ReviewAnnual review of physical chemistry2011
Solid-state NMR studies of amyloid fibril structure.
Review in Annual review of physical chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 268 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
268 citing papers in PubMed, 543 citations in OpenAlex.
- Investigating Structural Heterogeneities of Amyloid Aggregates with Spatially Resolved Infrared Spectroscopy.Accounts of chemical research · 2026Article
- Structural Hierarchy and Maturation of Amyloid Fibrils Revealed by Interface Descriptor Analysis.Journal of chemical information and modeling · 2026Article
- In Silicon Deciphering Atomic-Scale Structural Units in Peptide Glass.Angewandte Chemie (International ed. in English) · 2026Article
- Engineered protein nanofibrils for chain-integrated water treatment: From source monitoring to end-point purification.Eco-Environment & Health · 2026Review
- Ultra-Wideline 2D Correlations Among Low-γ Species in Solid-State NMR via the Progressive Saturation of a Common Proton Reservoir.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Single Amino Acid-Based Control of Fibril Supramolecular Chirality.The journal of physical chemistry letters · 2026Article
- amyloid-predict and LLPS-predict: Predicting phase separation propensities in the intrinsically disordered proteome.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- In vitro, cellular and in vivo studies of amyloid oligomers structure and toxicity: Challenges and advances.Protein science : a publication of the Protein Society · 2026Review
- Single-fibril Förster resonance energy transfer imaging and deep learning reveal concentration dependence of amyloid β 42 aggregation pathways.PNAS nexus · 2025Article
- High-qualitySolid state nuclear magnetic resonance · 2025Article
- Illuminating High-Affinity ATP Binding to the Sodium-Potassium Pump Using Solid-State NMR Spectroscopy.Molecules (Basel, Switzerland) · 2025Review
- Pulse sequence design for high field NMR with NV centers in dipolarly coupled samples.Scientific reports · 2025Article
- Protein aggregation and neurodegenerative disease: Structural outlook for the novel therapeutics.Proteins · 2025Review
- Recent Advances in Amyloids Structural Studies and Thin Film Applications.Molecules (Basel, Switzerland) · 2025Review
- Ligands for Protein Fibrils of Amyloid-β, α-Synuclein, and Tau.Chemical reviews · 2025Review
- Experimental methods for studying amyloid cross-interactions.Protein science : a publication of the Protein Society · 2025Review
- A β-hairpin peptide derived from Aβ forms different oligomers in the crystal state and in aqueous solution.Organic & biomolecular chemistry · 2025Article
- Sampling Conformational Ensembles of Highly Dynamic Proteins via Generative Deep Learning.Journal of chemical information and modeling · 2025Article
- Conformational Analysis of UniformlyMolecules (Basel, Switzerland) · 2025Article
- Ordered Aggregates of Fmoc-Diphenylalanine at Alkaline pH as a Precursor of Fibril Formation and Peptide Gelation.The journal of physical chemistry. B · 2025Article
208 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
1 author at 1 institution in 1 country.
Funding
Abstract
Current interest in amyloid fibrils stems from their involvement in neurodegenerative and other diseases and from their role as an alternative structural state for many peptides and proteins. Solid-state nuclear magnetic resonance (NMR) methods have the unique capability of providing detailed structural constraints for amyloid fibrils, sufficient for the development of full molecular models. In this article, recent progress in the application of solid-state NMR to fibrils associated with Alzheimer's disease, prion fibrils, and related systems is reviewed, along with relevant developments in solid-state NMR techniques and technology.
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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.