The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Accelerated α‐synuclein fibrillation in crowded milieu
Abstract
Parkinson's disease is the second most common age‐related neurodegenerative disease, resulting from loss of dopaminergic neurons in the substantia nigra. The aggregation and fibrillation of α‐synuclein has been implicated as a causative factor in the disease, and the process of fibril formation has been intensively studied in vitro with dilute protein solutions. However, the intracellular environment of proteins is crowded with other macromolecules, whose concentration can reach 400 g/l. To address this discrepancy, the effect of molecular crowding on α‐synuclein fibrillation has being studied. The addition of high concentrations of different polymers (proteins, polysaccharides and polyethylene glycols) dramatically accelerated α‐synuclein fibrillation in vitro. The magnitude of the accelerating effect depended on the nature of the polymer, its length and concentration. Our results suggest that the major factor responsible for the accelerated fibrillation under crowded conditions is the excluded volume.
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Cites
Macromolecular crowding: obvious but underappreciated
Ellis, R. J. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01938-7 · Cited by 2,309
Minton, A. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.r100005200 · Cited by 1,474
Zimmerman, S. B., & Trach, S. O. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90499-v · Cited by 1,337
Iwai, A., Masliah, E., Yoshimoto, M., Ge, N., Flanagan, L., Rohan de Silva, H. A., Kittel, A., & Saitoh, T. (1995) · Neuron · doi:10.1016/0896-6273(95)90302-x · Cited by 1,316
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-citationImplications of macromolecular crowding for protein assembly
Minton, A. P. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00045-7 · Cited by 649
Molecular confinement influences protein structure and enhances thermal protein stability
Eggers, D. K., & Valentine, J. S. (2001) · Protein Science · doi:10.1110/ps.36201 · Cited by 393
Minton, A. P. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76576-3 · Cited by 218
Influence of excluded volume upon macromolecular structure and associations in ‘crowded” media
Minton, A. P. (1997) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(97)80159-0 · Cited by 212
Cited by
Conformational constraints for amyloid fibrillation: the importance of being unfolded
Uversky, V. N., & Fink, A. L. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2003.12.008 · Cited by 1,015
Self-citationTHE BIOCHEMISTRY OF PARKINSON'S DISEASE
Cookson, M. R. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133400 · Cited by 664
α-Synuclein misfolding and Parkinson's disease
Breydo, L., Wu, J. W., & Uversky, V. N. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.10.002 · Cited by 657
Self-citationNeuropathology, 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
Self-citationUnusual biophysics of intrinsically disordered proteins
Uversky, V. N. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.12.008 · Cited by 566
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Metadata
- Authors
- Uversky, V. N., M. Cooper, E., Bower, K. S., Li, J., & Fink, A. L.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2002-03-04
- Volume
- 515
- Issue
- 1-3
- Pages
- 99-103
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2098004479
- Cited by
- 291
- References
- 9
- FWCI
- 7.53
- Type
- journal article
- Language
- en
- Open access
- closed
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- Uversky, V. N., M. Cooper, E., Bower, K. S., Li, J., & Fink, A. L. (2002). Accelerated α‐synuclein fibrillation in crowded milieu. FEBS Letters. https://doi.org/10.1016/s0014-5793(02)02446-8
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