Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions.

By Heidi Olzscha, Sonya M. Schermann, Andreas C. Woerner, Stefan Pinkert, M. Hecht, G. Tartaglia, Michele Vendruscolo, M. Hayer-Hartl, F. Hartl, R. Vabulas. Cell, 2011

688 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/72d641548858592ca1298e52533da4e21a39be99

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Citations in the corpus

Systematic and quantitative assessment of the ubiquitin modified proteome (2011, neutral): “Recent proteomic studies suggest that aggregation-prone proteins sequester newly synthesized proteins before they reach their native state (Olzscha et al., 2011).”
Molecular chaperones in protein folding and proteostasis (2011, background): “In support of this proposal, a recent proteomics study in human cells showed that certain metastable proteins are targeted preferentially by such interactions, resulting in their co-aggregation with the amyloidogenic disease protei”
The amyloid cascade hypothesis for Alzheimer's disease: an appraisal for the development of therapeutics (2011, background): “However, a recent study demonstrated that the formation of intracellular amyloid-like fibrils resulted in the sequestration of key intracellular proteins, which subsequently led to the derangement of essential cellular processe”
Pathways of cellular proteostasis in aging and disease (2018, background): “However, key cellular factors, including PN components, that interact aberrantly with soluble oligomers may also be sequestered in the insoluble deposits, contributing to cellular dysfunction (Olzscha et al., 2011; Park et al., 2013; Hipp et al., 2014; Ripaud et al., 2014; Yu et al., 2014; Woerner e”
In vivo aspects of protein folding and quality control (2016, background): “A key role in aggregation prevention and aggregate dissociation is played by the Hsp70 machinery, as shown by overexpressing single or multiple components of the system in cellular and animal disease models (124, 154, 182, 183).”
Intrinsically disordered proteins: regulation and disease. (2011, background): “sensitive genes contribute to toxicity because of nonfunctional binding mediated by linear motif or sequestration of other proteins through aggregation prone segments (possibly via stretches enriched in glutamine or hydrophobic amino-acids) [34,35,44,45].”