ArticleMethods in molecular biology (Clifton, N.J.)2019
Probing Structural Changes in Alpha-Synuclein by Nuclear Magnetic Resonance Spectroscopy.
Article in Methods in molecular biology (Clifton, N.J.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed.
- Microfluidic platform for understanding Parkinson's disease and α-synuclein conformation.Translational neurodegeneration · 2025Review
- Control of G protein-coupled receptor function via membrane-interacting intrinsically disordered C-terminal domains.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Control of G protein-coupled receptor function via membrane-interacting intrinsically disordered C-terminal domains.bioRxiv : the preprint server for biology · 2024Article
- IDPConformerGenerator: A Flexible Software Suite for Sampling the Conformational Space of Disordered Protein States.The journal of physical chemistry. A · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Alpha-synuclein, the principal protein involved in the pathogenesis of Parkinson's disease, has been shown to exchange between multiple conformational states, with hitherto unclear physiological role of such conformational changes. Due to its ability to provide rich structural information for proteins in their near-native environment, nuclear magnetic resonance (NMR) spectroscopy has been a valuable tool to study these conformational states. In this review we describe the application of model systems and NMR methods to the study of membrane-bound states of alpha-synuclein. We provide a detailed description, primarily meant for someone new to the field, of how to prepare the necessary samples, perform the basic experiments, and obtain an initial interpretation of the results.
Indexed as
Identifiers
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.