The molecular basis for load-induced skeletal muscle hypertrophy - Wikidata - wikimedia - TriplyDB

The molecular basis for load-induced skeletal muscle hypertrophy

The molecular basis for load-induced skeletal muscle hypertrophy

http://www.wikidata.org/entity/Q26829477

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MicroRNAs in Muscle: Characterizing the Powerlifter Phenotype.Intramuscular anabolic signaling and endocrine response following high volume and high intensity resistance exercise protocols in trained men Korean mistletoe (Viscum album coloratum) extract regulates gene expression related to muscle atrophy and muscle hypertrophy Hypertrophy-Promoting Effects of Leucine Supplementation and Moderate Intensity Aerobic Exercise in Pre-Senescent Mice.Erythropoietin Does Not Enhance Skeletal Muscle Protein Synthesis Following Exercise in Young and Older Adults.Integrated therapies for osteoporosis and sarcopenia: from signaling pathways to clinical trials.Do metabolites that are produced during resistance exercise enhance muscle hypertrophy?Intramuscular Anabolic Signaling and Endocrine Response Following Resistance Exercise: Implications for Muscle Hypertrophy.Overload-mediated skeletal muscle hypertrophy is not impaired by loss of myofiber STAT3.Leucine elicits myotube hypertrophy and enhances maximal contractile force in tissue engineered skeletal muscle in vitro.Carbohydrate intake and resistance-based exercise: are current recommendations reflective of actual need?Differential localisation and anabolic responsiveness of mTOR complexes in human skeletal muscle in response to feeding and exercise.Increased autophagy signaling but not proteasome activity in human skeletal muscle after prolonged low-intensity exercise with negative energy balance.Enhanced skeletal muscle regrowth and remodelling in massaged and contralateral non-massaged hindlimb.Interpreting Signal Amplitudes in Surface Electromyography Studies in Sport and Rehabilitation Sciences.Mammalian target of rapamycin complex 2 regulates muscle glucose uptake during exercise in mice.Select Skeletal Muscle mRNAs Related to Exercise Adaptation Are Minimally Affected by Different Pre-exercise Meals that Differ in Macronutrient Profile.The effect of exercise hypertrophy and disuse atrophy on muscle contractile properties: a mechanomyographic analysis.Translocation and protein complex co-localization of mTOR is associated with postprandial myofibrillar protein synthesis at rest and after endurance exercise.Genes Whose Gain or Loss-Of-Function Increases Skeletal Muscle Mass in Mice: A Systematic Literature Review.

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The molecular basis for load-induced skeletal muscle hypertrophy

http://www.wikidata.org/entity/Q26829477

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2015 nî lūn-bûn

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2015 թուականի Մարտին հրատարակուած գիտական յօդուած

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2015 թվականի մարտին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

@zh-hk

2015年論文

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2015年論文

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2015年论文

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name

The molecular basis for load-induced skeletal muscle hypertrophy

@ast

The molecular basis for load-induced skeletal muscle hypertrophy

@en

The molecular basis for load-induced skeletal muscle hypertrophy

@nl

type

label

The molecular basis for load-induced skeletal muscle hypertrophy

@ast

The molecular basis for load-induced skeletal muscle hypertrophy

@en

The molecular basis for load-induced skeletal muscle hypertrophy

@nl

prefLabel

The molecular basis for load-induced skeletal muscle hypertrophy

@ast

The molecular basis for load-induced skeletal muscle hypertrophy

@en

The molecular basis for load-induced skeletal muscle hypertrophy

@nl

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S00223-014-9925-9

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Calcified Tissue International

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The molecular basis for load-induced skeletal muscle hypertrophy

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Daniel W. D. West

http://www.w3.org/2001/XMLSchema#string

George R. Marcotte

http://www.w3.org/2001/XMLSchema#string

Keith Baar

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P2860

A mutation in the myostatin gene increases muscle mass and enhances racing performance in heterozygote dogs

Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B

TBC1D7 is a third subunit of the TSC1-TSC2 complex upstream of mTORC1

A Tumor suppressor complex with GAP activity for the Rag GTPases that signal amino acid sufficiency to mTORC1

Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex

Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1

Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action

Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids

Leucyl-tRNA synthetase is an intracellular leucine sensor for the mTORC1-signaling pathway

Myostatin reduces Akt/TORC1/p70S6K signaling, inhibiting myoblast differentiation and myotube size

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