Aggresomes, inclusion bodies and protein aggregation.

By R. Kopito. Trends in Cell Biology, 2000

1,984 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/1bd14cfb5737d448a13b21acc1414d33e4f0755c

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

In Molecular Biology

Citations in the corpus

The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. (2003, background): “Second, HDAC6 contains an ubiqui- chaperones are actively recruited to, and are abundantly tin binding zinc finger, and becomes associated with present in, aggresomes (reviewed in Garcia-Mata et al., ubiquitinated proteins upon inhibition of proteasome ac- 2002; Kopito, 2000).”
Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies (2002, positive): “Extracellular amyloid deposits, intracellular aggregates, (e.g., aggresomes) (Kopito, 2000), and other large protein ac-cretions may be late-stage features of a disease process in which the most important effectors of neuronal dysfunction are soluble assemblies that act early and irreversibly…”
Rationalization of the effects of mutations on peptide andprotein aggregation rates (2003, methodology): “Interestingly, application of equation (1) reveals that many mutations are predicted not to increase but to reduce very significantly the rates of aggregation of the peptides and proteins that we investigated.”
A role for ubiquitin in selective autophagy. (2009, background): “They may play protective role by sequestering toxic misfolded protein species and providing the cell with an opportunity of delayed protein degradation (Bjorkoy et al., 2005; Kopito, 2000).”
The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men (2008, background): “The expression of misfolded proteins in cells often leads to the formation of aggresome”
The CamSol method of rational design of protein mutants with enhanced solubility. (2015, background): “This problem affects particularly the recombinant expression of proteins, resulting in insoluble protein aggregates in many cases, such as inclusion bodies [20,21].”
Molecular chaperones in protein folding and proteostasis (2011, background): “These inclusions are often deposited at specific subcellular sites close to the microtubule-organizing centre, referred to as the aggresom”
Neuronal Cell Death. (2018, positive): “In each disease, an unusual misfolding of proteins causes protein deposition as structured or amorphous aggregates that may involve inclusion body formation (360), triggering degenerative signals in the neurons.”
Selective autophagy: ubiquitin-mediated recognition and beyond (2010, background): “This polymerization of partly unfolded proteins is promoted by non-specific hydrophobic interactions that can lead to the formation of large structures known as inclusion bodies and aggresome”
Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice (2005, background): “Autophagy has been implicated in not only organelle turnover but also in elimination of protein aggregates (Kopito, 2000).”
Anticancer activities of histone deacetylase inhibitors (2006, background): “Aggresomes sequester misfolded proteins that would otherwise stimulate a cell-stress response and be toxic to the cell, and facilitate their proteasomal degradatio”