This page is alzhub.org's plain-English summary of a published study, not the paper itself. It is generated from the record we hold for this study, sourced and linked below — check the original for the full text and methods.

41/100

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

Topic: Brain proteins, microglia and lab models

Intraneuronal accumulation of hyperphosphorylated protein tau in paired helical filaments together with amyloid-beta peptide (Abeta) deposits confirm the clinical diagnosis of Alzheimer disease. A common cellular mechanism leading to the production of these potent toxins remains elusive. Here we show that, in cultured neurons, membrane depolarization induced a calcium-mediated transient phosphorylation of both microtubule-associated protein tau and amyloid precursor protein (APP), followed by a dephosphorylation of these proteins.

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

APA 7th

Pierrot, N., Santos, S. F., Feyt, C., Morel, M., Brion, J. P., & Octave, J. N. (2006). Calcium-mediated transient phosphorylation of tau and amyloid precursor protein followed by intraneuronal amyloid-beta accumulation. The Journal of biological chemistry. https://doi.org/10.1074/jbc.m606015200

Vancouver

Pierrot N, Santos SF, Feyt C, Morel M, Brion JP, Octave JN. Calcium-mediated transient phosphorylation of tau and amyloid precursor protein followed by intraneuronal amyloid-beta accumulation. The Journal of biological chemistry. 2006. doi:10.1074/jbc.m606015200. PMID: 17085446.

BibTeX

@article{pierrot2006-17085446,
  author  = {Pierrot, N. and Santos, S. F. and Feyt, C. and Morel, M. and Brion, J. P. and Octave, J. N.},
  title   = {{Calcium-mediated transient phosphorylation of tau and amyloid precursor protein followed by intraneuronal amyloid-beta accumulation}},
  journal = {The Journal of biological chemistry},
  year    = {2006},
  doi     = {10.1074/jbc.m606015200},
  pmid    = {17085446},
  url     = {https://doi.org/10.1074/jbc.m606015200}
}

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

A common cellular mechanism leading to the production of these potent toxins remains elusive.
Here we show that, in cultured neurons, membrane depolarization induced a calcium-mediated transient phosphorylation of both microtubule-associated protein tau and amyloid precursor protein (APP), followed by a dephosphorylation of these proteins.
Phosphorylation was mediated by glycogen synthase kinase 3 and cyclin-dependent kinase 5 protein kinases, while calcineurin was responsible for dephosphorylation.
Following the transient phosphorylation of APP, intraneuronal Abeta accumulated and induced neurotoxicity.

Why it matters

In cultured neurons, membrane depolarization caused a calcium-mediated transient phosphorylation of tau and APP, followed by dephosphorylation. This is a laboratory cell study and does not demonstrate any treatment, cure, or prevention for Alzheimer's disease.

New to this subject? Start with our plain-English guide: Genetics →

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	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)
Randomized / blinded	0 / 2	No randomization or blinding stated — scores zero (not stated in the record — scored 0)
Times cited	5 / 7	Cited 121 times (OpenAlex, 2026-10-10)
Citations per year	2 / 5	5.5 citations a year over 22 year(s) since 2006
Impact for its field and year	3 / 6	Cited 4.5× the average for papers of its field and year (OpenAlex FWCI)
Cited by studies here	1 / 6	Cited by 2 other studies in this library
Still being cited	2 / 4	Cited 15 times in 2024–2026 (2026 still in progress; OpenAlex)
Senior author's track record	1 / 4	Last-listed author Jean Noël Octave: h-index 18 (OpenAlex, whole career)
Institution's track record	1 / 3	Université Libre de Bruxelles: institution h-index 904 (OpenAlex)
Multicenter collaboration	1 / 3	OpenAlex lists 2 institution(s) in 1 country
Indexed in PubMed	2 / 2	Indexed in PubMed (PMID 17085446)
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 →

Read the original

Full text: free to read — OpenAlex lists this copy as free to read: the link above (checked 6 Feb 1020).

Studies in the library that share something with this one. The line above each title says what.

Studies this one cites

Referenced by this study and also in the alzhub library, so you can read them here.

Later studies that cite this one

2 studies in the alzhub library list this one in their references.

Related studies in Risk genes beyond APOE

Also tagged “phosphorylated”

732 studies in the library carry the topic tag “phosphorylated”; these are this study's neighbours in a fixed, alphabetical-by-hash tour of them, not the closest in content. All 732 tagged studies.

Studies sharing this one's topic tags

Similar studies

More on Risk genes beyond APOE

See all studies in Risk genes beyond APOE →