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Amyloid precursor protein-mediated free radicals and oxidative damage: implications for the development and progression of Alzheimer's disease
Reddy PH.. Journal of neurochemistry, 2005-11-23
Topic: Amyloid, tau and blood-test diagnosis
Alzheimer's disease (AD) is a late-onset dementia that is characterized by the loss of memory and an impairment of multiple cognitive functions. Advancements in molecular, cellular, and animal model studies have revealed that the formation of amyloid beta (Abeta) and other derivatives of the amyloid precursor protein (APP) are key factors in cellular changes in the AD brain, including the generation of free radicals, oxidative damage, and inflammation. Recent molecular, cellular, and gene expression studies have revealed that Abeta enters mitochondria, induces the generation of free radicals, and leads to oxidative damage in post-mortem brain neurons from AD patients and in brain neurons from cell models and transgenic mouse models of AD.
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
Reddy, P. H. (2006). Amyloid precursor protein-mediated free radicals and oxidative damage: implications for the development and progression of Alzheimer's disease. Journal of neurochemistry. https://doi.org/10.1111/j.1471-4159.2005.03530.x
Vancouver
Reddy PH. Amyloid precursor protein-mediated free radicals and oxidative damage: implications for the development and progression of Alzheimer's disease. Journal of neurochemistry. 2006. doi:10.1111/j.1471-4159.2005.03530.x. PMID: 16305625.
BibTeX
@article{reddy2006-16305625,
author = {Reddy, P. H.},
title = {{Amyloid precursor protein-mediated free radicals and oxidative damage: implications for the development and progression of Alzheimer's disease}},
journal = {Journal of neurochemistry},
year = {2006},
doi = {10.1111/j.1471-4159.2005.03530.x},
pmid = {16305625},
url = {https://doi.org/10.1111/j.1471-4159.2005.03530.x}
}
Built from the record alzhub holds for this paper, not looked up. Volume, issue and page numbers are not held in the record. Check the citation against the original before you use it.
Key findings
- Advancements in molecular, cellular, and animal model studies have revealed that the formation of amyloid beta (Abeta) and other derivatives of the amyloid precursor protein (APP) are key factors in cellular changes in the AD brain, including the generation of free radicals, oxidative damage, and inflammation.
- Recent molecular, cellular, and gene expression studies have revealed that Abeta enters mitochondria, induces the generation of free radicals, and leads to oxidative damage in post-mortem brain neurons from AD patients and in brain neurons from cell models and transgenic mouse models of AD.
- In the last three decades, tremendous progress has been made in mitochondrial research and has provided significant findings to link mitochondrial oxidative damage and neurodegenerative diseases such as AD.
- Researchers in the AD field are beginning to recognize the possible involvement of a mutant APP and its derivatives in causing mitochondrial oxidative damage in AD.
Why it matters
This paper reviews evidence from cell and animal models that amyloid beta and other amyloid precursor protein derivatives enter mitochondria, generate free radicals, and cause oxidative damage in Alzheimer's disease. It is a review of laboratory findings, not a clinical trial, so it does not show that any treatment targeting these processes works in patients.
Study details
- Evidence strengthLow
How this study scored 45/100
Published in a peer-reviewed journal. Scored zero for study design, sample size, effect reported, studied in people and randomised / blinded because the record does not state it.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (Journal of neurochemistry) |
| Journal's citation record | 3 / 4 | Journal of Neurochemistry: journal h-index 349 (OpenAlex, 2026-10-29) |
| Study design | 0 / 12 | No study design recorded — scores zero, not guessed (not stated in the record — scored 0) |
| Strength of evidence | 1 / 5 | Rated “low” in our summary |
| Peer-review validation | 10 / 10 | Peer-reviewed. Published as an article in a named peer-reviewed journal. |
| How recent | 1 / 5 | 2006 — older than 20 years, still counted |
| Sample size | 0 / 4 | Participant count not stated — scores zero (not stated in the record — scored 0) |
| Effect reported | 0 / 3 | No effect size reported — scores zero (not stated in the record — scored 0) |
| Studied in people | 0 / 3 | Not stated whether this was studied in people — scores zero (not stated in the record — scored 0) |
| Randomised / blinded | 0 / 2 | No randomisation or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 6 / 7 | Cited 358 times (OpenAlex, 2026-10-10) |
| Citations per year | 3 / 5 | 16.3 citations a year over 22 year(s) since 2006 |
| Impact for its field and year | 4 / 6 | Cited 11.7× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 2 / 6 | Cited by 4 other studies in this library |
| Still being cited | 2 / 4 | Cited 23 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 3 / 4 | Last-listed author P. Hemachandra Reddy: h-index 97 (OpenAlex, whole career) |
| Institution's track record | 1 / 3 | Oregon Health & Science University: institution h-index 1,025 (OpenAlex) |
| Multi-centre collaboration | 0 / 3 | OpenAlex lists 1 institution(s) in 1 country — scores zero (affiliation lists can be incomplete) |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 16305625) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 45 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
- DOI: 10.1111/j.1471-4159.2005.03530.x
- PubMed: 16305625
- Original source →
- Free full text: Journal of Neurochemistry →
Full text: free to read — OpenAlex lists this copy as free to read: the link above (checked 6 Feb 1020).
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