ReviewCurrent opinion in structural biology2019
Cryo-EM of amyloid fibrils and cellular aggregates.
Review in Current opinion in structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
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
74 citing papers in PubMed, 133 citations in OpenAlex.
- From Disordered to Ordered: Nanoscale Spectroscopy Reveals Structural Evolution of Amyloid Beta 40 Fibrils.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Endogenous Aβ and Exogenous Wheat Gluten Nanostructures: Understanding Peptide Self-Assembly in Disease.ACS nano · 2025Review
- Cryo-EM for atomic characterization of supramolecular gels.Faraday discussions · 2025Article
- Lipid mediated formation of antiparallel aggregates in cerebral amyloid angiopathy.Acta neuropathologica · 2025Article
- Guide to the structural characterization of protein aggregates and amyloid fibrils by CD spectroscopy.Protein science : a publication of the Protein Society · 2025Article
- Amyloids in bladder cancer hijack cancer-related proteins and are positive correlated to tumor stage.Scientific reports · 2025Article
- Integrative determination of atomic structure of mutant huntingtin exon 1 fibrils implicated in Huntington disease.Nature communications · 2024Article
- Proteomic Evidence for Amyloidogenic Cross-Seeding in Fibrinaloid Microclots.International journal of molecular sciences · 2024Article
- Integrative determination of the atomic structure of mutant huntingtin exon 1 fibrils implicated in Huntington's disease.bioRxiv : the preprint server for biology · 2024Article
- Heterotypic Seeding Generates Mixed Amyloid Polymorphs.Small science · 2024Article
- Article
- Screening Carbon Nano Materials for Preventing Amyloid Protein Aggregation by Adopting a Facile Method.Cell biochemistry and biophysics · 2024Article
- Impact of distinct FG nucleoporin repeats on Nup98 self-association.Nature communications · 2024Article
- Solid-state nuclear magnetic resonance in the structural study of polyglutamine aggregation.Biochemical Society transactions · 2024Review
- Review
- Peptide Self-Assembly into Amyloid Fibrils: Unbiased All-Atom Simulations.The journal of physical chemistry. B · 2024Review
- An overview on glycation: molecular mechanisms, impact on proteins, pathogenesis, and inhibition.Biophysical reviews · 2024Review
- Lung endothelium, tau, and amyloids in health and disease.Physiological reviews · 2024Review
- Screening Carbon Nano Materials for preventing amyloid protein aggregation by adopting a facile method.Research square · 2024Article
- Improving cryo-EM grids for amyloid fibrils using interface-active solutions and spectator proteins.Biophysical journal · 2024Article
14 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Neurodegenerative and other protein misfolding diseases are associated with the aggregation of a protein, which may be mutated in genetic forms of disease, or the wild type form in late onset sporadic disease. A wide variety of proteins and peptides can be involved, with aggregation originating from a natively folded or a natively unstructured species. Large deposits of amyloid fibrils are typically associated with cell death in late stage pathology. In this review, we illustrate the contributions of cryo-EM and related methods to the structure determination of amyloid fibrils extracted post mortem from patient brains or formed in vitro. We also discuss cell models of protein aggregation and the contributions of electron tomography to understanding the cellular context of aggregation.
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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.