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Article summary:

1. Mitochondrial dysfunction leads to cytosolic accumulation of mitochondrial precursor proteins, compromising cellular proteostasis and triggering a mitoprotein-induced stress response.

2. Pre-post thermal proteome profiling is a multiplexed time-resolved proteome-wide thermal stability profiling approach that can elucidate dynamic proteostasis changes in several dimensions, including adaptations in protein abundance and rapid modulations of the thermal stability of individual cellular proteins.

3. Different functional groups of proteins show characteristic response patterns and react with group-specific kinetics, allowing the identification of functional modules that are relevant for mitoprotein-induced stress. This complex response network orchestrates proteome homeostasis in eukaryotic cells by time-controlled adaptations of the abundance and conformation of proteins.

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