ReviewMethods (San Diego, Calif.)2018
Hidden motions and motion-induced invisibility: Dynamics-based spectral editing in solid-state NMR.
Review in Methods (San Diego, Calif.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 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.
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Who cites it
54 citing papers in PubMed.
- Standardization of cross-site biophysical studies of bovine insulin amyloids is challenged by structural polymorphism.European biophysics journal : EBJ · 2026Article
- Matrix plasticity and the molecular basis of extracellular filament assembly inScience advances · 2026Article
- Photochromic Cholesteric Liquid Crystals via Arylazopyrazole Functionalization of Hydroxypropyl Cellulose.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Molecular dynamics in the stratum corneum of plantar heels in atopic dermatitis patients.Biophysical journal · 2026Article
- Crosslinking, salt-induced aging, and secondary structure formation in Peptide-containing coacervates inspired by spider silk.Communications chemistry · 2025Article
- Probing How Anti-huntingtin Antibodies Bind the Fibrillar Fuzzy Coat Using Solid-State NMR.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Capturing the Conformational Heterogeneity of HSPB1 Chaperone Oligomers at Atomic Resolution.Journal of the American Chemical Society · 2025Article
- Decoding Order and Disorder in Proteins by NMR Spectroscopy.Journal of the American Chemical Society · 2025Article
- Inhibitor-based modulation of huntingtin aggregation mechanisms mitigates fibril-induced cellular stress.Nature communications · 2025Article
- Solid-state NMR protocols for unveiling dynamics and (drug) interactions of membrane-bound proteins.Protein science : a publication of the Protein Society · 2025Article
- Solid state NMR spectral editing of histidine, arginine and lysine using Hadamard encoding.Journal of biomolecular NMR · 2025Article
- Conformational Dynamics of BacteriochlorophyllThe journal of physical chemistry. B · 2025Article
- From molecular descriptions to cellular functions of intrinsically disordered protein regions.Biophysics reviews · 2024Review
- Insights into Ligand-Mediated Activation of an Oligomeric Ring-Shaped Gene-Regulatory Protein from Solution- and Solid-State NMR.Journal of molecular biology · 2024Article
- Resolving Atomic-Level Dynamics and Interactions of High-Molecular-Weight Hyaluronic Acid by Multidimensional Solid-State NMR.ACS applied materials & interfaces · 2024Article
- A solid beta-sheet structure is formed at the surface of FUS droplets during aging.Nature chemical biology · 2024Article
- Magic-angle spinning NMR structure of Opa60 in lipid bilayers.Journal of structural biology: X · 2024Article
- Insights into Ligand-Mediated Activation of an Oligomeric Ring-Shaped Gene-Regulatory Protein from Solution- and Solid-State NMR.bioRxiv : the preprint server for biology · 2024Article
- Solid-state nuclear magnetic resonance in the structural study of polyglutamine aggregation.Biochemical Society transactions · 2024Review
- Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Solid-state nuclear magnetic resonance (ssNMR) spectroscopy enables the structural characterization of a diverse array of biological assemblies that include amyloid fibrils, non-amyloid aggregates, membrane-associated proteins and viral capsids. Such biological samples feature functionally relevant molecular dynamics, which often affect different parts of the sample in different ways. Solid-state NMR experiments' sensitivity to dynamics represents a double-edged sword. On the one hand, it offers a chance to measure dynamics in great detail. On the other hand, certain types of motion lead to signal loss and experimental inefficiencies that at first glance interfere with the application of ssNMR to overly dynamic proteins. Dynamics-based spectral editing (DYSE) ssNMR methods leverage motion-dependent signal losses to simplify spectra and enable the study of sub-structures with particular motional properties.
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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.