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Proteins that mediate protein aggregation and cytotoxicity distinguish Alzheimer's hippocampus from normal controls
Ayyadevara S, Balasubramaniam M, Parcon PA, Barger SW, Griffin WS, Alla R, Tackett AJ, Mackintosh SG et al.. Aging cell, 2016-07-23
Topic: Amyloid, tau and blood-test diagnosis
Neurodegenerative diseases are distinguished by characteristic protein aggregates initiated by disease-specific 'seed' proteins; however, roles of other co-aggregated proteins remain largely unexplored. Compact hippocampal aggregates were purified from Alzheimer's and control-subject pools using magnetic-bead immunoaffinity pulldowns. Their components were fractionated by electrophoretic mobility and analyzed by high-resolution proteomics.
Key findings
- Compact hippocampal aggregates were purified from Alzheimer's and control-subject pools using magnetic-bead immunoaffinity pulldowns.
- Their components were fractionated by electrophoretic mobility and analyzed by high-resolution proteomics.
- Although total detergent-insoluble aggregates from Alzheimer's and controls had similar protein content, within the fractions isolated by tau or Aβ1-42 pulldown, the protein constituents of Alzheimer-derived aggregates were more abundant, diverse, and post-translationally modified than those from controls.
- Tau- and Aβ-containing aggregates were distinguished by multiple components, and yet shared >90% of their protein constituents, implying similar accretion mechanisms.
Why it matters
This study purified hippocampal protein aggregates from Alzheimer's and control brains and analyzed their components by proteomics. It is basic laboratory research on protein aggregation and does not test any treatment, cure, or prevention.
New to this subject? Start with our plain-English guide: Blood tests & biomarkers →
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 randomised / blinded because the record does not state it.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (Aging cell) |
| Journal's citation record | 2 / 4 | Aging Cell: journal h-index 216 (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 | 2016 — 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) |
| Randomised / blinded | 0 / 2 | No randomisation or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 4 / 7 | Cited 79 times (OpenAlex, 2026-10-10) |
| Citations per year | 2 / 5 | 6.6 citations a year over 12 year(s) since 2016 |
| Impact for its field and year | 3 / 6 | Cited 4.1× 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 21 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 2 / 4 | Last-listed author Robert J. Shmookler Reis: h-index 44 (OpenAlex, whole career) |
| Institution's track record | 0 / 3 | University of Arkansas for Medical Sciences: institution h-index 591 (OpenAlex) |
| Multi-centre collaboration | 2 / 3 | OpenAlex lists 5 institution(s) in 1 country |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 27448508) |
| Free to read | 2 / 2 | Free to read |
| 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).
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. 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.
APA 7th
Ayyadevara, S., Balasubramaniam, M., Parcon, P. A., Barger, S. W., Griffin, W. S., Alla, R., et al. (2016). Proteins that mediate protein aggregation and cytotoxicity distinguish Alzheimer's hippocampus from normal controls. Aging cell. https://doi.org/10.1111/acel.12501
Vancouver
Ayyadevara S, Balasubramaniam M, Parcon PA, Barger SW, Griffin WS, Alla R, et al. Proteins that mediate protein aggregation and cytotoxicity distinguish Alzheimer's hippocampus from normal controls. Aging cell. 2016. doi:10.1111/acel.12501. PMID: 27448508.
BibTeX
@article{ayyadevara2016-27448508,
author = {Ayyadevara, S. and Balasubramaniam, M. and Parcon, P. A. and Barger, S. W. and Griffin, W. S. and Alla, R. and Tackett, A. J. and Mackintosh, S. G. and others},
title = {{Proteins that mediate protein aggregation and cytotoxicity distinguish Alzheimer's hippocampus from normal controls}},
journal = {Aging cell},
year = {2016},
doi = {10.1111/acel.12501},
pmid = {27448508},
url = {https://doi.org/10.1111/acel.12501}
}
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