Cellular strategies for controlling protein aggregation
By J. Tyedmers, Axel Mogk, Bernd Bukau. Nature reviews. Molecular cell biology, 2010
909 citations recorded by the source corpus.
Subfields: Cell Biology, Cellular and Molecular Neuroscience, Materials Chemistry
View Paper: https://www.semanticscholar.org/paper/4ce64b456fdba786e3fa0db6a7b60d19eba99dd1
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In Cell Biology
In Cellular and Molecular Neuroscience
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Citations in the corpus
- Oxidative stress in neurodegenerative diseases (2012, background): “Although the pathogenicity of protein aggregates remains uncertain [56] , a causative link between the formation of protein aggregates and neurodegeneration has been established, which may occur as a result of the toxic action of substances produced during early phases, and soluble oligomers and pro”
- Quantifying absolute protein synthesis rates reveals principles underlying allocation of cellular resources. (2014, background): “The subunits of these complexes require balanced steady-state levels because excess components are often prone to misfolding or aggregation (Tyedmers et al., 2010).”
- Order out of Disorder: Working Cycle of an Intrinsically Unfolded Chaperone (2012, background): “Molecularchaperonesare involved inmaintaininga functionalproteome (Tyedmers et al., 2010).”
- Liquid-liquid phase separation in biology. (2014, background): “The cell copes with such aggregation processes using deaggregases (Doyle et al. 2013, Pickett 2006, Tyedmers et al. 2010) and will also regulate the dynamics of the compartments by, for instance, phosphorylation and dephosphorylation (Wippich et al. 2013).”