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000280046 1001_ $$00000-0002-3389-136X$$aEspay, Alberto J$$b0
000280046 245__ $$aPhysics of Protein Aggregation in Normal and Accelerated Brain Aging.
000280046 260__ $$aNew York, NY$$bWiley-Liss$$c2025
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000280046 520__ $$aProtein aggregation is a normal response to age-related exposures. According to the thermodynamic hypothesis of protein folding, soluble proteins precipitate into amyloids (pathology) under supersaturated conditions through a process similar to crystallization. This soluble-to-insoluble phase transition occurs via nucleation and may be catalyzed by ectopic surfaces such as lipid nanoparticles, microbes, or chemical pollutants. The increasing prevalence of these exposures with age correlates with the rising incidence of pathology over the lifespan. However, the formation of amyloid fibrils does not inherently cause neurodegeneration. Neurodegeneration emerges when the levels of functional monomeric proteins, from which amyloids form, fall below a critical threshold. The preservation of monomeric proteins may explain neurological resilience, regardless of the extent of amyloid deposition. This biophysical framework challenges the traditional clinicopathological view that considers amyloids intrinsically toxic, despite the absence of a known mechanism of toxicity. Instead, it suggests that chronic exposures driving persistent nucleation consume monomeric proteins as they aggregate. In normal aging, replacement matches loss; in accelerated aging, it does not. A biophysical approach to neurodegenerative diseases has important therapeutic implications, refocusing treatment strategies from removing pathology to restoring monomeric protein homeostasis above the threshold needed to sustain normal brain function.
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000280046 650_7 $$2Other$$aAlzheimer's disease
000280046 650_7 $$2Other$$aParkinson's disease
000280046 650_7 $$2Other$$aamyloid
000280046 650_7 $$2Other$$across‐beta
000280046 650_7 $$2Other$$anucleation
000280046 650_7 $$2Other$$aseed amplification assay
000280046 650_7 $$2Other$$asupersaturation
000280046 650_7 $$2NLM Chemicals$$aAmyloid
000280046 650_7 $$2NLM Chemicals$$aProtein Aggregates
000280046 650_2 $$2MeSH$$aHumans
000280046 650_2 $$2MeSH$$aAging: metabolism
000280046 650_2 $$2MeSH$$aAging: pathology
000280046 650_2 $$2MeSH$$aBrain: metabolism
000280046 650_2 $$2MeSH$$aBrain: pathology
000280046 650_2 $$2MeSH$$aAmyloid: metabolism
000280046 650_2 $$2MeSH$$aAmyloid: chemistry
000280046 650_2 $$2MeSH$$aProtein Aggregates
000280046 650_2 $$2MeSH$$aNeurodegenerative Diseases: metabolism
000280046 650_2 $$2MeSH$$aNeurodegenerative Diseases: pathology
000280046 650_2 $$2MeSH$$aAnimals
000280046 650_2 $$2MeSH$$aProtein Aggregation, Pathological: metabolism
000280046 650_2 $$2MeSH$$aProtein Folding
000280046 650_2 $$2MeSH$$aThermodynamics
000280046 7001_ $$aSturchio, Andrea$$b1
000280046 7001_ $$00000-0002-1206-4170$$aImarisio, Alberto$$b2
000280046 7001_ $$aHill, Emily J$$b3
000280046 7001_ $$aWilliamson, Brady$$b4
000280046 7001_ $$aMontemagno, Kora$$b5
000280046 7001_ $$0P:(DE-2719)9000582$$aHoffmann, Christian$$b6$$udzne
000280046 7001_ $$aRoy, Hugo Le$$b7
000280046 7001_ $$0P:(DE-2719)9000670$$aMilovanovic, Dragomir$$b8$$udzne
000280046 7001_ $$aManfredsson, Fredric P$$b9
000280046 773__ $$0PERI:(DE-600)1473795-4$$a10.1002/bies.70030$$gVol. 47, no. 8, p. e70030$$n8$$pe70030$$tBioessays$$v47$$x0265-9247$$y2025
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