ReviewTrends in biochemical sciences2011
Recent progress in understanding Alzheimer's β-amyloid structures.
Review in Trends in biochemical sciences, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 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
67 citing papers in PubMed.
- Recruitment of Aβ into α‑Synuclein Condensates Catalyzes Primary Nucleation of α‑Synuclein Aggregation.ACS central science · 2025Article
- Efficient and accurate binding free energy calculation of AβProteins · 2025Article
- Ligands for Protein Fibrils of Amyloid-β, α-Synuclein, and Tau.Chemical reviews · 2025Review
- Morphological and Molecular Profiling of Amyloid-β Species in Alzheimer's Pathogenesis.Molecular neurobiology · 2025Review
- FLIM-Phasor Analysis (FLIM-ϕ) of Aβ-Induced Membrane Order Alterations: Towards a Cell-Based Biosensor for Early Alzheimer's Disease Diagnosis.Micromachines · 2025Article
- Structural diversity of Alzheimer-related protein aggregations revealed using photothermal ratio-metric micro-spectroscopy.Biomedical optics express · 2024Article
- Aggregation of the amyloid-β peptide (Aβ40) within condensates generated through liquid-liquid phase separation.Scientific reports · 2024Article
- Repurposing Anidulafungin for Alzheimer's Disease via Fragment-Based Drug Discovery.ACS chemical neuroscience · 2024Article
- An N-terminal acidic β-sheet domain is responsible for the metal-accumulation properties of amyloid-β protofibrils: a molecular dynamics study.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- Amyloid Beta in Aging and Alzheimer's Disease.International journal of molecular sciences · 2022Review
- Conformational Variability of Amyloid-β and the Morphological Diversity of Its Aggregates.Molecules (Basel, Switzerland) · 2022Review
- Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain.Journal of visualized experiments : JoVE · 2022Article
- Proteins Do Not Replicate, They Precipitate: Phase Transition and Loss of Function Toxicity in Amyloid Pathologies.Biology · 2022Review
- Non-monotonic fibril surface occlusion by GFP tags from coarse-grained molecular simulations.Computational and structural biotechnology journal · 2022Article
- Curcumin as Scaffold for Drug Discovery against Neurodegenerative Diseases.Biomedicines · 2021Review
- Ultrastructural evidence for self-replication of Alzheimer-associated Aβ42 amyloid along the sides of fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Structural Basis of Amyloid Strains in Alzheimer's Disease.ACS biomaterials science & engineering · 2020Review
- Unraveling the complexity of amyloid polymorphism using gold nanoparticles and cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Characterization of amyloid β fibril formation under microgravity conditions.NPJ microgravity · 2020Article
- Oligomers Are Promising Targets for Drug Development in the Treatment of Proteinopathies.Frontiers in molecular neuroscience · 2019Article
7 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
3 authors.
Funding
Abstract
The formation of amyloid fibrils, protofibrils and oligomers from the β-amyloid (Aβ) peptide represents a hallmark of Alzheimer's disease. Aβ-peptide-derived assemblies might be crucial for disease onset, but determining their atomic structures has proven to be a major challenge. Progress over the past 5 years has yielded substantial new data obtained with improved methodologies including electron cryo-microscopy and NMR. It is now possible to resolve the global fibril topology and the cross-β sheet organization within protofilaments, and to identify residues that are crucial for stabilizing secondary structural elements and peptide conformations within specific assemblies. These data have significantly enhanced our understanding of the mechanism of Aβ aggregation and have illuminated the possible relevance of specific conformers for neurodegenerative pathologies.
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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.