The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Release of long-range tertiary interactions potentiates aggregation of natively unstructured α-synuclein
Open accessAbstract
In idiopathic Parkinson's disease, intracytoplasmic neuronal inclusions (Lewy bodies) containing aggregates of the protein α-synuclein (αS) are deposited in the pigmented nuclei of the brainstem. The mechanisms underlying the structural transition of innocuous, presumably natively unfolded, αS to neurotoxic forms are largely unknown. Using paramagnetic relaxation enhancement and NMR dipolar couplings, we show that monomeric αS assumes conformations that are stabilized by long-range interactions and act to inhibit oligomerization and aggregation. The autoinhibitory conformations fluctuate in the range of nanoseconds to micro-seconds corresponding to the time scale of secondary structure formation during folding. Polyamine binding and/or temperature increase, conditions that induce aggregation in vitro , release this inherent tertiary structure, leading to a completely unfolded conformation that associates readily. Stabilization of the native, autoinhibitory structure of αS constitutes a potential strategy for reducing or inhibiting oligomerization and aggregation in Parkinson's disease.
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Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
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
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Cited by
-Synuclein in Parkinson's Disease
Stefanis, L. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009399 · Cited by 1,446
Structural Polymorphism of 441-Residue Tau at Single Residue Resolution
Mukrasch, M. D., Bibow, S., Korukottu, J., Jeganathan, S., Biernat, J., Griesinger, C., Mandelkow, E., & Zweckstetter, M. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000034 · Cited by 652
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
Bernadó, P., Blanchard, L., Timmins, P., Marion, D., Ruigrok, R. W. H., & Blackledge, M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506202102 · Cited by 441
Karpinar, D. P., Balija, M. B. G., Kügler, S., Opazo, F., Rezaei‐Ghaleh, N., Wender, N., Kim, H., Taschenberger, G., Falkenburger, B. H., Heise, H., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.257 · Cited by 432
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Metadata
- Authors
- Bertoncini, C. W., Jung, Y.-S., Fernandez, C. O., Hoyer, W., Griesinger, C., Jovin, T. M., & Zweckstetter, M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2005-01-25
- Volume
- 102
- Issue
- 5
- Pages
- 1430-1435
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1680110353
- Cited by
- 790
- References
- 4
- FWCI
- 21.18
- Type
- journal article
- Language
- en
- Open access
- green
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- Bertoncini, C. W., Jung, Y.-S., Fernandez, C. O., Hoyer, W., Griesinger, C., Jovin, T. M., & Zweckstetter, M. (2005). Release of long-range tertiary interactions potentiates aggregation of natively unstructured α-synuclein. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0407146102
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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