Browsing by Subject "Protein Biosynthesis"
Now showing items 1-8 of 8
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Complementary Roles of GADD34- and CReP-Containing Eukaryotic Initiation Factor 2α Phosphatases during the Unfolded Protein Response.
(Molecular and cellular biology, 2016-07)Phosphorylation of eukaryotic initiation factor 2α (eIF2α) controls transcriptome-wide changes in mRNA translation in stressed cells. While phosphorylated eIF2α (P-eIF2α) attenuates global protein synthesis, mRNAs encoding ... -
MicroRNA antagonism of the picornaviral life cycle: alternative mechanisms of interference.
(PLoS Pathog, 2010-03-19)In addition to modulating the function and stability of cellular mRNAs, microRNAs can profoundly affect the life cycles of viruses bearing sequence complementary targets, a finding recently exploited to ameliorate toxicities ... -
Proteome-wide muscle protein fractional synthesis rates predict muscle mass gain in response to a selective androgen receptor modulator in rats.
(Am J Physiol Endocrinol Metab, 2016-03-15)Biomarkers of muscle protein synthesis rate could provide early data demonstrating anabolic efficacy for treating muscle-wasting conditions. Androgenic therapies have been shown to increase muscle mass primarily by increasing ... -
Simple and inexpensive ribosome profiling analysis of mRNA translation.
(Methods (San Diego, Calif.), 2015-12)The development and application of ribosome profiling has markedly advanced our understanding of ribosomes and mRNA translation. The experimental approach, which relies on deep sequencing of ribosome-protected mRNA fragments ... -
Structural and Functional Analysis of the GADD34:PP1 eIF2α Phosphatase.
(Cell reports, 2015-06-18)The attenuation of protein synthesis via the phosphorylation of eIF2α is a major stress response of all eukaryotic cells. The growth-arrest- and DNA-damage-induced transcript 34 (GADD34) bound to the serine/threonine protein ... -
Targeting phosphorylation of eukaryotic initiation factor-2α to treat human disease.
(Progress in molecular biology and translational science, 2012-01)The unfolded protein response, also known as endoplasmic reticulum (ER) stress, has been implicated in numerous human diseases, including atherosclerosis, cancer, diabetes, and neurodegenerative disorders. Protein misfolding ... -
The DLK-1 kinase promotes mRNA stability and local translation in C. elegans synapses and axon regeneration.
(Cell, 2009-09-04)Growth cone guidance and synaptic plasticity involve dynamic local changes in proteins at axons and dendrites. The Dual-Leucine zipper Kinase MAPKKK (DLK) has been previously implicated in synaptogenesis and axon outgrowth ... -
The unfolded protein response triggers selective mRNA release from the endoplasmic reticulum.
(Cell, 2014-09)The unfolded protein response (UPR) is a stress response program that reprograms cellular translation and gene expression in response to proteotoxic stress in the endoplasmic reticulum (ER). One of the primary means by which ...
