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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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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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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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C-reactive protein: the nexus between inflammation and protein misfolding diseases [PDF]
Frontiers in ImmunologyC-reactive protein (CRP), an acute-phase protein primarily produced by hepatocytes in response to pro-inflammatory cytokines, is a widely used clinical marker for inflammation and tissue damage. In its native state, CRP exists in a stable pentameric form
Abhishek Roy +19 more
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Protein misfolding disorders and macroautophagy [PDF]
Current Opinion in Cell Biology, 2011 A large group of diseases, termed protein misfolding disorders, share the common feature of the accumulation of misfolded proteins. The possibility of a common mechanism underlying either the pathogenesis or therapy for these diseases is appealing. Thus, there is great interest in the role of protein degradation via autophagy in such conditions where ...
Menzies, Fiona M +2 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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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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Editorial: Protein misfolding, altered mechanisms and neurodegeneration [PDF]
Frontiers in Molecular Neuroscience, 2023 Neha Gogia +7 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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