نتایج جستجو برای: amyloid beta25 35 folding
تعداد نتایج: 244389 فیلتر نتایج به سال:
There is growing interest both from consumers and researchers in the role that berries play in human health. In the experiments reported here, we assessed the ability of anthocyanins and phenolic fractions of Boysenberry and blackcurrant to ameliorate the deleterious effect of the amyloid β25– 35 (100 μmol L−1, 24 h) and dopamine (1 mmol L−1, 4 h) on calcium buffering (recovery) of M1 muscarini...
The solvation shell is essential for the folding and function of proteins, but how it contributes to protein misfolding aggregation has still be elucidated. We show that mobility H2O molecules influences rate amyloid α-synuclein (αSyn), a associated with Parkinson's disease. When within reduced by presence NaCl, αSyn increases. Conversely, in CsI increased reduced. Changing solvent from D2O lea...
Amyloids are highly organized protein filaments, rich in β-sheet secondary structures that self-assemble to form dense plaques in brain tissues affected by severe neurodegenerative disorders (e.g. Alzheimer's Disease). Identified as natural functional materials in bacteria, in addition to their remarkable mechanical properties, amyloids have also been proposed as a platform for novel biomateria...
This mini-review focuses on the processes and consequences of protein folding and misfolding. The latter process often leads to protein aggregation and precipitation with the aggregates adopting either highly ordered (amyloid fibril) or disordered (amorphous) forms. In particular, the amyloid fibril is discussed because this form has gained considerable notoriety due to its close links to a var...
Elucidation of the molecular determinants that drive proteins to aggregate is important both to advance our fundamental understanding of protein folding and misfolding, and as a step towards successful intervention in human disease. Combinatorial strategies enable unbiased and model-free approaches to probe sequence/structure relationships. Through the use of combinatorial methods, it is possib...
Amyloid folds not only represent the underlying cause of a large class of human diseases but also display a variety of functional roles both in prokaryote and eukaryote organisms. Among these roles is a recently-described activity in signal transduction cascades functioning in host defense and programmed cell death and involving Nod-like receptors (NLRs). In different fungal species, prion amyl...
Amyloidosis describes a group of protein folding diseases in which amyloid proteins are abnormally deposited in organs and/or tissues as fine fibrils. Mouse senile amyloidosis is a disorder in which apolipoprotein A-II (apoA-II) deposits as amyloid fibrils (AApoAII) and can be transmitted from one animal to another both by the feces and milk excreted by mice with amyloidosis. Thus, mouse AApoAI...
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