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41/100

✓ Peer-reviewed alzhub usefulness score 41 out of 100. Risk genes beyond APOE

Topic: Brain proteins, microglia and lab models

Plain-language summary

Alzheimer disease (AD) is neuropathologically characterized by the formation of senile plaques from amyloid-β (Aβ) and neurofibrillary tangles composed of phosphorylated Tau. Although there is growing evidence for the pathogenic role of soluble Aβ species in AD, the major question of how Aβ induces hyperphosphorylation of Tau remains unanswered. To address this question, we here developed a novel cell coculture system to assess the effect of extracellular Aβ at physiologically relevant levels naturally secreted from donor cells on the phosphorylation of Tau in recipient cells.

What this study adds

Evidence grade: Low

In a cell coculture system, naturally secreted amyloid-beta at physiologically relevant levels induced hyperphosphorylation of Tau, and this was modulated by insulin-dependent Akt-GSK3beta signaling. This is laboratory cell work, so it does not yet show whether targeting this pathway can treat or prevent Alzheimer's disease in people.

Taken from this record’s own fields, not from reading the paper. The grade is assigned from the abstract’s wording; what that means.

Cite this study APA, Vancouver, BibTeX · download .bib or .ris

APA 7th

Tokutake, T., Kasuga, K., Yajima, R., Sekine, Y., Tezuka, T., Nishizawa, M., et al. (2012). Hyperphosphorylation of Tau induced by naturally secreted amyloid-β at nanomolar concentrations is modulated by insulin-dependent Akt-GSK3β signaling pathway. The Journal of biological chemistry. https://doi.org/10.1074/jbc.m112.348300

Vancouver

Tokutake T, Kasuga K, Yajima R, Sekine Y, Tezuka T, Nishizawa M, et al. Hyperphosphorylation of Tau induced by naturally secreted amyloid-β at nanomolar concentrations is modulated by insulin-dependent Akt-GSK3β signaling pathway. The Journal of biological chemistry. 2012. doi:10.1074/jbc.m112.348300. PMID: 22910909.

BibTeX

@article{tokutake2012-22910909,
  author  = {Tokutake, T. and Kasuga, K. and Yajima, R. and Sekine, Y. and Tezuka, T. and Nishizawa, M. and Ikeuchi, T.},
  title   = {{Hyperphosphorylation of Tau induced by naturally secreted amyloid-β at nanomolar concentrations is modulated by insulin-dependent Akt-GSK3β signaling pathway}},
  journal = {The Journal of biological chemistry},
  year    = {2012},
  doi     = {10.1074/jbc.m112.348300},
  pmid    = {22910909},
  url     = {https://doi.org/10.1074/jbc.m112.348300}
}

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.

How to read this study

Design: our record does not state a study design, so check the methods section of the original before weighing the result.
Size: the record gives no participant count. Look for one in the original before trusting a pattern.
Effect: the record gives no effect size, so the summary above cannot say how large any difference was.

What the evidence grade means here

This page is graded low. alzhub.org assigns the grade automatically from keywords in the abstract, not from reading the paper. Low means the abstract matched neither pattern. It is the default label, and it does not mean the work is poor; many sound lab and imaging papers land here. It can add at most 5 of the 100 points in the study score, and it is a label about design, not a verdict on whether the findings are true.

New to reading papers? Six questions to ask of any Alzheimer’s study · how we score.

Key findings

Although there is growing evidence for the pathogenic role of soluble Aβ species in AD, the major question of how Aβ induces hyperphosphorylation of Tau remains unanswered.
To address this question, we here developed a novel cell coculture system to assess the effect of extracellular Aβ at physiologically relevant levels naturally secreted from donor cells on the phosphorylation of Tau in recipient cells.
Using this assay, we demonstrated that physiologically relevant levels of secreted Aβ are sufficient to cause hyperphosphorylation of Tau in recipient N2a cells expressing human Tau and in primary culture neurons.
This hyperphosphorylation of Tau is inhibited by blocking Aβ production in donor cells.

Why it matters

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Study details

Evidence strengthLow

How this study scored 41/100

Published in a peer-reviewed journal. Scored zero for study design, sample size, effect reported, studied in people and randomized / blinded because the record does not state it.

Component	Points	Why
Journal tier	7 / 10	Tier 3 — peer-reviewed journal (The Journal of biological chemistry)
Journal's citation record	4 / 4	Journal of Biological Chemistry: journal h-index 780 (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	2012 — within 20 year(s) of the newest study here
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)
Randomized / blinded	0 / 2	No randomization or blinding stated — scores zero (not stated in the record — scored 0)
Times cited	5 / 7	Cited 117 times (OpenAlex, 2026-10-10)
Citations per year	2 / 5	7.3 citations a year over 16 year(s) since 2012
Impact for its field and year	3 / 6	Cited 6.1× 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	2 / 4	Cited 26 times in 2024–2026 (2026 still in progress; OpenAlex)
Senior author's track record	3 / 4	Last-listed author Takeshi Ikeuchi: h-index 64 (OpenAlex, whole career)
Institution's track record	0 / 3	Niigata University: institution h-index 473 (OpenAlex)
Multicenter 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 22910909)
Free to read	0 / 2	Behind a paywall — scores zero
Total	41 / 100	—

What each of these 20 components measures, and what this score is not →

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