Cell biology of protein misfolding: The examples of Alzheimer's and Parkinson's diseases
By D. Selkoe. Nature Cell Biology, 2004
894 citations recorded by the source corpus.
Subfields: Cell Biology, Neurology, Physiology
View Paper: https://www.semanticscholar.org/paper/55f0f716a355adc7e29593bf650590b1a5a552b5
How researchers see this paper
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In Cell Biology
In Neurology
- Kaj Blennow
- Henrik Zetterberg
- Oskar Hansson
- Philip Scheltens
- Birgit Liss
- Jochen Roeper
- Markus R. Wenk
- Dag Aarsland
In Physiology
- Henrik Zetterberg
- Kaj Blennow
- Oskar Hansson
- D. Sinclair
- Harald Hampel
- Joseph A. Baur
- Lennart Minthon
- Philip Scheltens
Citations in the corpus
- Hereditary parkinsonism with dementia is caused by mutations in ATP13A2, encoding a lysosomal type 5 P-type ATPase (2006, background): “This has led to the discovery of common pathophysiological pathways such as enhanced oxidative stress, protein misfolding and aggregation and dysfunction of the ubiquitin-proteasome syste”
- AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides (2007, neutral): “Actually, Tau is an usually highly soluble microtubule-associated protein [28] but in Alzheimer's disease it aggregates into fibres with a tendency to form neurofibrillary tangles.”
- SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis (2007, background): “…neurodegenera- tion raises the possibility of developing a class of therapeutic interventions that treat a variety of neurological disorders by activating the body’s own defenses against age-related dete- rioration and cell death (Bossy-Wetzel et al, 2004; Forman et al, 2004; Selkoe, 2004).”
- Alzheimer’s disease: pathogenesis, diagnostics, and therapeutics (2019, background): “which is soluble and translocates to nuclei for further geneexpression function.(5)”
- CSF biomarkers and incipient Alzheimer disease in patients with mild cognitive impairment. (2009, methodology): “A 142 levels were determined using a sandwich ELISA (Innotest -amyloid[1-42]), specifically constructed to measure A containing both the 1st and 42nd amino acids, as previously described.”
- The emerging field of lipidomics (2005, background): “A common mechanistic explanation for many of the above disorders is imbalanced protein–protein and protein–lipid interactions, both of which lead to an increased probability of the formation of (intracellular) protein deposit”
- Rho kinase, a promising drug target for neurological disorders (2005, background): “In addition, significant correlations in humans have been reported between levels of soluble Aβ42, the formation of small aggregates (oligomers) and the extent of cognitive impairmen”