about
Guidelines for the use and interpretation of assays for monitoring autophagyThe role of AMP-activated protein kinase in the coordination of skeletal muscle turnover and energy homeostasisAutophagy is essential to support skeletal muscle plasticity in response to endurance exerciseATP-modulated K+ channels sensitive to antidiabetic sulfonylureas are present in adenohypophysis and are involved in growth hormone release.FoxO transcription factors: their roles in the maintenance of skeletal muscle homeostasis.Mechanisms involved in the inhibition of myoblast proliferation and differentiation by myostatin.Pharmacology and regulation of ATP-sensitive K+ channels.AMPK promotes skeletal muscle autophagy through activation of forkhead FoxO3a and interaction with Ulk1.Wnt4 activates the canonical β-catenin pathway and regulates negatively myostatin: functional implication in myogenesis.The atypical alpha2beta2 IGF receptor expressed in inducible c2.7 myoblasts is derived from post-translational modifications of the mouse IGF-I receptor.Autophagy and protein turnover signaling in slow-twitch muscle during exercise.Characterization of a null mutation in ace-1, the gene encoding class A acetylcholinesterase in the nematode Caenorhabditis elegans.ATP/ADP binding sites are present in the sulfonylurea binding protein associated with brain ATP-sensitive K+ channels.AMP-activated protein kinase stabilizes FOXO3 in primary myotubes.Antidiabetic sulfonylureas: localization of binding sites in the brain and effects on the hyperpolarization induced by anoxia in hippocampal slices.Insulin-like growth factor I (IGF-I) receptor overexpression abolishes the IGF requirement for differentiation and induces a ligand-dependent transformed phenotype in C2 inducible myoblastseIF3f depletion impedes mouse embryonic development, reduces adult skeletal muscle mass and amplifies muscle loss during disuse
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description
Forscher
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chercheur
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investigador
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researcher
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ricercatore
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wetenschapper
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研究者
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name
H Bernardi
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H Bernardi
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Henri Bernardi
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Henri Bernardi
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Henri Bernardi
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H Bernardi
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H Bernardi
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Henri Bernardi
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Henri Bernardi
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Henri Bernardi
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H Bernardi
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H Bernardi
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H Bernardi
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Henri Bernardi
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Henri Bernardi
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Henri Bernardi
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P31
P496
0000-0003-3570-8925