| Abstrakt: |
Aging is associated with multiple so-called "hallmarks of aging", including accumulation of genetic mutations, epigenetic and metabolic changes, telomere shortening, protein misfolding, accumulation of senescent cells, stem cell exhaustion, altered cell-cell communication and changes to the immune system. These proteins are co-translationally exported across the inner membrane by Oxa1 and assemble with newly imported proteins into membrane protein complexes of the respiratory chain. ShT-06.3-1 GSSG at the center of the protein oxidative folding scene S. Notari* 1, G. Gambardella* 1, M. Castagnola 2, A. Bocedi 1, G. Ricci 1 1 University of Rome "Tor Vergata" - Department of Chemical Sciences and Technologies, Rome,... Oxidized glutathione (GSSG) was considered for many years the main actor for protein oxidative folding, but 20 years ago, ER oxidoreductin 1 and the protein disulphide isomerase were indicated as being mainly responsible for this process. However, these cell fate decisions reveal a wide range of heterogeneity and dynamics depending on physical (radiation quality, dose, etc.), cell biological (origin of the cell, genetic repertoire, cell cycle phase, cell state, etc.), microenvironmental (oxygenation, nutrient supply, pH, etc.), and systemic (overall condition, age, sex, time-of-day, etc.) parameters and have distinct cell autonomous and non-cell autonomous consequences with large impact on the treatment success and adverse side effects. By site-specifically incorporating artificial designer amino acids into proteins, we have developed tools to image and probe proteins [1,2] to study protein-protein interactions and stabilize low-affinity protein complexes [3-6] and to re-engineer and manipulate molecular networks and biological pathways such as ubiquitylation in living cells [7-9]. [Extracted from the article] |
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