ArticleJournal of molecular biology2026
Brain-seeded 42-residue Amyloid-β Fibrils That Resemble Fibrils Directly Extracted From Alzheimer's Disease Brain Tissue.
Article in Journal of molecular biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Fibrils formed by the 42-residue amyloid-β peptide (Aβ42) are known to be polymorphic, with molecular conformations and supramolecular structures that depend on conditions of nucleation, growth, seeding, or other factors. Structural studies of Aβ42 fibrils that develop in human brain tissue have been based on two different approaches, either direct extraction and partial purification of fibrils from brain tissue for characterization by cryogenic electron microscopy (cryo-EM) or growth of fibrils in vitro from seeds in amyloid-containing brain tissue extracts for characterization by solid state nuclear magnetic resonance (ssNMR) or cryo-EM. To date, studies of brain-extracted and brain-seeded Aβ42 fibrils have produced qualitatively different sets of structures. Here we report structures of two new brain-seeded Aβ42 fibril polymorphs, derived from cortical tissue of an Alzheimer's disease (AD) patient, that share certain structural features with previously characterized polymorphs extracted from AD brain tissue. These structures contribute to our understanding of the relationships between brain-seeded and brain-extracted fibril structures and expand our understanding of the full range of polymorphism in amyloid-β fibrils.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.