ReviewJournal of structural biology2011
Amyloid structure and assembly: insights from scanning transmission electron microscopy.
Review in Journal of structural biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 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
45 citing papers in PubMed, 115 citations in OpenAlex.
- Cognitive and Histological Methodological Framework for an Intrahippocampal AβNeurology international · 2026Article
- Digging Deep into Alzheimer Disease: How Electron Microscopy Helps Elucidating Its Pathogenesis.Cellular and molecular neurobiology · 2026Review
- Multimodal Diagnosis of Cardiac Amyloidosis: Integrating Imaging, Histochemistry, and Proteomics of Precise Typing.International journal of molecular sciences · 2026Review
- Systematic Comparison of Commercial Uranyl-Alternative Stains for Negative- and Positive-Staining Transmission Electron Microscopy of Organic Specimens.Advanced healthcare materials · 2025Article
- Advancing Amyloid Aggregation Research: A Focus on Innovative Therapies, Molecular Modeling and Nano-Delivery Systems in Alzheimer's Disease.Current drug targets · 2025Review
- Analyzing Amylin Aggregation Inhibition Through Quantum Dot Fluorescence Imaging.International journal of molecular sciences · 2024Article
- Structural Mapping of Protein Aggregates in Live Cells Modeling Huntington's Disease.Angewandte Chemie (International ed. in English) · 2024Article
- Nasopharyngeal amyloidoma: report of three cases and review of the literature.Journal of cancer research and clinical oncology · 2024Review
- Transthyretin Stabilizers and Seeding Inhibitors as Therapies for Amyloid Transthyretin Cardiomyopathy.Pharmaceutics · 2023Review
- Hyperphosphorylated tau (p-tau) and drug discovery in the context of Alzheimer's disease and related tauopathies.Drug discovery today · 2023Review
- Monitoring α-synuclein aggregation.Neurobiology of disease · 2023Review
- Amyloid seeding as a disease mechanism and treatment target in transthyretin cardiac amyloidosis.Heart failure reviews · 2022Review
- Folding Mechanism and Aggregation Propensity of the KH0 Domain of FMRP and Its R138Q Pathological Variant.International journal of molecular sciences · 2022Article
- Challenges in Experimental Methods.Methods in molecular biology (Clifton, N.J.) · 2022Article
- From Quantum Mechanics, Classical Mechanics, and Bioinformatics to Artificial Intelligence Studies in Neurodegenerative Diseases.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Modified Low-Temperature Extraction Method for Isolation ofInternational journal of molecular sciences · 2021Article
- Amyloid-β oligomerization monitored by single-molecule stepwise photobleaching.Methods (San Diego, Calif.) · 2021Article
- Amyloidoma: a review and case report.Skeletal radiology · 2021Review
- Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective.Frontiers in molecular neuroscience · 2021Review
- Revealing the assembly of filamentous proteins with scanning transmission electron microscopy.PloS one · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 5 institutions in 3 countries.
Funding
Abstract
Amyloid fibrils are filamentous protein aggregates implicated in several common diseases such as Alzheimer's disease and type II diabetes. Similar structures are also the molecular principle of the infectious spongiform encephalopathies such as Creutzfeldt-Jakob disease in humans, scrapie in sheep, and of the so-called yeast prions, inherited non-chromosomal elements found in yeast and fungi. Scanning transmission electron microscopy (STEM) is often used to delineate the assembly mechanism and structural properties of amyloid aggregates. In this review we consider specifically contributions and limitations of STEM for the investigation of amyloid assembly pathways, fibril polymorphisms and structural models of amyloid fibrils. This type of microscopy provides the only method to directly measure the mass-per-length (MPL) of individual filaments. Made on both in vitro assembled and ex vivo samples, STEM mass measurements have illuminated the hierarchical relationships between amyloid fibrils and revealed that polymorphic fibrils and various globular oligomers can assemble simultaneously from a single polypeptide. The MPLs also impose strong constraints on possible packing schemes, assisting in molecular model building when combined with high-resolution methods like solid-state nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR).
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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.