Hallmarks of neurodegenerative diseases
DM Wilson, MR Cookson, L Van Den Bosch… - Cell, 2023 - cell.com
Decades of research have identified genetic factors and biochemical pathways involved in
neurodegenerative diseases (NDDs). We present evidence for the following eight hallmarks …
neurodegenerative diseases (NDDs). We present evidence for the following eight hallmarks …
Stress granules and neurodegeneration
Recent advances suggest that the response of RNA metabolism to stress has an important
role in the pathophysiology of neurodegenerative diseases, particularly amyotrophic lateral …
role in the pathophysiology of neurodegenerative diseases, particularly amyotrophic lateral …
Stress granules and processing bodies in translational control
P Ivanov, N Kedersha… - Cold Spring Harbor …, 2019 - cshperspectives.cshlp.org
Stress granules (SGs) and processing bodies (PBs) are non-membrane-enclosed RNA
granules that dynamically sequester translationally inactive messenger ribonucleoprotein …
granules that dynamically sequester translationally inactive messenger ribonucleoprotein …
Structural and hydrodynamic properties of an intrinsically disordered region of a germ cell-specific protein on phase separation
Membrane encapsulation is frequently used by the cell to sequester biomolecules and
compartmentalize their function. Cells also concentrate molecules into phase-separated …
compartmentalize their function. Cells also concentrate molecules into phase-separated …
A new phase of networking: the molecular composition and regulatory dynamics of mammalian stress granules
SR Millar, JQ Huang, KJ Schreiber, YC Tsai… - Chemical …, 2023 - ACS Publications
Stress granules (SGs) are cytosolic biomolecular condensates that form in response to
cellular stress. Weak, multivalent interactions between their protein and RNA constituents …
cellular stress. Weak, multivalent interactions between their protein and RNA constituents …
ALS/FTD mutation-induced phase transition of FUS liquid droplets and reversible hydrogels into irreversible hydrogels impairs RNP granule function
T Murakami, S Qamar, JQ Lin, GSK Schierle, E Rees… - Neuron, 2015 - cell.com
The mechanisms by which mutations in FUS and other RNA binding proteins cause ALS
and FTD remain controversial. We propose a model in which low-complexity (LC) domains …
and FTD remain controversial. We propose a model in which low-complexity (LC) domains …
Stress granules, RNA-binding proteins and polyglutamine diseases: too much aggregation?
A Marcelo, R Koppenol, LP de Almeida, CA Matos… - Cell death & …, 2021 - nature.com
Stress granules (SGs) are membraneless cell compartments formed in response to different
stress stimuli, wherein translation factors, mRNAs, RNA-binding proteins (RBPs) and other …
stress stimuli, wherein translation factors, mRNAs, RNA-binding proteins (RBPs) and other …
The proof is in the process: self-reporting under international human rights treaties
CD Creamer, BA Simmons - American Journal of International Law, 2020 - cambridge.org
Recent research has shown that state reporting to human rights monitoring bodies is
associated with improvements in rights practices, calling into question earlier claims that self …
associated with improvements in rights practices, calling into question earlier claims that self …
An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function
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 …
during stress. Aberrant forms of SGs have been implicated in age‐related diseases, such as …
RNA-binding proteins with prion-like domains in health and disease
AF Harrison, J Shorter - Biochemical Journal, 2017 - portlandpress.com
Approximately 70 human RNA-binding proteins (RBPs) contain a prion-like domain (PrLD).
PrLDs are low-complexity domains that possess a similar amino acid composition to prion …
PrLDs are low-complexity domains that possess a similar amino acid composition to prion …