Supersaturation is a major driving force for protein aggregation in neurodegenerative diseases.
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Are aberrant phase transitions a driver of cellular aging?CPAD, Curated Protein Aggregation Database: A Repository of Manually Curated Experimental Data on Protein and Peptide Aggregation.Control of mitochondrial biogenesis and function by the ubiquitin-proteasome systemBiophysical chemistry of the ageing eye lens.Spinal motor neuron protein supersaturation patterns are associated with inclusion body formation in ALS.Protein homeostasis of a metastable subproteome associated with Alzheimer's disease.Nanoscale Control of Amyloid Self-Assembly Using Protein Phase Transfer by Host-Guest ChemistryGranulostasis: Protein Quality Control of RNP Granules.Retrotransposon activation contributes to neurodegeneration in a Drosophila TDP-43 model of ALSA transcriptional signature of Alzheimer's disease is associated with a metastable subproteome at risk for aggregationLiquid-liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau.Amyotrophic lateral sclerosis-like superoxide dismutase 1 proteinopathy is associated with neuronal loss in Parkinson's disease brain.Understanding and predicting protein misfolding and aggregation: Insights from proteomics.The Amyloid Phenomenon and Its Links with Human Disease.Repair or destruction-an intimate liaison between ubiquitin ligases and molecular chaperones in proteostasisIn vitro aggregating β-lactamase-polyQ chimeras do not induce toxic effects in an in vivo Caenorhabditis elegans model.What Can the Kinetics of Amyloid Fibril Formation Tell about Off-pathway Aggregation?Using bicistronic constructs to evaluate the chaperone activities of heat shock proteins in cells.N-terminal Prion Protein Peptides (PrP(120-144)) Form Parallel In-register β-Sheets via Multiple Nucleation-dependent PathwaysAggregation landscapes of Huntingtin exon 1 protein fragments and the critical repeat length for the onset of Huntington's disease.Supersaturated proteins in ALS.High capacity of the endoplasmic reticulum to prevent secretion and aggregation of amyloidogenic proteins.Ion Specificity and Nonmonotonic Protein Solubility from Salt Entropy.Salt-induced formations of partially folded intermediates and amyloid fibrils suggests a common underlying mechanism.mPOS is a novel mitochondrial trigger of cell death - implications for neurodegeneration.Common molecular pathogenesis of disease-related intrinsically disordered proteins revealed by NMR analysis.Polylogarithmic equilibrium treatment of molecular aggregation and critical concentrations.Profilin reduces aggregation and phase separation of huntingtin N-terminal fragments by preferentially binding to soluble monomers and oligomers.Cell biology: Sort and destroy.The Retrotransposon storm and the dangers of a Collyer's genome.Tau protein liquid-liquid phase separation can initiate tau aggregation.The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade.Formation of Toxic Oligomeric Assemblies of RNA-binding Protein: Musashi in Alzheimer's disease
P2860
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P2860
Supersaturation is a major driving force for protein aggregation in neurodegenerative diseases.
description
2015 nî lūn-bûn
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2015年の論文
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2015年学术文章
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name
Supersaturation is a major dri ...... in neurodegenerative diseases.
@en
type
label
Supersaturation is a major dri ...... in neurodegenerative diseases.
@en
prefLabel
Supersaturation is a major dri ...... in neurodegenerative diseases.
@en
P2860
P50
P1476
Supersaturation is a major dri ...... in neurodegenerative diseases.
@en
P2093
Prajwal Ciryam
Richard I Morimoto
P2860
P356
10.1016/J.TIPS.2014.12.004
P577
2015-01-27T00:00:00Z