The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Biochemical Characterization of the Core Structure of α-Synuclein Filaments
Open accessAbstract
Intracellular filamentous aggregates comprised of alpha-synuclein such as Lewy bodies and glial cytoplasmic inclusions are the defining hallmarks of a subset of neurodegenerative diseases including Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy. We have analyzed biochemical and structural properties of alpha-synuclein filaments assembled in vitro or extracted from brains of patients with multiple system atrophy and found that both types of filaments are insoluble to detergents and partially resistant to proteinase K digestion. Immunoelectron microscopy and immunoblot analysis showed that both amino and carboxyl termini of alpha-synuclein in in vitro assembled filaments were degraded by proteinase K treatment, whereas the central portion of alpha-synuclein is resistant to proteinase K and retains filamentous structures. Protein sequencing and mass spectrometric analyses of the proteinase K-resistant, minimal fragment of 7 kDa revealed that amino acid residues 31-109 of alpha-synuclein constitute the core unit of the filaments. These observations suggest that the central half of the alpha-synuclein polypeptide, containing five tandem repeats as well as a part of the carboxyl-terminal acidic region, forms the core structure of alpha-synuclein filaments, which is coated by the amino- and carboxyl-terminal portions at the periphery.
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Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
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Self-citationα-Synuclein is phosphorylated in synucleinopathy lesions
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Evidence for a Partially Folded Intermediate in α-Synuclein Fibril Formation
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Chiti, F., & Dobson, C. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045115 · Cited by 2,629
Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein
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Structures of α-synuclein filaments from multiple system atrophy
Schweighauser, M., Shi, Y., Tarutani, A., Kametani, F., Murzin, A. G., Ghetti, B., Matsubara, T., Tomita, T., Ando, T., Hasegawa, K., et al. (2020) · Nature · doi:10.1038/s41586-020-2317-6 · Cited by 789
Self-citationDistinct α-Synuclein Strains Differentially Promote Tau Inclusions in Neurons
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Metadata
- Authors
- Miake, H., Mizusawa, H., Iwatsubo, T., & Hasegawa, M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-05
- Volume
- 277
- Issue
- 21
- Pages
- 19213-19219
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1977846417
- Cited by
- 260
- References
- 35
- FWCI
- 6.07
- Type
- journal article
- Language
- en
- Open access
- hybrid
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