Protein Misfolded Oligomers: Experimental Approaches, Mechanism of Formation, and Structure-Toxicity Relationships
نویسندگان
چکیده
منابع مشابه
Structure-Toxicity Relationships of Amyloid Peptide Oligomers
The accumulation of misfolded proteins as insoluble, fibrillar aggregates is characteristic of several degenerative diseases. Examples include the proteins involved in amyloid diseases such as Alzheimer’s disease (Aβ) (Glenner and Wong 1984), type II diabetes (amylin) (Cooper et al. 1987) and Parkinson’s disease (α-synuclein) (Spillantini et al. 1997), as well as the mammalian prion diseases (P...
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Formation and Toxicity of Soluble Polyglutamine Oligomers in Living Cells
BACKGROUND Aggregation and cytotoxicity of mutant proteins containing an expanded number of polyglutamine (polyQ) repeats is a hallmark of several diseases, including Huntington's disease (HD). Within cells, mutant Huntingtin (mHtt) and other polyglutamine expansion mutant proteins exist as monomers, soluble oligomers, and insoluble inclusion bodies (IBs). Determining which of these forms const...
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Chaperones have long been recognized to play well defined functions such as to: (i) assist protein folding and promote formation and maintenance of multisubunit complexes; (ii) mediate protein degradation; (iii) inhibit protein aggregation; and (iv) promote disassembly of undesired aberrant protein aggregates. In addition to these well-established functions, it is increasingly clear that chaper...
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Amyloid-beta (Aβ) peptide oligomers are believed to be the causative agents of Alzheimer's disease (AD). Though post-mortem examination shows that insoluble fibrils are deposited in the brains of AD patients in the form of intracellular (tangles) and extracellular (plaques) deposits, it has been observed that cognitive impairment is linked to synaptic dysfunction in the stages of the illness we...
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ژورنال
عنوان ژورنال: Chemistry & Biology
سال: 2012
ISSN: 1074-5521
DOI: 10.1016/j.chembiol.2012.02.003