ArticleJournal of molecular biology2012
Fiber diffraction data indicate a hollow core for the Alzheimer's aβ 3-fold symmetric fibril.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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.
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Who cites it
26 citing papers in PubMed, 36 citations in OpenAlex.
- Investigation of biomolecular dynamics by sensitivity-enhancedJournal of magnetic resonance open · 2024Article
- Persistence of Methionine Side Chain Mobility at Low Temperatures in a Nine-Residue Low Complexity Peptide, as Probed byChemphyschem : a European journal of chemical physics and physical chemistry · 2024Article
- Comparative Hydrophobic Core Dynamics Between Wild-Type Amyloid-β Fibrils, Glutamate-3 Truncation, and Serine-8 Phosphorylation.Chemphyschem : a European journal of chemical physics and physical chemistry · 2022Article
- General Principles Underpinning Amyloid Structure.Frontiers in neuroscience · 2022Review
- The Structural Basis of Amyloid Strains in Alzheimer's Disease.ACS biomaterials science & engineering · 2020Review
- Deuteron Quadrupolar Chemical Exchange Saturation Transfer (Q-CEST) Solid-State NMR for Static Powder Samples: Approach and Applications to Amyloid-β Fibrils.Chemphyschem : a European journal of chemical physics and physical chemistry · 2020Article
- Phenyl-Ring Dynamics in Amyloid Fibrils and Proteins: The Microscopic-Order-Macroscopic-Disorder Perspective.The journal of physical chemistry. B · 2018Article
- MOMD Analysis of NMR Line Shapes from Aβ-Amyloid Fibrils: A New Tool for Characterizing Molecular Environments in Protein Aggregates.The journal of physical chemistry. B · 2018Article
- Solid-State NMR Structural Characterization of Self-Assembled Peptides with SelectiveMethods in molecular biology (Clifton, N.J.) · 2018Review
- Structural Biology of PrP Prions.Cold Spring Harbor perspectives in medicine · 2017Review
- Water Distribution, Dynamics, and Interactions with Alzheimer's β-Amyloid Fibrils Investigated by Solid-State NMR.Journal of the American Chemical Society · 2017Article
- Fast Motions of Key Methyl Groups in Amyloid-β Fibrils.Biophysical journal · 2016Article
- Amyloid structure exhibits polymorphism on multiple length scales in human brain tissue.Scientific reports · 2016Article
- Flexibility and Solvation of Amyloid-β Hydrophobic Core.The Journal of biological chemistry · 2016Article
- Structural Polymorphism of Alzheimer's β-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study.Journal of the American Chemical Society · 2016Article
- Molecular Structure of Aggregated Amyloid-β: Insights from Solid-State Nuclear Magnetic Resonance.Cold Spring Harbor perspectives in medicine · 2016Review
- On the lack of polymorphism in Aβ-peptide aggregates derived from patient brains.Protein science : a publication of the Protein Society · 2015Article
- Structural studies of truncated forms of the prion protein PrP.Biophysical journal · 2015Article
- Truncated forms of the prion protein PrP demonstrate the need for complexity in prion structure.Prion · 2015Article
- A synchrotron-based hydroxyl radical footprinting analysis of amyloid fibrils and prefibrillar intermediates with residue-specific resolution.Biochemistry · 2014Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Amyloid β protein (Aβ), the principal component of the extracellular plaques found in the brains of patients with Alzheimer's disease, forms fibrils well suited to structural study by X-ray fiber diffraction. Fiber diffraction patterns from the 40-residue form Aβ(1-40) confirm a number of features of a 3-fold symmetric Aβ model from solid-state NMR (ssNMR) but suggest that the fibrils have a hollow core not present in the original ssNMR models. Diffraction patterns calculated from a revised 3-fold hollow model with a more regular β-sheet structure are in much better agreement with the observed diffraction data than patterns calculated from the original ssNMR model. Refinement of a hollow-core model against ssNMR data led to a revised ssNMR model, similar to the fiber diffraction model.
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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.