Global ETD Search

Search theses and dissertations gathered from participating repositories worldwide. Every result links back to the library that holds it. No account is needed.

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Showing 1 to 3 of 3 for “"5' adenosine monophosphate-activated protein kinase (AMPK)"”.

  1. Skeletal Muscle Protein Turnover During Cancer Cachexia In the Apc<sup>min/+</sup> Mouse

    … exhibits an imbalance in the rate at which proteins are synthesized and degraded, referred to as protein turnover. Our laboratory has shown the ApcMin/+ mouse, a model of colorectal cancer is an excellent model to study the progression of cachexia due to the gradual decline in body weight …

    south-carolina Repository record for Skeletal Muscle Protein Turnover During Cancer Cachexia In the Apc<sup>min/+</sup> Mouse (opens in a new tab)

  2. Regulation of AMPA receptor acetylation and translation by SIRT2 and AMPK: the molecular mechanisms and implications in memory formation

    … neurons is determined by balanced processes of protein translation and degradation. Changes in AMPAR function and trafficking have direct impacts on synaptic transmission and cognitive functions. However, the molecular mechanisms regulating AMPAR expression and dynamics in neurons remain largely …

    bu Repository record for Regulation of AMPA receptor acetylation and translation by SIRT2 and AMPK: the molecular mechanisms and implications in memory formation (opens in a new tab)

  3. Effects of dietary stimulators of metabolism and mitochondrial biogenesis in vitro and in vivo: Implications for metabolic disease

    … of metabolism and peroxisome proliferator-activated receptor gamma co-activator 1 (PGC-1) in skeletal muscle. Our work uniquely describes the effects of a commercially available dietary supplement on resting metabolic rate in humans as well as the metabolic and biochemical effects in vitro. …

    unm Repository record for Effects of dietary stimulators of metabolism and mitochondrial biogenesis in vitro and in vivo: Implications for metabolic disease (opens in a new tab)