Evidence map›Paper›PMID 18368143›Full record

ReviewMolecular medicine (Cambridge, Mass.)

Protein aggregation in the brain: the molecular basis for Alzheimer's and Parkinson's diseases.

G Brent Irvine, Omar M El-Agnaf, Ganesh M Shankar, Dominic M Walsh

Open access · goldAbstract readReview
In one paragraph

Review in Molecular medicine (Cambridge, Mass.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 230 papers.

0numbers the graph read from it
0cells of the map it votes in
230citing papers in PubMed
14.7field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

230 citing papers in PubMed, 545 citations in OpenAlex.

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  3. Elevated NaInternational journal of molecular sciences · 2026
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  6. Elevated NabioRxiv : the preprint server for biology · 2025
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  14. Prion-like Properties of Short Isoforms of Human Chromatin Modifier PHC3.International journal of molecular sciences · 2025
    Article
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170 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 4 countries.

G Brent IrvineSchool of Medicine and Dentistry, The Queen's University of Belfast, Belfast, Northern Ireland. b.irvine@qub.ac.uk
Omar M El-Agnaf
Ganesh M Shankar
Dominic M Walsh
Harvard University · USQueen's University Belfast · GBUnited Arab Emirates University · AE

Funding

Wellcome TrustWellcome Trust 067660
6 · The paper itself

Abstract

Developing effective treatments for neurodegenerative diseases is one of the greatest medical challenges of the 21st century. Although many of these clinical entities have been recognized for more than a hundred years, it is only during the past twenty years that the molecular events that precipitate disease have begun to be understood. Protein aggregation is a common feature of many neurodegenerative diseases, and it is assumed that the aggregation process plays a central role in pathogenesis. In this process, one molecule (monomer) of a soluble protein interacts with other monomers of the same protein to form dimers, oligomers, and polymers. Conformation changes in three-dimensional structure of the protein, especially the formation of beta-strands, often accompany the process. Eventually, as the size of the aggregates increases, they may precipitate as insoluble amyloid fibrils, in which the structure is stabilized by the beta-strands interacting within a beta-sheet. In this review, we discuss this theme as it relates to the two most common neurodegenerative conditions-Alzheimer's and Parkinson's diseases.

Indexed as

alpha-SynucleinAlzheimer DiseaseAmyloid beta-PeptidesBrainHumansIncidenceModels, BiologicalParkinson DiseasePlaque, Amyloidalpha-SynucleinAmyloid beta-Peptides

Identifiers

PMID18368143
PMCPMC2274891
OpenAlexW1582795354

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.