ReviewCurrent opinion in structural biology2025
The evolving role of solid state nuclear magnetic resonance methods in studies of amyloid fibrils.
Review in Current opinion in structural biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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Who cites it
7 citing papers in PubMed.
- Controlled Seeding of β-Amyloid Fibrillation Reveals Propagation of Structural Polymorphisms in Cellular Environments.Biochemistry · 2026Article
- Integrating NMR Restraints into Coarse-Grained Simulations: Toward Accurate Conformational Ensembles of Complex Protein Systems.Journal of the American Chemical Society · 2026Article
- Article
- Aducanumab binding to AβProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Atomic Structure of GNNQQNY Nanocrystals: A Validated Approach for Polymorphic Amyloids.The journal of physical chemistry letters · 2025Article
- Prions and protein aggregates as pathogens, self-propagating structures, biomarkers, and therapeutic targets.Microbiology and molecular biology reviews : MMBR · 2025Review
- Aducanumab Binding to AβbioRxiv : the preprint server for biology · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
Abstract
Beginning in the 1990s, solid state nuclear magnetic resonance (ssNMR) methods played a major role in elucidating the molecular structures and properties of amyloid fibrils. General principles that explain these structures and properties were uncovered and experimentally-based structural models were first developed from ssNMR data. Since 2017, cryogenic electron microscopy (cryo-EM) techniques have become capable of solving amyloid structures at near-atomic resolution. Although cryo-EM measurements are now the main approach for structural studies of amyloid fibrils, ssNMR measurements remain essential for studies of certain structures and structural features, as well as studies of dynamical and mechanistic aspects. Recent publications from various research groups illustrate the continuing importance of ssNMR and the unique information available from ssNMR measurements in amyloid research.
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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.