ArticleChemphyschem : a European journal of chemical physics and physical chemistry2011
A FRET sensor for non-invasive imaging of amyloid formation in vivo.
Article in Chemphyschem : a European journal of chemical physics and physical chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 115 citations in OpenAlex.
- The Intrinsic UV-Visible Fluorescence of Peptides Widely Used for Studying Amyloid Aggregation Devoid of Aromatic Residues.International journal of molecular sciences · 2026Article
- Mutational Scanning of α-Synuclein using a Clickable Protein Tag Reveals Determinants of Membrane-Induced Aggregation.bioRxiv : the preprint server for biology · 2026Article
- PROTAC-Mediated Degradation of mHTT Aggregates Attenuates Neurotoxicity in Cellular and R6/2 Mouse Models of Huntington's Disease.Journal of the American Chemical Society · 2026Article
- Mechanisms of Alpha-Synuclein-Seeded Aggregation in Neurons Revealed by Fluorescence Lifetime Imaging.ACS chemical neuroscience · 2025Article
- A safety mechanism enables tissue-specific resistance to protein aggregation during aging in C. elegans.PLoS biology · 2023Article
- Degradation of neurodegenerative disease-associated TDP-43 aggregates and oligomers via a proteolysis-targeting chimera.Journal of biomedical science · 2023Article
- Monitoring α-synuclein aggregation.Neurobiology of disease · 2023Review
- Dissecting aggregation and seeding dynamics of α-Syn polymorphs using the phasor approach to FLIM.Communications biology · 2022Article
- Molecular mechanism for the synchronized electrostatic coacervation and co-aggregation of alpha-synuclein and tau.Nature communications · 2022Article
- Protein Fibrillation under Crowded Conditions.Biomolecules · 2022Review
- Exploiting flow cytometry for the unbiased quantification of protein inclusions in Caenorhabditis elegans.Journal of neurochemistry · 2022Article
- A FRET-based method for monitoring structural transitions in protein self-organization.Cell reports methods · 2022Article
- Fӧrster resonance energy transfer analysis of amyloid state of proteins.BBA advances · 2022Article
- Observation of an α-synuclein liquid droplet state and its maturation into Lewy body-like assemblies.Journal of molecular cell biology · 2021Article
- An Expanded Polyproline Domain Maintains Mutant Huntingtin SolubleFrontiers in molecular neuroscience · 2021Article
- Comparative Studies in the A30P and A53T α-SynucleinFrontiers in cell and developmental biology · 2021Article
- Alpha-Synuclein FRET Biosensors Reveal Early Alpha-Synuclein Aggregation in the Endoplasmic Reticulum.Life (Basel, Switzerland) · 2020Article
- Intramitochondrial proteostasis is directly coupled to α-synuclein and amyloid β1-42 pathologies.The Journal of biological chemistry · 2020Article
- Localization of Fluorescent Targets in Deep Tissue With Expanded Beam Illumination for Studies of Cancer and the Brain.IEEE transactions on medical imaging · 2020Article
- Reducing INS-IGF1 signaling protects against non-cell autonomous vesicle rupture caused by SNCA spreading.Autophagy · 2020Article
Corrections and comments
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Authors and funding
13 authors at 4 institutions in 4 countries.
Funding
Abstract
Misfolding and aggregation of amyloidogenic polypeptides lie at the root of many neurodegenerative diseases. Whilst protein aggregation can be readily studied in vitro by established biophysical techniques, direct observation of the nature and kinetics of aggregation processes taking place in vivo is much more challenging. We describe here, however, a Förster resonance energy transfer sensor that permits the aggregation kinetics of amyloidogenic proteins to be quantified in living systems by exploiting our observation that amyloid assemblies can act as energy acceptors for variants of fluorescent proteins. The observed lifetime reduction can be attributed to fluorescence energy transfer to intrinsic energy states associated with the growing amyloid species. Indeed, for a-synuclein, a protein whose aggregation is linked to Parkinson's disease, we have used this sensor to follow the kinetics of the self-association reactions taking place in vitro and in vivo and to reveal the nature of the ensuing aggregated species. Experiments were conducted in vitro, in cells in culture and in living Caenorhabditis elegans. For the latter the readout correlates directly with the appearance of a toxic phenotype. The ability to measure the appearance and development of pathogenic amyloid species in a living animal and the ability to relate such data to similar processes observed in vitro provides a powerful new tool in the study of the pathology of the family of misfolding disorders. Our study confirms the importance of the molecular environment in which aggregation reactions take place, highlighting similarities as well as differences between the processes occurring in vitro and in vivo, and their significance for defining the molecular physiology of the diseases with which they are associated.
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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.