ArticleJournal of molecular biology2023
Genetically Encoded Aryl Alkyne for Raman Spectral Imaging of Intracellular α-Synuclein Fibrils.
Article in Journal of molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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
15 citing papers in PubMed, 14 citations in OpenAlex.
- Seeing the Chemistry of Biomolecular Condensates: In Situ Mapping of Composition and Water Content.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Expanding the methionine toolkit:bioRxiv : the preprint server for biology · 2026Article
- Site-Specific Raman Probes Reveal Droplet Aging and Residue-Level Fibril Polymorphism in TDP-43Journal of the American Chemical Society · 2026Article
- Kinetics and Spatial Distribution of β-Sheet Development in TDP-43ACS chemical neuroscience · 2026Article
- Nano-plasmonic SERS-based serum fingerprinting for analytical monitoring of Parkinson's disease and therapeutic response.Mikrochimica acta · 2026Article
- Correlative Raman and immunofluorescence imaging reveals different protein abundance between stress granules induced by oxidative damage.Journal of inorganic biochemistry · 2026Article
- Advances in Probing Amyloid Heterogeneity Using Vibrational Spectroscopy and Imaging.The journal of physical chemistry. B · 2025Review
- A dual fluorescent-Raman bioorthogonal probe for specific biosynthetic labeling of intracellular gangliosides.Communications chemistry · 2025Article
- Development of a Spectroscopic Map to Explain the Broad Raman Peak for Alkynes Solvated in Triethylamine.The journal of physical chemistry. B · 2025Article
- Raman spectroscopy and imaging of protein droplet formation and aggregation.Current opinion in structural biology · 2025Review
- Defining essential charged residues in fibril formation of a lysosomal derived N-terminal α-synuclein truncation.Nature communications · 2025Article
- Raman spectroscopy in the study of amyloid formation and phase separation.Biochemical Society transactions · 2024Review
- Water bend-libration as a cellular Raman imaging probe of hydration.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Analytical Techniques for Single-Cell Biochemical Assays of Lipids.Annual review of biomedical engineering · 2023Review
- Raman Spectroscopy on Brain Disorders: Transition from Fundamental Research to Clinical Applications.Biosensors · 2022Review
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 at 2 institutions in 1 country.
Funding
Abstract
α-Synuclein (α-syn) is an intrinsically disordered protein involved in a group of diseases collectively termed synucleinopathies, characterized by the aggregation of α-syn to form insoluble, β-sheet-rich amyloid fibrils. Amyloid fibrils are thought to contribute to disease progression through cell-to-cell transmission, templating and propagating intracellular amyloid formation. Raman spectral imaging offers a direct characterization of protein secondary structure via the amide-I backbone vibration; however, specific detection of α-syn conformational changes against the background of other cellular components presents a challenge. Here, we demonstrate the ability to unambiguously identify cellularly internalized α-syn fibrils by coupling Raman spectral imaging with the use of a genetically encoded aryl alkyne, 4-ethynyl-l-phenylalanine (F
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.