ArticleProceedings of the National Academy of Sciences of the United States of America2020
Sequence-independent recognition of the amyloid structural motif by GFP protein family.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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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
9 citing papers in PubMed, 11 citations in OpenAlex.
- A New Soaking Protocol to Live StainbioRxiv : the preprint server for biology · 2026Article
- Self-assembled metabolite-derived amyloid-like structures: implications for disease, therapeutics, and biomedical applications.Molecular biology reports · 2026Review
- Quantitative detection of amyloid fibrils using fluorescence resonance energy transfer between engineered yellow and cyan proteins.Protein science : a publication of the Protein Society · 2025Article
- Recent Developments of Hybrid Fluorescence Techniques: Advances in Amyloid Detection Methods.Current protein & peptide science · 2024Review
- A FRET-based method for monitoring structural transitions in protein self-organization.Cell reports methods · 2022Article
- Super-resolution microscopy: a closer look at synaptic dysfunction in Alzheimer disease.Nature reviews. Neuroscience · 2021Review
- β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis.International journal of molecular sciences · 2021Review
- Vacuolar accumulation and colocalization is not a proper criterion for cytoplasmic soluble proteins undergoing selective autophagy.Plant signaling & behavior · 2021Article
- GFP lights up amyloid fibrils.Nature methods · 2020Article
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8 authors at 2 institutions in 1 country.
Funding
Abstract
Cnidarian fluorescent protein (FP) derivatives such as GFP, mCherry, and mEOS2 have been widely used to monitor gene expression and protein localization through biological imaging because they are considered functionally inert. We demonstrate that FPs specifically bind amyloid fibrils formed from many natural peptides and proteins. FPs do not bind other nonamyloid fibrillar structures such as microtubules or actin filaments and do not bind to amorphous aggregates. FPs can also bind small aggregates formed during the lag phase and early elongation phase of fibril formation and can inhibit amyloid fibril formation in a dose-dependent manner. These findings suggest caution should be taken in interpreting FP-fusion protein localization data when amyloid structures may be present. Given the pathological significance of amyloid-related species in some diseases, detection and inhibition of amyloid fibril formation using FPs can provide insights on developing diagnostic tools.
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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.