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Do axonal defects in tau and amyloid precursor protein transgenic animals model axonopathy in Alzheimer's disease?
Götz J, Ittner LM, Kins S.. Journal of neurochemistry, 2006-06-19
Topic: Brain proteins, microglia and lab models
The subcellular localization of organelles, mRNAs and proteins is particularly challenging in neurons. Owing to their extended morphology, with axons in humans exceeding a meter in length, in addition to which they are not renewed but persist for the entire lifespan, it is no surprise that neurons are highly vulnerable to any perturbation of their sophisticated transport machinery. There is emerging evidence that impaired transport is not only causative for a range of motor disorders, but possibly also for Alzheimer's disease (AD) and related neurodegenerative disorders.
Key findings
- Owing to their extended morphology, with axons in humans exceeding a meter in length, in addition to which they are not renewed but persist for the entire lifespan, it is no surprise that neurons are highly vulnerable to any perturbation of their sophisticated transport machinery.
- There is emerging evidence that impaired transport is not only causative for a range of motor disorders, but possibly also for Alzheimer's disease (AD) and related neurodegenerative disorders.
- Support for this hypothesis comes from transgenic animal models.
- Overexpression of human tau and amyloid precursor protein (APP) in mice and flies models the key hallmark histopathological characteristics of AD, such as somatodendritic accumulation of phosphorylated forms of tau and beta-amyloid (Abeta) peptide-containing amyloid plaques, as well as axonopathy.
Why it matters
This review discusses whether axonal defects in tau and amyloid precursor protein transgenic animals model axonopathy in Alzheimer's disease. It does not report any treatment, cure, or prevention for Alzheimer's disease.
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Study details
- Evidence strengthLow
How this study scored 39/100
Published in a peer-reviewed journal. Scored zero for study design, sample size, effect reported 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 | Laboratory or animal study (title names “transgenic”) — scores zero |
| Randomised / blinded | 0 / 2 | No randomisation or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 5 / 7 | Cited 115 times (OpenAlex, 2026-10-10) |
| Citations per year | 2 / 5 | 5.2 citations a year over 22 year(s) since 2006 |
| Impact for its field and year | 3 / 6 | Cited 5.9× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 1 / 6 | Cited by 1 other studies in this library |
| Still being cited | 0 / 4 | Cited 1 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 2 / 4 | Last-listed author Stefan Kins: h-index 34 (OpenAlex, whole career) |
| Institution's track record | 1 / 3 | The University of Sydney: institution h-index 1,466 (OpenAlex) |
| Multi-centre collaboration | 1 / 3 | OpenAlex lists 2 institution(s) in 2 countries |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 16787410) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 39 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
- DOI: 10.1111/j.1471-4159.2006.03955.x
- PubMed: 16787410
- 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).
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
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.
APA 7th
Götz, J., Ittner, L. M., & Kins, S. (2006). Do axonal defects in tau and amyloid precursor protein transgenic animals model axonopathy in Alzheimer's disease? Journal of neurochemistry. https://doi.org/10.1111/j.1471-4159.2006.03955.x
Vancouver
Götz J, Ittner LM, Kins S. Do axonal defects in tau and amyloid precursor protein transgenic animals model axonopathy in Alzheimer's disease? Journal of neurochemistry. 2006. doi:10.1111/j.1471-4159.2006.03955.x. PMID: 16787410.
BibTeX
@article{gotz2006-16787410,
author = {Götz, J. and Ittner, L. M. and Kins, S.},
title = {{Do axonal defects in tau and amyloid precursor protein transgenic animals model axonopathy in Alzheimer's disease?}},
journal = {Journal of neurochemistry},
year = {2006},
doi = {10.1111/j.1471-4159.2006.03955.x},
pmid = {16787410},
url = {https://doi.org/10.1111/j.1471-4159.2006.03955.x}
}
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