Regulation of skeletal muscle oxidative capacity and muscle mass by SIRT3. - Test2 - elhamkhani - TriplyDB

Regulation of skeletal muscle oxidative capacity and muscle mass by SIRT3.

Regulation of skeletal muscle oxidative capacity and muscle mass by SIRT3.

http://www.wikidata.org/entity/Q37484275

about

SIRT3 as a Regulator of Non-alcoholic Fatty Liver Disease Improvement of Endurance Based on Muscle Fiber-Type Composition by Treatment with Dietary Apple Polyphenols in Rats FoxO1: a novel insight into its molecular mechanisms in the regulation of skeletal muscle differentiation and fiber type specification Combined training enhances skeletal muscle mitochondrial oxidative capacity independent of age Sirtuin3 Dysfunction Is the Key Determinant of Skeletal Muscle Insulin Resistance by Angiotensin II SIRT3-AMP-Activated Protein Kinase Activation by Nitrite and Metformin Improves Hyperglycemia and Normalizes Pulmonary Hypertension Associated With Heart Failure With Preserved Ejection Fraction Mild endothelial dysfunction in Sirt3 knockout mice fed a high-cholesterol diet: protective role of a novel C/EBP-β-dependent feedback regulation of SOD2 Mitochondrial SIRT3 Mediates Adaptive Responses of Neurons to Exercise and Metabolic and Excitatory Challenges AAV-mediated Sirt1 overexpression in skeletal muscle activates oxidative capacity but does not prevent insulin resistance AMPK in skeletal muscle function and metabolism.Fast-to-slow shift of muscle fiber-type composition by dietary apple polyphenols in rats: Impact of the low-dose supplementation.Preventing muscle wasting by osteoporosis drug alendronate in vitro and in myopathy models via sirtuin-3 down-regulation.Beneficial Autophagic Activities, Mitochondrial Function, and Metabolic Phenotype Adaptations Promoted by High-Intensity Interval Training in a Rat Model.Elevated Nicotinamide Phosphoribosyl Transferase in Skeletal Muscle Augments Exercise Performance and Mitochondrial Respiratory Capacity Following Exercise Training.

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Regulation of skeletal muscle oxidative capacity and muscle mass by SIRT3.

http://www.wikidata.org/entity/Q37484275

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 15 January 2014

@en

vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

@cs

name

Regulation of skeletal muscle oxidative capacity and muscle mass by SIRT3.

@en

Regulation of skeletal muscle oxidative capacity and muscle mass by SIRT3.

@nl

type

label

Regulation of skeletal muscle oxidative capacity and muscle mass by SIRT3.

@en

Regulation of skeletal muscle oxidative capacity and muscle mass by SIRT3.

@nl

prefLabel

Regulation of skeletal muscle oxidative capacity and muscle mass by SIRT3.

@en

Regulation of skeletal muscle oxidative capacity and muscle mass by SIRT3.

@nl

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JOURNAL.PONE.0085636

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Regulation of skeletal muscle oxidative capacity and muscle mass by SIRT3.

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Béatrice Chabi

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Chantal Wrutniak-Cabello

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Henry Yang

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Jack Lee Ward

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Keyun Chen

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Ligen Lin

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Qiang Tong

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Waed Abdel Khalek

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P2860

Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2

Identification and characterization of proteins interacting with SIRT1 and SIRT3: implications in the anti-aging and metabolic effects of sirtuins

AMP kinase is required for mitochondrial biogenesis in skeletal muscle in response to chronic energy deprivation.

Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases

SIRT3 is a mitochondria-localized tumor suppressor required for maintenance of mitochondrial integrity and metabolism during stress

SIRT3 deacetylates mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase 2 and regulates ketone body production

AMPK and PPARdelta agonists are exercise mimetics

Regulation of muscle fiber type and running endurance by PPARdelta

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling

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e85636

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scholarly article

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10.1371/JOURNAL.PONE.0085636

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259879559

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