Results 11 to 20 of about 92,071 (194)
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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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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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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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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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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Highly efficient protein misfolding cyclic amplification. [PDF]
PLoS Pathogens, 2011 Protein misfolding cyclic amplification (PMCA) provides faithful replication of mammalian prions in vitro and has numerous applications in prion research.
Nuria Gonzalez-Montalban +6 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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Molecular dynamics as an approach to study prion protein misfolding and the effect of pathogenic mutations [PDF]
, 2011 Computer simulation of protein dynamics offers unique high-resolution information that complements experiment. Using experimentally derived structures of the natively folded prion protein (PrP), physically realistic dynamics and conformational changes ...
Daggett, Valerie, van der Kamp, Marc W
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Frontiers in Neuroscience, 2020 Background: Amyotrophic lateral sclerosis (ALS) is a rapidly progressive fatal neurodegenerative condition. There are no effective treatments. The only globally licensed medication, that prolongs life by 2–3 months, was approved by the FDA in 1995.
Elizabeth Elliott +27 more
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