ReviewNature reviews. Molecular cell biology2018
A new era for understanding amyloid structures and disease.
Review in Nature reviews. Molecular cell biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 434 papers, 1 of them a synthesis that pooled 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.
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
434 citing papers in PubMed, 1 synthesis or guideline pooled it, 981 citations in OpenAlex.
- The Role of Gut Microbiota in Pediatric Obesity and Metabolic Disorders: Insights from a Comprehensive Review.Nutrients · 2025Pooled it
- Extracellular vesicles participate in proteostasis and heat shock adaptation inEmerging microbes & infections · 2026Article
- Small molecules rescue pathogenic POLGA aggregation and restore its functions in a mouse model of PEO.EMBO molecular medicine · 2026Article
- Programmable DNA protonuclei reveal environmental context on protein phase separation.Nature communications · 2026Article
- Polyol-Functionalized Manganese-Based Nanoparticles: From Insulin Amyloid Inhibition to Nanozyme-Mediated Antioxidant Activity.International journal of molecular sciences · 2026Article
- Article
- No Significant Secondary Structural Change of α-Synuclein Monomer by Site-Specific DOPA or Phosphorylation Introduction in Its C-Terminal Region.Journal of peptide science : an official publication of the European Peptide Society · 2026Article
- Intratubular light chain amyloidosis: a comprehensive analysis of disease spectrum and clinicopathological characteristics.Clinical kidney journal · 2026Article
- Multipathway Aggregation Drives Concentration-Dependent Amyloid Polymorphism and Time-Dependent Morphological Evolution.The journal of physical chemistry letters · 2026Article
- Modeling Peptides in Aqueous Ionic Liquid Mixtures: A Quantum Mechanics/Molecular Dynamics Study of Structural and NMR Properties.Journal of chemical theory and computation · 2026Article
- Targeting soluble misfolded oligomers in anti-amyloid research.Nature reviews. Chemistry · 2026Review
- A Metabolomics-Based Strategy for Identifying Endogenous Inhibitors of IAPP Aggregation.Metabolites · 2026Article
- Spontaneous aging of mature amyloids alters structural stability, cytotoxicity, and susceptibility to biological clearance.Cell death discovery · 2026Article
- Orthogonal Ionic Liquid-Based Extraction Strategy Enables Amyloid-Specific Profiling of Aggregate Proteome.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Helical reconstruction of amyloids in cryoSPARC.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Self-assembling proteins compose the chemically resistant shell biomaterial of planktonic tintinnid ciliates.Nature communications · 2026Article
- Fragmentation-Induced Disassembly and Reaggregation of α-Synuclein Amyloid Fibrils.ACS chemical neuroscience · 2026Article
- Oral AA amyloidosis with granulomatous cheilitis: a case report and literature review.Clinical rheumatology · 2026Review
- Amyloid fibril polymorphism: Structural mechanisms of assembly and the links to disease.Current opinion in structural biology · 2026Review
- Enzymes of physiological amyloidogenesis control pathological amyloid toxicity.Life science alliance · 2026Article
374 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
5 authors at 1 institution in 1 country.
Funding
Abstract
The aggregation of proteins into amyloid fibrils and their deposition into plaques and intracellular inclusions is the hallmark of amyloid disease. The accumulation and deposition of amyloid fibrils, collectively known as amyloidosis, is associated with many pathological conditions that can be associated with ageing, such as Alzheimer disease, Parkinson disease, type II diabetes and dialysis-related amyloidosis. However, elucidation of the atomic structure of amyloid fibrils formed from their intact protein precursors and how fibril formation relates to disease has remained elusive. Recent advances in structural biology techniques, including cryo-electron microscopy and solid-state NMR spectroscopy, have finally broken this impasse. The first near-atomic-resolution structures of amyloid fibrils formed in vitro, seeded from plaque material and analysed directly ex vivo are now available. The results reveal cross-β structures that are far more intricate than anticipated. Here, we describe these structures, highlighting their similarities and differences, and the basis for their toxicity. We discuss how amyloid structure may affect the ability of fibrils to spread to different sites in the cell and between organisms in a prion-like manner, along with their roles in disease. These molecular insights will aid in understanding the development and spread of amyloid diseases and are inspiring new strategies for therapeutic intervention.
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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.