Results 11 to 20 of about 53,939 (158)
Editorial: Protein misfolding, altered mechanisms and neurodegeneration [PDF]
Frontiers in Molecular Neuroscience, 2023 Neha Gogia +7 more
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A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers
Communications Biology, 2021 Cataldi et al. investigates the impact of the dopamine derivative DOPAL on the Aβ peptide oligomer formation. They report that DOPAL promotes the formation of stable Aβ oligomers that exert toxicity on neuroblastoma cells by increasing cytosolic calcium ...
Rodrigo Cataldi +15 more
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Publisher Correction: A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers
Communications Biology, 2021 A Correction to this paper has been published: https://doi.org/10.1038/s42003-021-01680 ...
Rodrigo Cataldi +15 more
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Protein Misfolding Thermodynamics [PDF]
The Journal of Physical Chemistry Letters, 2019 It is known that protein misfolding is governed by the hydrophobic effect of solutes at hydrophobic amino acid side chains. The hydrophobic force of nonaqueous solutes acts as a driving force for the spatial rearrangement of protein side chains, whose structural transitions need to be regulated in both time and space.
Md Mozzammel Haque, Richard Bayford
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Oxidative Stress-Induced Misfolding and Inclusion Formation of Nrf2 and Keap1
Antioxidants, 2022 Cells that experience high levels of oxidative stress respond by inducing antioxidant proteins through activation of the protein transcription factor nuclear factor erythroid 2-related factor 2 (Nrf2).
Vy Ngo +4 more
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Protein Misfolding and Neurodegeneration [PDF]
Archives of Neurology, 2008 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.
Soto, Claudio, Estrada, Lisbell D.
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Protein Misfolding and the Serpinopathies [PDF]
Prion, 2007 The serpins are the largest superfamily of protease inhibitors. They are found in almost all branches of life including viruses, prokaryotes and eukaryotes. They inhibit their target protease by a unique mechanism that involves a large conformational transition and the translocation of the enzyme from the upper to the lower pole of the protein.
Didier, Belorgey +3 more
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Molecular and Cellular Basis of Misfolded Proteins in Neurodegenerative Diseases [PDF]
International Clinical Neuroscience Journal, 2022 Background: Neurodegeneration is characterized by a progressive loss of nerve structure and function which lead to cognitive impairment such as dementia.
Alireza Zali +3 more
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Insights from nature: A review of natural compounds that target protein misfolding in vivo
Current Research in Biotechnology, 2020 Protein misfolding is fundamental to a number of human disorders including Alzheimer’s disease, prion diseases, Parkinson’s disease and type 2 diabetes mellitus. To date, there are still no cures for protein misfolding disorders.
Cassandra Terry
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Prion Protein Misfolding [PDF]
Current Molecular Medicine, 2009 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 ...
Kupfer, L, Hinrichs, W, Groschup, M.H
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