Biomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing

S Alberti, AA Hyman - Nature reviews Molecular cell biology, 2021 - nature.com
Biomolecular condensates are membraneless intracellular assemblies that often form via
liquid− liquid phase separation and have the ability to concentrate biopolymers. Research …

The proteostasis network and its decline in ageing

MS Hipp, P Kasturi, FU Hartl - Nature reviews Molecular cell biology, 2019 - nature.com
Ageing is a major risk factor for the development of many diseases, prominently including
neurodegenerative disorders such as Alzheimer disease and Parkinson disease. A hallmark …

[HTML][HTML] Pathways of cellular proteostasis in aging and disease

CL Klaips, GG Jayaraj, FU Hartl - The Journal of cell biology, 2018 - ncbi.nlm.nih.gov
Ensuring cellular protein homeostasis, or proteostasis, requires precise control of protein
synthesis, folding, conformational maintenance, and degradation. A complex and adaptive …

In vivo aspects of protein folding and quality control

D Balchin, M Hayer-Hartl, FU Hartl - Science, 2016 - science.org
BACKGROUND Proteins are synthesized on ribosomes as linear chains of amino acids and
must fold into unique three-dimensional structures to fulfill their biological functions. Protein …

p62 links the autophagy pathway and the ubiqutin–proteasome system upon ubiquitinated protein degradation

WJ Liu, L Ye, WF Huang, LJ Guo, ZG Xu, HL Wu… - Cellular & molecular …, 2016 - Springer
The ubiquitin–proteasome system (UPS) and autophagy are two distinct and interacting
proteolytic systems. They play critical roles in cell survival under normal conditions and …

Proteasomal and autophagic degradation systems

I Dikic - Annual review of biochemistry, 2017 - annualreviews.org
Autophagy and the ubiquitin–proteasome system are the two major quality control pathways
responsible for cellular homeostasis. As such, they provide protection against age …

Protein misfolding in neurodegenerative diseases: implications and strategies

P Sweeney, H Park, M Baumann, J Dunlop… - Translational …, 2017 - Springer
A hallmark of neurodegenerative proteinopathies is the formation of misfolded protein
aggregates that cause cellular toxicity and contribute to cellular proteostatic collapse …

Functional amyloids

D Otzen, R Riek - Cold Spring Harbor perspectives in …, 2019 - cshperspectives.cshlp.org
When protein/peptides aggregate, they usually form the amyloid state consisting of cross β-
sheet structure built by repetitively stacked β-strands forming long fibrils. Amyloids are …

The amyloid state and its association with protein misfolding diseases

TPJ Knowles, M Vendruscolo… - Nature reviews Molecular …, 2014 - nature.com
The phenomenon of protein aggregation and amyloid formation has become the subject of
rapidly increasing research activities across a wide range of scientific disciplines. Such …

An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function

D Mateju, TM Franzmann, A Patel, A Kopach… - The EMBO …, 2017 - embopress.org
Stress granules (SG) are membrane‐less compartments involved in regulating mRNAs
during stress. Aberrant forms of SGs have been implicated in age‐related diseases, such as …