Results 11 to 20 of about 92,941 (293)

Role of Protein Misfolding and Proteostasis Deficiency in Protein Misfolding Diseases and Aging [PDF]

open access: yesInternational Journal of Cell Biology, 2013
The misfolding, aggregation, and tissue accumulation of proteins are common events in diverse chronic diseases, known as protein misfolding disorders.
Karina Cuanalo-Contreras   +2 more
doaj   +3 more sources

Protein Misfolding and Neurodegenerative Diseases [PDF]

open access: yesInternational Journal of Cell Biology, 2014
This special issue includes fifteen reviews and two original research articles by leading scientists in the fields of neuropathology, biochemistry, and cell biology, dealing with the role of protein aggregation and prion-like propagation of protein misfolding in neurodegenerative diseases.
Alessio Cardinale   +2 more
doaj   +3 more sources

Protein Misfolding and Human Disease [PDF]

open access: yesThe Scientific World Journal, 2002
Protein folding is perhaps the most fundamental process associated with the generation of functional structures in biology. There has been considerable progress in the last few years in understanding the underlying principles that govern this highly complex process.
Christopher Dobson
doaj   +3 more sources

Publisher Correction: A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers

open access: yesCommunications Biology, 2021
A Correction to this paper has been published: https://doi.org/10.1038/s42003-021-01680 ...
Rodrigo Cataldi   +15 more
doaj   +1 more source

Protein Misfolding Thermodynamics [PDF]

open access: yesThe 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
openaire   +3 more sources

Oxidative Stress-Induced Misfolding and Inclusion Formation of Nrf2 and Keap1

open access: yesAntioxidants, 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
doaj   +1 more source

Protein Misfolding and Neurodegeneration [PDF]

open access: yesArchives 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.
openaire   +2 more sources

Protein Misfolding and the Serpinopathies [PDF]

open access: yesPrion, 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
openaire   +2 more sources

Molecular and Cellular Basis of Misfolded Proteins in Neurodegenerative Diseases [PDF]

open access: yesInternational 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
doaj   +1 more source

Insights from nature: A review of natural compounds that target protein misfolding in vivo

open access: yesCurrent 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
doaj   +1 more source

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