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42/100

✓ Peer-reviewed alzhub usefulness score 42 out of 100. Disease mechanisms

Topic: Brain proteins, microglia and lab models

Plain-language summary

A wide range of human diseases are associated with protein misfolding and amyloid aggregates. Recent studies suggest that in certain neurological disorders, including Amyotrophic Lateral Sclerosis (ALS), Frontotemporal Dementia (FTD) and various tauopathies, protein aggregation may be promoted by virus-like particles (VLPs) formed by endogenous retroviruses (ERVs). The molecular mechanisms by which these VLPs contribute to protein aggregation, however, remain enigmatic. Here, we discuss possible molecular mechanisms of ERV-derived VLPs in the formation and spread of protein aggregates. An intriguing possibility is that liquid-like condensates may facilitate the formation of both protein aggregates and ERV-derived VLPs. We also describe how RNA chaperoning, and the encapsulation and trafficking of misfolded proteins, may contribute to protein homeostasis through the elimination of protein aggregates from cells. Based on these insights, we discuss future potential therapeutic opportunities.

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

APA 7th

Carra, S., Fábián, B., Taghavi, H. V., Milanetti, E., Giliberti, V., Ruocco, G., et al. (2025). Virus-like particles of retroviral origin in protein aggregation and neurodegenerative diseases. Molecular Aspects of Medicine. https://doi.org/10.1016/j.mam.2025.101369

Vancouver

Carra S, Fábián B, Taghavi HV, Milanetti E, Giliberti V, Ruocco G, et al. Virus-like particles of retroviral origin in protein aggregation and neurodegenerative diseases. Molecular Aspects of Medicine. 2025. doi:10.1016/j.mam.2025.101369. PMID: 40398193.

BibTeX

@article{carra2025-40398193,
  author  = {Carra, Serena and Fábián, Balázs and Taghavi, Hamed Vaez and Milanetti, Edoardo and Giliberti, Valeria and Ruocco, Giancarlo and Shepherd, Jason D. and Vendruscolo, Michele and others},
  title   = {{Virus-like particles of retroviral origin in protein aggregation and neurodegenerative diseases}},
  journal = {Molecular Aspects of Medicine},
  year    = {2025},
  doi     = {10.1016/j.mam.2025.101369},
  pmid    = {40398193},
  url     = {https://doi.org/10.1016/j.mam.2025.101369}
}

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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.

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Key findings

A wide range of human diseases are associated with protein misfolding and amyloid aggregates.
Recent studies suggest that in certain neurological disorders, including Amyotrophic Lateral Sclerosis (ALS), Frontotemporal Dementia (FTD) and various tauopathies, protein aggregation may be promoted by virus-like particles (VLPs) formed by endogenous retroviruses (ERVs).

Why it matters

This discussion paper proposes possible molecular mechanisms by which virus-like particles from endogenous retroviruses might promote protein aggregation in conditions such as ALS, FTD and tauopathies. It is a theoretical review that only discusses future potential therapeutic opportunities, with no tested treatment.

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 randomized / blinded because the record does not state it.

Component	Points	Why
Journal tier	7 / 10	Tier 3 — peer-reviewed journal (Molecular Aspects of Medicine)
Journal's citation record	2 / 4	Molecular Aspects of Medicine: journal h-index 195 (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	4 / 5	2025 — within 3 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	2 / 7	Cited 7 times (OpenAlex, 2026-10-10)
Citations per year	1 / 5	2.3 citations a year over 3 year(s) since 2025
Impact for its field and year	3 / 6	Cited 3.8× the average for papers of its field and year (OpenAlex FWCI)
Cited by studies here	0 / 6	No other study in this library cites it
Still being cited	1 / 4	Cited 7 times in 2024–2026 (2026 still in progress; OpenAlex)
Senior author's track record	3 / 4	Last-listed author Mónika Fuxreiter: h-index 51 (OpenAlex, whole career)
Institution's track record	2 / 3	University of Cambridge: institution h-index 1,973 (OpenAlex)
Multicenter collaboration	2 / 3	OpenAlex lists 7 institution(s) in 4 countries
Indexed in PubMed	2 / 2	Indexed in PubMed (PMID 40398193)
Free to read	2 / 2	Free to read
Total	42 / 100	—

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

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