Toxic Proteins in Neurodegenerative Disease
By J. Taylor, John Hardy, K. Fischbeck. Science, 2002
1,266 citations recorded by the source corpus.
Subfields: Cellular and Molecular Neuroscience, Neurology, Physiology
View Paper: https://www.semanticscholar.org/paper/f117784c140dadd49790df5adb078a76118582bb
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Cellular and Molecular Neuroscience
- D. Rubinsztein
- Fiona M Menzies
- Cahir O'Kane
- Christopher M. Dobson
- S. Alberti
- Tamer A E Ahmed
- Xia Zhang
- Wei-Wei Chen
In Neurology
- D. Rubinsztein
- Fiona M Menzies
- Cahir O'Kane
- Christopher M. Dobson
- S. Alberti
- Arthur W. Toga
- Tamer A E Ahmed
- L. Beckett
In Physiology
- Clifford R. Jack Jr.
- William J. Jagust
- John Q. Trojanowski
- Ronald C. Petersen
- Christopher M. Dobson
- Arthur W. Toga
- Tamer A E Ahmed
- L. Beckett
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”
- Hallmarks of neurodegenerative diseases. (2023, neutral): “1,2,29,39,43 1–”
- Rapamycin alleviates toxicity of different aggregate-prone proteins. (2006, background): “Proteinopathies are a growing family of human disorders associated with the aggregation of misfolded proteins in specific tissues (1).”
- Coupling endoplasmic reticulum stress to the cell death program (2004, background): “residues may permit interaction with a wide range of cellular targets to elicit cellular toxicity.(12,14,39) It is believed that toxicity may arise either due to organelle dysfunction, sequestration of critical factors by the misfolded proteins, inhibition of the”
- Liquid-Liquid Phase Separation in Disease. (2019, background): “A key feature of all neurodegenerative disorders is the regional aggregation of cytosolic or nuclear proteins, which are believed to drive neurodegeneration (145).”
- Role of neuroinflammation in neurodegenerative diseases (Review) (2016, positive): “These neurotoxic mediators are, in general, associated with several neurodegenerative diseases including AD, MS, PD and ALS, which are commonly linked to intracellular mechanisms such as the degradation of protein, the dysfunction of mitochondria, the defects of axonal transport and apoptosis (20-22”
- Human Disease Models in Drosophila melanogaster and the Role of the Fly in Therapeutic Drug Discovery (2011, background): “Many late-onset neurodegenerative diseases, including PD and HD, are associated with the formation of intracellular aggregates of toxic proteins (Taylor et al., 2002).”
- EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers (2008, background): “Amyloid formation is associated with protein-misfolding disorders, including neurodegenerative diseases such as Alzheimer's disease (AD), Parkinson's disease (PD) and Huntington's disease (HD) [ 3 ,4].”