The DOI matches its Crossref record; 33 of the 34 references it cites were found in a registry or an index.
Trimethylamine‐ N ‐oxide‐induced folding of α‐synuclein
Abstract
The effect of the natural osmolyte trimethylamine-N-oxide (TMAO) on the structural properties and fibril formation of the natively unfolded protein human alpha-synuclein was studied using several physico-chemical methods. TMAO induced folding of alpha-synuclein: at moderate concentrations, a partially folded intermediate with enhanced propensity for fibrillation accumulated; at higher concentrations, alpha-synuclein was tightly folded and underwent self-association to form oligomers. The latter conformation was significantly helical and probably represents the physiologically folded form of the protein.
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“When the concentration of TMAO is high enough, α-synuclein forms oligomers in which the subunits are folded and are not able to fibrillate [88].”
From Implication of Trimethylamine N-Oxide (TMAO) in Disease: Potential Biomarker or New Therapeutic Target (2018) · cites this paper as [88]
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Cites
Bhushan, B. (2016) · Springer eBooks · doi:10.1007/978-94-017-9780-1_101037 · Cited by 3,800
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Intrinsically disordered protein
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Why are ?natively unfolded? proteins unstructured under physiologic conditions?
Uversky, V. N., Gillespie, J. R., & Fink, A. L. (2000) · Proteins Structure Function and Bioinformatics · doi:10.1002/1097-0134(20001115)41:3 · Cited by 2,097
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Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal
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NACP, A Protein Implicated in Alzheimer's Disease and Learning, Is Natively Unfolded
Weinreb, P. H., Zhen, W., Poon, A. W., Conway, K. A., & Lansbury, P. T. (1996) · Biochemistry · doi:10.1021/bi961799n · Cited by 1,524
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- Naiki H., 1990, Lab. Invest., 62, 768
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Gharibyan, A. L. (2012) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Pastwa, P., Panuszko, A., Pladzyk, A., & Bruździak, P. (2026) · ChemPhysChem · doi:10.1002/cphc.202500640
Solvent-mediated modulation of biopolymer interactions and aggregation
Martins, L. D. A., Araújo, J. C. B., de Andrade, G. C., & Marques, M. A. (2026) · Elsevier eBooks · doi:10.1016/b978-0-323-99507-8.00066-4
Dollar, A. N., Kelley, D. W., & Webb, I. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c10987
Altahrawi, A. Y., Sofi, F., Kanjwal, Z., & Shah, Z. A. (2026) · Cells · doi:10.3390/cells15201845
Influence of Temperature and Osmolytes on Conformational Dynamics of Alpha Synuclein
Hampton, J., Lynch, C., Rider, R. L., Lantz, C., Xi, Z., & Russell, D. H. (2026) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6c04859
A study of intrinsic disorder and its role in functional proteomics
Mohan, A. (2009) · IUScholarWorks (Indiana University)
Metadata
- Authors
- Uversky, V. N., Li, J., & Fink, A. L.
- Affiliations
- Russian Academy of Sciences (RU)
- University of California, Santa Cruz (US)
- Corresponding author
- Fink, Anthony L.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2001-11-09
- Volume
- 509
- Issue
- 1
- Pages
- 31-35
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1988949963
- Cited by
- 208
- References
- 34
- Citations by year
- 2026: 9 · 2025: 13 · 2024: 11 · 2023: 5 · 2022: 12 · 2021: 8 · 2020: 10 · 2019: 7 · 2018: 8 · 2017: 8 · 2016: 8 · 2015: 8 · 2014: 12 · 2013: 10 · 2012: 11
- FWCI
- 3.54
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Digital Commons - University of South Florida (University of South Florida) (submittedVersion)
- Topics
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Keywords
- trimethylamine N-oxide, alpha-synuclein, protein folding, osmolytes, intrinsically disordered proteins, fibril formation, folding intermediates, oligomerization, helical conformation, protein self-association
- MeSH terms
- Acrylamides, Circular Dichroism, Dose-Response Relationship, Drug, Methylamines, Nerve Tissue Proteins, Peptides, Protein Conformation, Recombinant Proteins, Scattering, Radiation, Spectrometry, Fluorescence, Time Factors, X-Rays, Oxidants, Protein Structure, Secondary, Protein Folding, Synucleins, alpha-Synuclein
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