ALS: Stress Granules

Amyotrophic Lateral Sclerosis (ALS) is a neurodegenerative disease characterized by cytoplasmic protein aggregates within motor neurons. TDP-43 is an ALS-linked protein that is known to regulate splicing and storage of specific mRNAs into stress granules, which have been implicated in formation of ALS protein aggregates. Here is the latest research.

August 5, 2020
Review
Open Access

The role of hnRNPs in frontotemporal dementia and amyotrophic lateral sclerosis

Acta Neuropathologica
Alexander BamptonAriana Gatt
July 6, 2020
Open Access

C9orf72 arginine-rich dipeptide repeats inhibit UPF1-mediated RNA decay via translational repression

Nature Communications
Yu SunJunjie U Guo
February 13, 2020
Review
Open Access

Implications of Selective Autophagy Dysfunction for ALS Pathology

Cells
Emiliano VicencioUte Woehlbier
August 23, 2020
Open Access

Chronic stress induces formation of stress granules and pathological TDP-43 aggregates in human ALS fibroblasts and iPSC-motoneurons

Neurobiology of Disease
Antonia RattiClaudia Colombrita
January 29, 2020
Preprint
Open Access

Spatio-temporal Proteomic Analysis of Stress Granule disassembly using APEX Reveals Regulation by SUMOylation and links to ALS pathogenesis

BioRxiv : the Preprint Server for Biology
Marmor-Kollet HagaiEran Hornstein
May 7, 2020
Review
Open Access

Regulation of RNA granules by FMRP and implications for neurological diseases

Traffic
Austin LaiGary J Bassell
September 17, 2020
Open Access

Mouse Ataxin-2 Expansion Downregulates CamKII and Other Calcium Signaling Factors, Impairing Granule-Purkinje Neuron Synaptic Strength

International Journal of Molecular Sciences
Aleksandar ArsovićGeorg Auburger
December 26, 2019
Open Access

Antiviral Immune Response as a Trigger of FUS Proteinopathy in Amyotrophic Lateral Sclerosis

Cell Reports
Tatyana A ShelkovnikovaVladimir L Buchman
August 9, 2020
Comment / Editorial

TDP-43 Nuclear Bodies: A NEAT Response to Stress?

Molecular Cell
Ahmed M Malik, Sami J Barmada
April 29, 2020

Cytoplasmic localization of amyotrophic lateral sclerosis (ALS)-related TDP-43 proteins modulates stress-granule formation

The European Journal of Neuroscience
Corinne Besnard-Guérin
January 14, 2020
Review
Open Access

Emerging small-molecule therapeutic approaches for amyotrophic lateral sclerosis and frontotemporal dementia

Bioorganic & Medicinal Chemistry Letters
Dean G BrownHeike J Wobst
May 4, 2020
Review

Changing faces of stress: Impact of heat and arsenite treatment on the composition of stress granules

Wiley Interdisciplinary Reviews. RNA
Klára FrydrýškováMartin Pospíšek
August 24, 2020

The pathophysiology of neurodegenerative disease: Disturbing the balance between phase separation and irreversible aggregation

Progress in Molecular Biology and Translational Science
Chelsea J WebberBenjamin Wolozin
July 22, 2020
Open Access

Lysine acetylation regulates the RNA binding, subcellular localization and inclusion formation of FUS

Human Molecular Genetics
Alexandra ArenasHaining Zhu
July 2, 2020
Open Access

Neuronal RNA-binding protein dysfunction in multiple sclerosis cortex

Annals of Clinical and Translational Neurology
Hannah E SalapaMichael C Levin
August 18, 2020
Open Access

An ALS-linked mutation in TDP-43 disrupts normal protein interactions in the motor neuron response to oxidative stress

Neurobiology of Disease
Emily FenebergKevin Talbot

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