frank, Madesh, Muniswamy, Madrigal-Matute, Julio, Maeda, Akiko, Maeda, Tatsuya, Maegawa, Gustavo, Maellaro, Emilia, Maes, Hannelore, Magarinos, Marta, Maiese, Kenneth, Maiti, Tapas K., Maiuri, Luigi, Maiuri, Maria Chiara, Maki, Carl G., Malli, Roland, Malorni, Walter, Maloyan, Alina, Mami-Chouaib, Fathia, Man, Na, Mancias, Joseph D., Mandelkow, Eva-Maria, Mandell, Michael A., Manfredi, Angelo A., Manie, Serge N., Manzoni, Claudia, Mao, Kai, Mao, Zixu, Mao, Zong-Wan, Marambaud, Philippe, Marconi, Anna Maria, Marelja, Zvonimir, Marfe, Gabriella, Margeta, Marta, Margittai, Eva, Mari, Muriel, Mariani, Francesca V., Marin, Concepcio, Marinelli, Sara, Marino, Guillermo, Markovic, Ivanka, Marquez, Rebecca, Martelli, Alberto M., Martens, Sascha, Martin, Katie R., Martin, Seamus J., Martin, Shaun, Martin-Acebes, Miguel A., Martin-Sanz, Paloma, Martinand-Mari, Camille, Martinet, Wim, Martinez, Jennifer, Martinez-Lopez, Nuria, Martinez-Outschoorn, Ubaldo, Martinez-Velazquez, Moises, Martinez-Vicente, Marta, Martins, Waleska Kerllen, Mashima, Hirosato, Mastrianni, James A., Matarese, Giuseppe, Matarrese, Paola, Mateo, Roberto, Matoba, Satoaki, Matsumoto, Naomichi, Matsushita, Takehiko, Matsuura, Akira, Matsuzawa, Takeshi, Mattson, Mark P., Matus, Soledad, Maugeri, Norma, Mauvezin, Caroline, Mayer, Andreas, Maysinger, Dusica, Mazzolini, Guillermo D., McBrayer, Mary Kate, McCall, Kimberly, McCormick, Craig, McInerney, Gerald M., McIver, Skye C., McKenna, Sharon, McMahon, John J., McNeish, Iain A., Mechta-Grigoriou, Fatima, Medema, Jan Paul, Medina, Diego L., Megyeri, Klara, Mehrpour, Maryam, Mehta, Jawahar L., Mei, Yide, Meier, Ute-Christiane, Meijer, Alfred J., Melendez, Alicia, Melino, Gerry, Melino, Sonia, Tenorio de Melo, Edesio Jose, Mena, Maria A., Meneghini, Marc D., Menendez, Javier A., Menezes, Regina, Meng, Liesu, Meng, Ling-hua, Meng, Songshu, Menghini, Rossella, Menko, A. Sue, Menna-Barreto, Rubem F. S., Menon, Manoj B., Meraz-Rios, Marco A., Merla, Giuseppe, Merlini, Luciano, Merlot, Angelica M., Meryk, Andreas, Meschini, Stefania, Meyer, Joel N., Mi, Man-Tian, Miao, Chao-Yu, Micale, Lucia, Michaeli, Simon, Michiels, Carine, Migliaccio, Anna Rita, Mihailidou, Anastasia Susie, Mijaljica, Dalibor, Mikoshiba, Katsuhiko, Milan, Enrico, Miller-Fleming, Leonor, Mills, Gordon B., Mills, Ian G., Minakaki, Georgia, Minassian, Berge A., Ming, Xiu-Fen, Minibayeva, Farida, Minina, Elena A., Mintern, Justine D., Minucci, Saverio, Miranda-Vizuete, Antonio, Mitchell, Claire H., Miyamoto, Shigeki, Miyazawa, Keisuke, Mizushima, Noboru, Mnich, Katarzyna, Mograbi, Baharia, Mohseni, Simin, Moita, Luis Ferreira, Molinari, Marco, Molinari, Maurizio, Moller, Andreas Buch, Mollereau, Bertrand, Mollinedo, Faustino, Monick, Martha M., Montagnaro, Serena, Montell, Craig, Moore, Darren J., Moore, Michael N., Mora-Rodriguez, Rodrigo, Moreira, Paula I., Morel, Etienne, Morelli, Maria Beatrice, Moreno, Sandra, Morgan, Michael J., Moris, Arnaud, Moriyasu, Yuji, Morrison, Janna L., Morrison, Lynda A., Morselli, Eugenia, Moscat, Jorge, Moseley, Pope L., Mostowy, Serge, Motori, Elisa, Mottet, Denis, Mottram, Jeremy C., Moussa, Charbel E-H, Mpakou, Vassiliki E., Mukhtar, Hasan, Levy, Jean