The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
Dopamine and L‐dopa disaggregate amyloid fibrils: implications for Parkinson's and Alzheimer's disease
Abstract
Protein deposition diseases involve the aggregation of normally soluble proteins, leading to both fibrillar and amorphous deposits. The aggregation of α‐synuclein is associated with Parkinson's disease, and the aggregation of the Aβ peptide is associated with Alzheimer's disease. Here we show that L‐dopa, dopamine, and other catecholamines dissolve fibrils of α‐synuclein and Aβ peptide generated in vitro. The catecholamines also inhibited the fibrillation of these proteins. In addition, intraneuronal α‐synuclein deposits formed in a mouse model were dissolved by incubation of tissue slices with L‐dopa. These catecholamines are susceptible to oxidative breakdown, and we show that oxidation products are more effective than the parent compounds in inhibition. The ability to dissolve fibrils provides a new approach for studying mechanisms and consequences (e.g., the relationship between fibril formation and neurodegeneration) of protein aggregation. It is also likely to help in the development of strategies for the prevention and treatment of protein deposition diseases.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Protein damage and degradation by oxygen radicals. I. general aspects.
Davies, K. J. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48018-0 · Cited by 1,634
(1998) · Europe PMC (PubMed Central) · Cited by 1,594
Neuropathology of Parkinsonʼs Disease
Forno, L. S. (1996) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199603000-00001 · Cited by 1,465
Amyloid pores from pathogenic mutations
Lashuel, H. A., Hartley, D., Petre, B. M., Walz, T., & Lansbury, P. T. (2002) · Nature · doi:10.1038/418291a · Cited by 1,289
Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavine T
Naiki, H., Higuchi, K., Hosokawa, M., & Takeda, T. (1989) · Analytical Biochemistry · doi:10.1016/0003-2697(89)90046-8 · Cited by 1,223
Kinetic Stabilization of the α-Synuclein Protofibril by a Dopamine-α-Synuclein Adduct
Conway, K. A., Rochet, J.-C., Bieganski, R. M., & Lansbury, P. T. (2001) · Science · doi:10.1126/science.1063522 · Cited by 1,127
Oxidative Pathways for Catecholamines in the Genesis of Neuromelanin and Cytotoxic Quinones
GRAHAM, D. G. (1978) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)13535-9 · Cited by 1,126
Evidence for a Partially Folded Intermediate in α-Synuclein Fibril Formation
Uversky, V. N., Li, J., & Fink, A. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010907200 · Cited by 1,096
Self-citationAlzheimer's Disease--Genotypes, Phenotype, and Treatments
Selkoe, D. J. (1997) · Science · doi:10.1126/science.275.5300.630 · Cited by 875
Carrell, R. W., & Lomas, D. A. (1997) · The Lancet · doi:10.1016/s0140-6736(97)02073-4 · Cited by 807
Cited by
Necula, M., Kayed, R., Milton, S., & Glabe, C. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608207200 · Cited by 680
Nguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Dominguez, L., Shea, J.-E., Dokholyan, N. V., De Simone, A., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01122 · Cited by 678
Neuropathology, biochemistry, and biophysics of α‐synuclein aggregation
Uversky, V. N. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04764.x · Cited by 567
DLB and PDD boundary issues: Diagnosis, treatment, molecular pathology, and biomarkers
Lippa, C. F., Duda, J. E., Grossman, M., Hurtig, H. I., Aarsland, D., Boeve, B. F., Brooks, D. J., Dickson, D. W., Dubois, B., Emre, M., et al. (2007) · Neurology · doi:10.1212/01.wnl.0000256715.13907.d3 · Cited by 548
α-Synuclein misfolding and aggregation: Implications in Parkinson’s disease pathogenesis
Mehra, S., Sahay, S., & Maji, S. K. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.03.001 · Cited by 499
Metadata
- Authors
- Li, J., Zhu, M., Manning-Bog, A. B., Di Monte, D. A., & Fink, A. L.
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2004-04
- Volume
- 18
- Issue
- 9
- Pages
- 962-964
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W1968990406
- Cited by
- 258
- References
- 45
- FWCI
- 8.02
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Dopamine and L‐dopa disaggregate amyloid fibrils: implications for Parkinson's and Alzheimer's disease. https://app.cochat.ai/papers/10.1096/fj.03-0770fje
- The paper
- Li, J., Zhu, M., Manning-Bog, A. B., Di Monte, D. A., & Fink, A. L. (2004). Dopamine and L‐dopa disaggregate amyloid fibrils: implications for Parkinson's and Alzheimer's disease. The FASEB Journal. https://doi.org/10.1096/fj.03-0770fje
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.