The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
A Protein-Chameleon: Conformational Plasticity of α-Synuclein, a Disordered Protein Involved in Neurodegenerative Disorders
Abstract
Under the physiological conditions in vitro, alpha-synuclein, a conservative presynaptic protein, the aggregation and fibrillation of which is assumed to be involved into the pathogenesis of Parkinson's disease and several other neurodegenerative disorders, known as synucleinopathies, is characterized by the lack of rigid well-defined structure; i.e., it belongs to the class of intrinsically unstructured proteins. Intriguingly, alpha-synuclein is characterized by a remarkable conformational plasticity, adopting a series of different conformations depending on the environment. For example, this protein may either stay substantially unfolded, or adopt an amyloidogenic partially folded conformation, or fold into alpha-helical or beta-structural species, both monomeric and oligomeric. Furthermore, it might form several morphologically different types of aggregates, including oligomers (spheres or doughnuts), amorphous aggregates, and or amyloid-like fibrils. The peculiarities of this astonishing conformational behavior are analyzed to shed light on structural plasticity of this protein-chameleon.
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Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
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Intrinsic Disorder and Protein Function
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A68: a Major Subunit of Paired Helical Filaments and Derivatized Forms of Normal Tau
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Self-citationDEXTER, D. T., CARAYON, A., JAVOY-AGID, F., AGID, Y., WELLS, F. R., DANIEL, S. E., LEES, A. J., JENNER, P., & MARSDEN, C. D. (1991) · Brain · doi:10.1093/brain/114.4.1953 · Cited by 1,043
Cited by
Function and structure of inherently disordered proteins
Dunker, A. K., Silman, I., Uversky, V. N., & Sussman, J. L. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.10.002 · Cited by 963
Self-citationShowing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
Uversky, V. N., Oldfield, C. J., & Dunker, A. K. (2005) · Journal of Molecular Recognition · doi:10.1002/jmr.747 · Cited by 847
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-citationα-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
Xie, H., Vucetic, S., Iakoucheva, L. M., Oldfield, C. J., Dunker, A. K., Obradovic, Z., & Uversky, V. N. (2007) · Journal of Proteome Research · doi:10.1021/pr060394e · Cited by 382
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Metadata
- Authors
- Uversky, V. N.
- Venue
- Journal of Biomolecular Structure and Dynamics
- Publisher
- Informa UK Limited
- Published
- 2003-10
- Volume
- 21
- Issue
- 2
- Pages
- 211-234
- ISSN
- 0739-1102 (ISSN-L)
- 1538-0254
- OpenAlex
- W2058674503
- Cited by
- 500
- References
- 21
- FWCI
- 9.53
- Type
- journal article
- Language
- en
- Open access
- closed
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- Uversky, V. N. (2003). A Protein-Chameleon: Conformational Plasticity of α-Synuclein, a Disordered Protein Involved in Neurodegenerative Disorders. Journal of Biomolecular Structure and Dynamics. https://doi.org/10.1080/07391102.2003.10506918
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