2P070 Solubility and Supersaturation-Dependent Protein Misfolding Revealed by Ultrasonication(01C. Protein: Property)
نویسندگان
چکیده
منابع مشابه
Protein misfolding and neurodegeneration.
A key molecular pathway implicated in diverse neurodegenerative diseases is the misfolding, aggregation, and accumulation of proteins in the brain. Compelling evidence strongly supports the hypothesis that accumulation of misfolded proteins leads to synaptic dysfunction, neuronal apoptosis, brain damage, and disease. However, the mechanism by which protein misfolding and aggregation trigger neu...
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The crucial event in the development of transmissible spongiform encephalopathies (TSEs) is the conformational change of a host-encoded membrane protein - the cellular PrP(C) - into a disease associated, fibril-forming isoform PrP(Sc). This conformational transition from the alpha-helix-rich cellular form into the mainly beta-sheet containing counterpart initiates an 'autocatalytic' reaction wh...
متن کاملProtein misfolding diseases
Protein misfolding diseases include highly debilitating degenerative disorders like Alzheimer’s and Parkinson’s diseases [1]. The healthcare and financial burden linked to these pathologies has been steadily increasing over the past decade [2]. Actually, there is currently no efficient treatment for misfolding diseases as well as no reliable early diagnostic techniques for them [3]. It is known...
متن کاملProtein Misfolding and Neurodegenerative Diseases
This special issue includes fifteen reviews and two original research articles by leading scientists in the fields of neu-ropathology, biochemistry, and cell biology, dealing with the role of protein aggregation and prion-like propagation of protein misfolding in neurodegenerative diseases. In the review article " Breaking the code of amyloid-í µí»½ oli-gomers, " available at the following link...
متن کاملProtein Misfolding Diseases.
The majority of protein molecules must fold into defined three-dimensional structures to acquire functional activity. However, protein chains can adopt a multitude of conformational states, and their biologically active conformation is often only marginally stable. Metastable proteins tend to populate misfolded species that are prone to forming toxic aggregates, including soluble oligomers and ...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2013
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.53.s170_4