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forms
6 studies tagged forms, dated 2011-06-01 to 2020-12-01. Bibliography: BibTeX (.bib) · RIS (.ris)
Newest in this topic
- Alzheimer's Aβ42 and Aβ40 form mixed oligomers with direct molecular interactions 2020-12-01
- CSF biomarkers of neuroinflammation in distinct forms and subtypes of neurodegenerative dementia 2019-12-31
- Evaluation of the Expression of Amyloid Precursor Protein and the Ratio of Secreted Amyloid Beta 42 to Amyloid Beta 40 in SH-SY5Y Cells Stably Transfected with Wild-Type, Single-Mutant and Double-Mutant Forms of the APP Gene for the Study of Alzheimer's Disease Pathology 2017-04-17
Studies
6 studies carry this tag.
Date range
2011 to 2020
Top journals
- Alzheimer's research & therapy 1
- Annals of neurology 1
- Applied biochemistry and biotechnology 1
- Biochemical and biophysical research communications 1
- Journal of peptide science : an official publication of the European Peptide Society 1
6 journals in all.
Newest first, then by address. Each study has a usefulness score out of 100 (rubric version 4.0); tap a score to see what makes it up. Tags were assigned automatically from each study's title and summary. The same studies as a filter in the library.
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Formation of Aβ oligomers and fibrils plays a central role in the pathogenesis of Alzheimer's disease.
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51/100
NDs share a CSF profile characterized by increased levels of CSF CHIT1, YKL-40, and GFAP, which likely reflects a common neuroinflammatory response to protein misfolding and aggregation.
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Neuroblastoma cell lines such as SH-SY5Y are the most frequently utilized models in neurodegenerative research, and their use has advanced the understanding of the pathology of neurodegeneration over the past few decades.
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38/100
The abnormal deposition of amyloid-β (Aβ) peptides in the brain is the main neuropathological hallmark of Alzheimer's disease (AD).
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Fibrillar amyloid-β (Aβ) is the major constituent of senile plaques in the brain of patients with Alzheimer's disease (AD).
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These results suggest that some SAD may involve alternative processing of multiple γ-secretase substrates, raising the possibility that the molecular pathogenesis of SAD might involve γ-secretase dysfunction.