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Pin1 in Alzheimer's disease
Butterfield DA, Abdul HM, Opii W, Newman SF, Joshi G, Ansari MA, Sultana R.. Journal of neurochemistry, 2006-09-01
Topic: Amyloid, tau and blood-test diagnosis
Proteolytic processing and phosphorylation of amyloid precursor protein (APP), and hyperphosphorylation of tau protein, have been shown to be increased in Alzheimer's disease (AD) brains, leading to increased production of beta-amyloid (Abeta) peptides and neurofibrillary tangles, respectively. These observations suggest that phosphorylation events are critical to the understanding of the pathogenesis and treatment of this devastating disease. Pin-1, one of the peptidyl-prolyl isomerases (PPIase), catalyzes the isomerization of the peptide bond between pSer/Thr-Pro in proteins, thereby regulating their biological functions which include protein assembly, folding, intracellular transport, intracellular signaling, transcription, cell cycle progression and apoptosis. A number of previous studies have shown that Pin1 is co-localized with phosphorylated tau in AD brain, and shows an inverse relationship to the expression of tau. Pin1 protects neurons under in vitro conditions. Moreover, recent studies demonstrate that APP is a target for Pin1 and thus, in Abeta production. Furthermore, Pin1 was found to be oxidatively modified and to have reduced activity in the hippocampus in mild cognitive impairment (MCI) and AD. Because of the diverse functions of Pin1, and the discovery that this protein is one of the oxidized proteins common to both MCI and AD brain, the question arises as to whether Pin1 is one of the driving forces for the initiation or progression of AD pathogenesis, finally leading to neurodegeneration and neuronal apoptosis. In the present review, we discuss the role of Pin1 with respect to Alzheimer's disease.
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
Butterfield, D. A., Abdul, H. M., Opii, W., Newman, S. F., Joshi, G., Ansari, M. A., et al. (2006). Pin1 in Alzheimer's disease. Journal of neurochemistry. https://doi.org/10.1111/j.1471-4159.2006.03995.x
Vancouver
Butterfield DA, Abdul HM, Opii W, Newman SF, Joshi G, Ansari MA, et al. Pin1 in Alzheimer's disease. Journal of neurochemistry. 2006. doi:10.1111/j.1471-4159.2006.03995.x. PMID: 16945100.
BibTeX
@article{butterfield2006-16945100,
author = {Butterfield, D. A. and Abdul, H. M. and Opii, W. and Newman, S. F. and Joshi, G. and Ansari, M. A. and Sultana, R.},
title = {{Pin1 in Alzheimer's disease}},
journal = {Journal of neurochemistry},
year = {2006},
doi = {10.1111/j.1471-4159.2006.03995.x},
pmid = {16945100},
url = {https://doi.org/10.1111/j.1471-4159.2006.03995.x}
}
Built from the record alzhub holds for this paper, not looked up. Volume, issue and page numbers are not held in the record. The record names 7 authors; APA and Vancouver show the first six, BibTeX and the downloads carry all of them. Check the citation against the original before you use it.
Key findings
- These observations suggest that phosphorylation events are critical to the understanding of the pathogenesis and treatment of this devastating disease.
- A number of previous studies have shown that Pin1 is co-localized with phosphorylated tau in AD brain, and shows an inverse relationship to the expression of tau.
Why it matters
This review discusses the protein Pin1, which is co-localized with phosphorylated tau in Alzheimer's disease brain and shows an inverse relationship to tau expression. It notes that Pin1 protects neurons under in vitro conditions and is oxidatively modified with reduced activity in the hippocampus in mild cognitive impairment and Alzheimer's disease.
Study details
- Evidence strengthLow
How this study scored 42/100
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 | 5 / 7 | Cited 179 times (OpenAlex, 2026-10-10) |
| Citations per year | 3 / 5 | 8.1 citations a year over 22 year(s) since 2006 |
| Impact for its field and year | 3 / 6 | Cited 6.9× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 2 / 6 | Cited by 6 other studies in this library |
| Still being cited | 1 / 4 | Cited 11 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 3 / 4 | Last-listed author Rukhsana Sultana: h-index 82 (OpenAlex, whole career) |
| Institution's track record | 1 / 3 | University of Kentucky: institution h-index 824 (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 16945100) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 42 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
- DOI: 10.1111/j.1471-4159.2006.03995.x
- PubMed: 16945100
- 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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