ReviewNature2016
The activities of amyloids from a structural perspective.
Review in Nature, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 218 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
218 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Amyloid Biomarkers in Conformational Diseases at Face Value: A Systematic Review.Molecules (Basel, Switzerland) · 2017Pooled it
- Anisotropic Electrostatics in the Instability of GLP‑1 Analog Micelles: Effects of Electrolytes, Denaturants, pH, and Temperature.ACS omega · 2026Article
- Targeting soluble misfolded oligomers in anti-amyloid research.Nature reviews. Chemistry · 2026Review
- Bioinformatic assessment of the potential amyloidogenicity of the human and evolutionarily more ancient proteomes.The Biochemical journal · 2026Article
- Adhesion Mechanisms of Amyloid-Like Oligomer Monolayers Enabling Stable Surface Modification for Inert Polymers.JACS Au · 2026Article
- The influence of H-bonding network disruption on morphology, structure and autofluorescence of amyloids.Materials advances · 2026Article
- Trimethylammonium-diphenylhexatriene and propionic acid-diphenylhexatriene are sensitive fluorescence probes of amyloid formation by human IAPP.Analytical biochemistry · 2026Article
- Structural Mechanism and Cellular Restriction of Tau Seeding from Endolysosomes.bioRxiv : the preprint server for biology · 2026Article
- ATP binding to lysozyme and superfolder GFP amyloid fibrils induces aggregate remodeling and attenuates their cytotoxicity.Cell death discovery · 2026Article
- YB-1 AP-CSD Forms Cross-β Amyloid Fibrils Without Secondary-Structure Conversion In Vitro.International journal of molecular sciences · 2026Article
- Transient Interactions of α-Synuclein N- and C-Termini.ACS chemical neuroscience · 2026Article
- Condensate State as Determinant of Amyloid Pathology in Neurodegeneration.Biomolecules · 2026Review
- Protection and Delivery of Phytochemicals from Passive Encapsulation to Guaranteed Self-Assembly Induced by Amyloid Template for Chronic Disease Prevention via Modulating Microbial-Host Crosstalk.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Structural and mechanistic characterization of heparin interactions with tau fibrils.The Journal of biological chemistry · 2026Article
- Atypical β-strand insertion mediates the noncovalent cross-linking in amyloid aggregates.Nature communications · 2026Article
- Mechanism of Self-Assembly of the Gonadropin Releasing Hormone Antagonist Teverelix into Amyloid Fibrils.Molecular pharmaceutics · 2026Article
- AmyloGram reveals amyloidogenic potential in stroke thrombus proteomes.The Biochemical journal · 2025Article
- Hippocampal Interneurons Shape Spatial Coding Alterations in Neurological Disorders.Molecular neurobiology · 2025Review
- Current Understanding of Protein Aggregation in Neurodegenerative Diseases.International journal of molecular sciences · 2025Review
- In vitro and in vivo disease models of cardiac amyloidosis: progress, pitfalls, and potential.Cardiovascular research · 2025Review
158 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.
Funding
Abstract
The aggregation of proteins into structures known as amyloids is observed in many neurodegenerative diseases, including Alzheimer's disease. Amyloids are composed of pairs of tightly interacting, many stranded and repetitive intermolecular β-sheets, which form the cross-β-sheet structure. This structure enables amyloids to grow by recruitment of the same protein and its repetition can transform a weak biological activity into a potent one through cooperativity and avidity. Amyloids therefore have the potential to self-replicate and can adapt to the environment, yielding cell-to-cell transmissibility, prion infectivity and toxicity.
Indexed as
Identifiers
27830791What 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.