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.

47/100

✓ Peer-reviewed alzhub usefulness score 47 out of 100. Risk genes beyond APOE

Topic: Brain proteins, microglia and lab models

Oxidative stress is closely linked to the pathogenesis of neurodegeneration. Soluble amyloid β (Aβ) oligomers cause cognitive impairment and synaptic dysfunction in Alzheimer disease (AD). However, the relationship between oligomers, oxidative stress, and their localization during disease progression is uncertain.

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

APA 7th

Murakami, K., Murata, N., Noda, Y., Tahara, S., Kaneko, T., Kinoshita, N., et al. (2011). SOD1 (copper/zinc superoxide dismutase) deficiency drives amyloid β protein oligomerization and memory loss in mouse model of Alzheimer disease. The Journal of biological chemistry. https://doi.org/10.1074/jbc.m111.279208

Vancouver

Murakami K, Murata N, Noda Y, Tahara S, Kaneko T, Kinoshita N, et al. SOD1 (copper/zinc superoxide dismutase) deficiency drives amyloid β protein oligomerization and memory loss in mouse model of Alzheimer disease. The Journal of biological chemistry. 2011. doi:10.1074/jbc.m111.279208. PMID: 22072713.

BibTeX

@article{murakami2011-22072713,
  author  = {Murakami, K. and Murata, N. and Noda, Y. and Tahara, S. and Kaneko, T. and Kinoshita, N. and Hatsuta, H. and Murayama, S. and others},
  title   = {{SOD1 (copper/zinc superoxide dismutase) deficiency drives amyloid β protein oligomerization and memory loss in mouse model of Alzheimer disease}},
  journal = {The Journal of biological chemistry},
  year    = {2011},
  doi     = {10.1074/jbc.m111.279208},
  pmid    = {22072713},
  url     = {https://doi.org/10.1074/jbc.m111.279208}
}

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's author list ends in “et al.”, so not every author is named. Check the citation against the original before you use it.

Key findings

Soluble amyloid β (Aβ) oligomers cause cognitive impairment and synaptic dysfunction in Alzheimer disease (AD).
However, the relationship between oligomers, oxidative stress, and their localization during disease progression is uncertain.
Our previous study demonstrated that mice deficient in cytoplasmic copper/zinc superoxide dismutase (CuZn-SOD, SOD1) have features of drusen formation, a hallmark of age-related macular degeneration (Imamura, Y., Noda, S., Hashizume, K., Shinoda, K., Yamaguchi, M., Uchiyama, S., Shimizu, T., Mizushima, Y., Shirasawa, T., and Tsubota, K.
Amyloid assembly has been implicated as a common mechanism of plaque and drusen formation.

Why it matters

In a mouse model, deficiency of the antioxidant enzyme SOD1 drove amyloid beta oligomerization and memory loss. This is an animal study and does not show that targeting oxidative stress treats or prevents Alzheimer's disease in people.

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

Study details

Evidence strengthLow

How this study scored 47/100

Published in a peer-reviewed journal. Scored zero for study design, sample size, effect reported 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	2011 — 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	Laboratory or animal study (title names “mouse”) — scores zero
Randomized / blinded	0 / 2	No randomization or blinding stated — scores zero (not stated in the record — scored 0)
Times cited	5 / 7	Cited 243 times (OpenAlex, 2026-10-10)
Citations per year	3 / 5	14.3 citations a year over 17 year(s) since 2011
Impact for its field and year	4 / 6	Cited 11.0× the average for papers of its field and year (OpenAlex FWCI)
Cited by studies here	2 / 6	Cited by 3 other studies in this library
Still being cited	2 / 4	Cited 31 times in 2024–2026 (2026 still in progress; OpenAlex)
Senior author's track record	3 / 4	Last-listed author Takahiko Shimizu: h-index 53 (OpenAlex, whole career)
Institution's track record	1 / 3	The University of Melbourne: institution h-index 1,342 (OpenAlex)
Multicenter collaboration	2 / 3	OpenAlex lists 5 institution(s) in 2 countries
Indexed in PubMed	2 / 2	Indexed in PubMed (PMID 22072713)
Free to read	0 / 2	Behind a paywall — scores zero
Total	47 / 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

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

Related studies in Risk genes beyond APOE from nearby years

Also tagged “tdp-43”

1,150 studies in the library carry the topic tag “tdp-43”; these are this study's neighbours in a fixed, alphabetical-by-hash tour of them, not the closest in content. All 1,150 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 →