Evidence of Native α-Synuclein Conformers in the Human Brain
| Autor: | Harry Ischiropoulos, Benoit I. Giasson, Kristen A. Malkus, Richard Lightfoot, Danielle Emille Mor, Neal S. Gould |
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| Rok vydání: | 2014 |
| Předmět: |
Protein Folding
Sucrose animal diseases Plasma protein binding Biochemistry Mass Spectrometry Epitope Epitopes chemistry.chemical_compound Protein structure mental disorders medicine Native state Humans Molecular Biology Alpha-synuclein Brain Hydrogen Bonding Neurodegenerative Diseases Parkinson Disease Cell Biology Human brain nervous system diseases Protein Structure Tertiary Epitope mapping medicine.anatomical_structure nervous system chemistry Chromatography Gel alpha-Synuclein Protein folding Ultracentrifugation Epitope Mapping Reports Protein Binding |
| Zdroj: | Journal of Biological Chemistry. 289:7929-7934 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.c113.538249 |
| Popis: | α-Synuclein aggregation is central to the pathogenesis of several brain disorders. However, the native conformations and functions of this protein in the human brain are not precisely known. The native state of α-synuclein was probed by gel filtration coupled with native gradient gel separation, an array of antibodies with non-overlapping epitopes, and mass spectrometry. The existence of metastable conformers and stable monomer was revealed in the human brain. |
| Databáze: | OpenAIRE |
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