M. Mulcahy, Muller, Sylviane, Munoz-Moreno, Raquel, Munoz-Pinedo, Cristina, Muenz, Christian, Murphy, Maureen E., Murray, James T., Murthy, Aditya, Mysorekar, Indira U., Nabi, Ivan R., Nabissi, Massimo, Nader, Gustavo A., Nagahara, Yukitoshi, Nagai, Yoshitaka, Nagata, Kazuhiro, Nagelkerke, Anika, Nagy, Peter, Naidu, Samisubbu R., Nair, Sreejayan, Nakano, Hiroyasu, Nakatogawa, Hitoshi, Nanjundan, Meera, Napolitano, Gennaro, Naqvi, Naweed I., Nardacci, Roberta, Narendra, Derek P., Narita, Masashi, Nascimbeni, Anna Chiara, Natarajan, Ramesh, Navegantes, Luiz C., Nawrocki, Steffan T., Nazarko, Taras Y., Nazarko, Volodymyr Y., Neill, Thomas, Neri, Luca M., Netea, Mihai G., Netea-Maier, Romana T., Neves, Bruno M., Ney, Paul A., Nezis, Ioannis P., Nguyen, Hang T. T., Nicot, Anne-Sophie, Nilsen, Hilde, Nilsson, Per, Nishimura, Mikio, Nishino, Ichizo, Niso-Santano, Mireia, Niu, Hua, Nixon, Ralph A., Njar, Vincent C. O., Noda, Takeshi, Noegel, Angelika A., Nolte, Elsie Magdalena, Norberg, Erik, Norga, Koenraad K., Noureini, Sakineh Kazemi, Notomi, Shoji, Notterpek, Lucia, Nowikovsky, Karin, Nukina, Nobuyuki, Nuernberger, Thorsten, O'Donnell, Valerie B., O'Donovan, Tracey, O'Dwyer, Peter J., Oehme, Ina, Oeste, Clara L., Ogawa, Michinaga, Ogretmen, Besim, Ogura, Yuji, Oh, Young J., Ohmuraya, Masaki, Ohshima, Takayuki, Ojha, Rani, Okamoto, Koji, Okazaki, Toshiro, Oliver, F. Javier, Ollinger, Karin, Olsson, Stefan, Orban, Daniel P., Ordonez, Paulina, Orhon, Idil, Orosz, Laszlo, O'Rourke, Eyleen J., Orozco, Helena, Ortega, Angel L., Ortona, Elena, Osellame, Laura D., Oshima, Junko, Oshima, Shigeru, Osiewacz, Heinz D., Otomo, Takanobu, Otsu, Kinya, Ou, Jing-hsiung James, Outeiro, Tiago F., Ouyang, Dong-yun, Ouyang, Hongjiao, Overholtzer, Michael, Ozbun, Michelle A., Ozdinler, P. Hande, Ozpolat, Bulent, Pacelli, Consiglia, Paganetti, Paolo, Page, Guylene, Pages, Gilles, Pagnini, Ugo, Pajak, Beata, Pak, Stephen C., Pakos-Zebrucka, Karolina, Pakpour, Nazzy, Palkova, Zdena, Palladino, Francesca, Pallauf, Kathrin, Pallet, Nicolas, Palmieri, Marta, Paludan, Soren R., Palumbo, Camilla, Palumbo, Silvia, Pampliega, Olatz, Pan, Hongming, Pan, Wei, Panaretakis, Theocharis, Pandey, Aseem, Pantazopoulou, Areti, Papackova, Zuzana, Papademetrio, Daniela L., Papassideri, Issidora, Papini, Alessio, Parajuli, Nirmala, Pardo, Julian, Parekh, Vrajesh V., Parenti, Giancarlo, Park, Jong-In, Park, Junsoo, Park, Ohkmae K., Parker, Roy, Parlato, Rosanna, Parys, Jan B., Parzych, Katherine R., Pasquet, Jean-Max, Pasquier, Benoit, Pasumarthi, Kishore B. S., Patschan, Daniel, Patterson, Cam, Pattingre, Sophie, Pattison, Scott, Pause, Arnim, Pavenstaedt, Hermann, Pavone, Flaminia, Pedrozo, Zully, Pena, Fernando J., Penalva, Miguel A., Pende, Mario, Peng, Jianxin, Penna, Fabio, Penninger, Josef M., Pensalfini, Anna, Pepe, Salvatore, Pereira, Gustavo J. S., Pereira, Paulo C., Perez-de la Cruz, Veronica, Esther Perez-Perez, Maria, Perez-Rodriguez, Diego, Perez-Sala, Dolores, Perier, Celine, Perl, Andras, Perlmutter, David H., Perrotta, Ida, Pervaiz, Shazib, Pesonen, Maija, Pessin, Jeffrey E., Peters, Godefridus J., Petersen, Morten, Petrache, Irina, Petrof, Basil J., Petrovski, Goran, Phang, James M., Piacentini, Mauro, Pierdominici, Marina, Pierre, Philippe, Pierrefite-Carle, Valerie, Pietrocola, Federico, Pimentel-Muinos, Felipe