Unfolding the role of protein misfolding in neurodegenerative diseases

By Claudio Soto. Nature Reviews Neuroscience, 2003

1,461 citations recorded by the source corpus.

Subfields: Molecular Biology, Neurology, Physiology

View Paper: https://www.semanticscholar.org/paper/6b3e788bba1176c6c47b37213461cf72a4fb666c

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Citations in the corpus

Ways toward an early diagnosis in Alzheimer's disease: The Alzheimer's Disease Neuroimaging Initiative (ADNI) (2005, positive): “While he pathway of the neurofibrillary tangles is very precise, ie, tarts in the entorhinal cortex from where it progresses to he hippocampus, the limbic system, and finally to neocorical regions, the amyloid deposition seems to be more eterogeneous and random starting first in neocortical reions b”
Central and Systemic Endotoxin Challenges Exacerbate the Local Inflammatory Response and Increase Neuronal Death during Chronic Neurodegeneration (2005, background): “…and other chronic neurodegenerative conditions in that they are typified by the extracellular deposition of insoluble plaques, show neurodegeneration along neuroanatomical pathways , and display marked astrocytosis and microglial activation (DeArmond, 1993; Price et al., 1993; Soto et al., 2003).”
ER stress and neurodegenerative diseases (2006, background): “It is generally thought that the activity of UPS is mitigated in these diseases either by the protein aggregates or by enhanced oxidative stress and other toxic products.(7,8) Dysfunctional UPS in turn cause more accumula-”
Widespread Protein Aggregation as an Inherent Part of Aging in C. elegans (2010, background): “In disease models for aberrant protein aggregation, protein aggregation is characterized by the assembly of the misfolded protein into microscopically visible aggregates [36].”
Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. (2005, background): “It is important to identify such regions, as they may represent very favourable targets for therapeutic strategies based on their shielding, for example through competitive binding.(97,98) We define the second type of sensitive regions as aggregation-susceptible, or S regions in which large changes ”
Principles of protein folding, misfolding and aggregation. (2004, neutral): “5, and many show considerable promise [86,99–103].”
Mistranslation-induced protein misfolding as a dominant constraint on coding-sequence evolution (2008, neutral): “Neurodegenerative diseases disproportionately involve protein misfolding and aggregation (Soto, 2003).”