Bridging biophysics and neurology: aberrant phase transitions in neurodegenerative disease
Explore this paper's citation graph
Summary
The evidence that disturbances in phase transition dynamics and the material properties of ribonucleoprotein granules underlie the pathogenesis of many neurodegenerative diseases, including forms of amyotrophic lateral sclerosis and frontotemporal dementia, among others is reviewed.
- Type
- review
- Published
- 2019-03-19
- Cited by
- 168
- References
- 191
- OpenAlex
- https://openalex.org/W2922280666
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:83463684
Keywords
Frontotemporal dementia, Amyotrophic lateral sclerosis, Neuroscience, Disease, C9orf72
References
- P-bodies and stress granules: possible roles in the control of translation and mRNA degradation.
- Short antisense-locked nucleic acids (all-LNAs) correct alternative splicing abnormalities in myotonic dystrophy
- Liquid demixing of intrinsically disordered proteins is seeded by poly(ADP-ribose)
- TDP-43 in aging and Alzheimer's disease - a review.
- Modifiers of C9orf72 DPR toxicity implicate nucleocytoplasmic transport impairments in c9FTD/ALS
- TDP-43 regulates β-adducin (Add2) transcript stability
- TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis
- GGGGCC repeat expansion in C9ORF72 compromises nucleocytoplasmic transport
- The C9ORF72 repeat expansion disrupts nucleocytoplasmic transport
- RNA Toxicity from the ALS/FTD C9ORF72 Expansion Is Mitigated by Antisense Intervention
- Formation and Maturation of Phase Separated Liquid Droplets by RNA Binding Proteins
- Distribution of dipeptide repeat proteins in cellular models and C9orf72 mutation cases suggests link to transcriptional silencing
- TDP-43 repression of nonconserved cryptic exons is compromised in ALS-FTD
- Polymer physics of intracellular phase transitions
- Phase Transitions of Spindle-Associated Protein Regulate Spindle Apparatus Assembly
- Subcellular Localization of Matrin 3 Containing Mutations Associated with ALS and Distal Myopathy
- A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation.
- TDP43 is a human low molecular weight neurofilament (hNFL) mRNA-binding protein.
- Autophagy meets FUS-positive Stress Granules
- Exome-wide Rare Variant Analysis Identifies TUBA4A Mutations Associated with Familial ALS
Cited by
- Liquid–liquid phase separation of tau protein: The crucial role of electrostatic interactions
- m6A-binding YTHDF proteins promote stress granule formation by modulating phase separation of stress granule proteins
- Short Tandem Repeat Expansions and RNA-Mediated Pathogenesis in Myotonic Dystrophy
- Formation of biological condensates via phase separation: Characteristics, analytical methods, and physiological implications
- Physiological, pathological, and targetable membraneless organelles in neurons
- Interplay of miR-137 and EZH2 contributes to the genome-wide redistribution of H3K27me3 underlying the Pb-induced memory impairment
- Molecular structure in biomolecular condensates
- Biomolecular condensates in neurodegeneration and cancer
- The Role of Post-Translational Modifications in the Phase Transitions of Intrinsically Disordered Proteins
- Excitation states of metabolic networks predict dose-response fingerprinting and ligand pulse phase signalling.
- Ropinirole, a New ALS Drug Candidate Developed Using iPSCs.
- Electrostatically driven complex coacervation and amyloid aggregation of tau are independent processes with overlapping conditions.
- hnRNPDL Phase Separation Is Regulated by Alternative Splicing and Disease-Causing Mutations Accelerate Its Aggregation
- Enhanced stress tolerance through reduction of G3BP and suppression of stress granules
- Phase separation at the synapse
- Phase Separation and Cytotoxicity of Tau Are Modulated by Protein Disulfide Isomerase and S-nitrosylation of this Molecular Chaperone.
- Poly(ADP-ribose): A Dynamic Trigger for Biomolecular Condensate Formation
- Tyrosine phosphorylation regulates hnRNPA2 granule protein partitioning and reduces neurodegeneration
- Liquid-liquid phase separation and its mechanistic role in pathological protein aggregation
- Omics Approach to Axonal Dysfunction of Motor Neurons in Amyotrophic Lateral Sclerosis (ALS)
Related papers
- Targeted Screening of the C9orf72 Gene in Bulgarian Amyotrophic Lateral Sclerosis Patients
- Amyotrophic Lateral Sclerosis with Frontotemporal Dementia in the Presence of C9orf72 Repeat Expansion-A Case Report.
- Analysis of C9orf72 hexanucleotide repeat expansions in SOD1 negative patients with amyotrophic lateral sclerosis
- [18F]AV‐1451 binding is increased in frontotemporal dementia due to C9orf72 expansion
- Clinico-pathological features in amyotrophic lateral sclerosis with expansions in C9ORF72.
- C9ORF72 and frontotemporal dementia: a systematic review and meta- analysis
- C9orf72 repeat expansions that cause frontotemporal dementia are detectable among patients with psychosis
- Slowly progressive behavioral frontotemporal dementia with C9orf72 mutation. Case report and review of the literature
- Pathogenic Genome Signatures That Damage Motor Neurons in Amyotrophic Lateral Sclerosis
- Phenotype of Amyotrophic Lateral Sclerosis (ALS) and Frontotemporal Dementia with ALS (FTD/ALS) Associated with the GGGGCC Repeat Expansion in C9ORF72 (c9FTD/ALS) (S05.003)