X., Pinar, Mario, Pineda, Benjamin, Pinkas-Kramarski, Ronit, Pinti, Marcello, Pinton, Paolo, Piperdi, Bilal, Piret, James M., Platanias, Leonidas C., Platta, Harald W., Plowey, Edward D., Poggeler, Stefanie, Poirot, Marc, Polcic, Peter, Poletti, Angelo, Poon, Audrey H., Popelka, Hana, Popova, Blagovesta, Poprawa, Izabela, Poulose, Shibu M., Poulton, Joanna, Powers, Scott K., Powers, Ted, Pozuelo-Rubio, Mercedes, Prak, Krisna, Prange, Reinhild, Prescott, Mark, Priault, Muriel, Prince, Sharon, Proia, Richard L., Proikas-Cezanne, Tassula, Prokisch, Holger, Promponas, Vasilis J., Przyklenk, Karin, Puertollano, Rosa, Pugazhenthi, Subbiah, Puglielli, Luigi, Pujol, Aurora, Puyal, Julien, Pyeon, Dohun, Qi, Xin, Qian, Wen-bin, Qin, Zheng-Hong, Qiu, Yu, Qu, Ziwei, Quadrilatero, Joe, Quinn, Frederick, Raben, Nina, Rabinowich, Hannah, Radogna, Flavia, Ragusa, Michael J., Rahmani, Mohamed, Raina, Komal, Ramanadham, Sasanka, Ramesh, Rajagopal, Rami, Abdelhaq, Randall-Demllo, Sarron, Randow, Felix, Rao, Hai, Rao, V. Ashutosh, Rasmussen, Blake B., Rasse, Tobias M., Ratovitski, Edward A., Rautou, Pierre-Emmanuel, Ray, Swapan K., Razani, Babak, Reed, Bruce H., Reggiori, Fulvio, Rehm, Markus, Reichert, Andreas S., Rein, Theo, Reiner, David J., Reits, Eric, Ren, Jun, Ren, Xingcong, Renna, Maurizio, Reusch, Jane E. B., Revuelta, Jose L., Reyes, Leticia, Rezaie, Alireza R., Richards, Robert I., Richardson, Des R., Richetta, Clemence, Riehle, Michael A., Rihn, Bertrand H., Rikihisa, Yasuko, Riley, Brigit E., Rimbach, Gerald, Rippo, Maria Rita, Ritis, Konstantinos, Rizzi, Federica, Rizzo, Elizete, Roach, Peter J., Robbins, Jeffrey, Roberge, Michel, Roca, Gabriela, Roccheri, Maria Carmela, Rocha, Sonia, Rodrigues, Cecilia M. P., Rodriguez, Clara I., Rodriguez de Cordoba, Santiago, Rodriguez-Muela, Natalia, Roelofs, Jeroen, Rogov, Vladimir V., Rohn, Troy T., Rohrer, Baerbel, Romanelli, Davide, Romani, Luigina, Silvia Romano, Patricia, Roncero, M. Isabel G., Luis Rosa, Jose, Rosello, Alicia, Rosen, Kirill V., Rosenstiel, Philip, Rost-Roszkowska, Magdalena, Roth, Kevin A., Roue, Gael, Rouis, Mustapha, Rouschop, Kasper M., Ruan, Daniel T., Ruano, Diego, Rubinsztein, David C., Rucker, Edmund B., III, Rudich, Assaf, Rudolf, Emil, Rudolf, Ruediger, Ruegg, Markus A., Ruiz-Roldan, Carmen, Ruparelia, Avnika Ashok, Rusmini, Paola, Russ, David W., Russo, Gian Luigi, Russo, Giuseppe, Russo, Rossella, Rusten, Tor Erik, Ryabovol, Victoria, Ryan, Kevin M., Ryter, Stefan W., Sabatini, David M., Sacher, Michael, Sachse, Carsten, Sack, Michael N., Sadoshima, Junichi, Saftig, Paul, Sagi-Eisenberg, Ronit, Sahni, Sumit, Saikumar, Pothana, Saito, Tsunenori, Saitoh, Tatsuya, Sakakura, Koichi, Sakoh-Nakatogawa, Machiko, Sakuraba, Yasuhito, Salazar-Roa, Maria, Salomoni, Paolo, Saluja, Ashok K., Salvaterra, Paul M., Salvioli, Rosa, Samali, Afshin, Sanchez, Anthony M. J., Sanchez-Alcazar, Jose A., Sanchez-Prieto, Ricardo, Sandri, Marco, Sanjuan, Miguel A., Santaguida, Stefano, Santambrogio, Laura, Santoni, Giorgio, dos Santos, Claudia Nunes, and Saran, Shweta
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- 2016
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