Results 71 to 80 of about 92,071 (194)
Brazilian Journal of Medical and Biological Research, 2005 In the last few years, hydrostatic pressure has been extensively used in the study of both protein folding and misfolding/aggregation. Compared to other chemical or physical denaturing agents, a unique feature of pressure is its ability to induce subtle ...
S.T. Ferreira +2 more
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The potential role of dietary polyphenols in Parkinson’s disease [PDF]
, 2011 Cumulative evidence now suggests that the abnormal aggregation of the neuronal protein alpha-synuclein is critically involved in the pathogenesis of synucleinopathies, of which Parkinson’s disease (PD) is the most prevalent. Development of neuropathology
Caruana, Mario, Vassallo, Neville
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Polyglutamine neurodegeneration: protein misfolding revisited [PDF]
Trends in Neurosciences, 2008 Polyglutamine diseases are a major cause of neurodegeneration worldwide. Recent studies highlight the importance of protein quality control mechanisms in regulating polyglutamine-induced toxicity. Here we discuss a model of disease pathogenesis that integrates current understanding of the role of protein folding in polyglutamine disease with emerging ...
Aislinn J, Williams, Henry L, Paulson
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Frontiers in Molecular Neuroscience, 2018 Protein quality control (PQC) is critical to maintain a functioning proteome. Misfolded or toxic proteins are either refolded or degraded by a system of temporal quality control and can also be sequestered into aggregates or inclusions by a system of ...
Kara L. Schneider +2 more
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Proteostasis collapse is a driver of cell aging and death. [PDF]
, 2019 What molecular processes drive cell aging and death? Here, we model how proteostasis-i.e., the folding, chaperoning, and maintenance of protein function-collapses with age from slowed translation and cumulative oxidative damage.
de Graff, Adam MR +2 more
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Direct single-molecule observation of calcium-dependent misfolding in human neuronal calcium sensor-1 [PDF]
, 2014 Neurodegenerative disorders are strongly linked to protein misfolding, and crucial to their explication is a detailed understanding of the underlying structural rearrangements and pathways that govern the formation of misfolded states. Here we use single-
Cecconi, Ciro +5 more
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Protein Misfolding and Retinal Degeneration [PDF]
Cold Spring Harbor Perspectives in Biology, 2011 The retina is a highly complex and specialized organ that performs preliminary analysis of visual information. Composed of highly metabolically active tissue, the retina requires a precise and well-balanced means of maintaining its functional activity during extended periods of time.
Radouil, Tzekov +2 more
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Biomolecules, 2020 Many devastating neurodegenerative diseases are driven by the misfolding of normal proteins into a pathogenic abnormal conformation. Examples of such protein misfolding diseases include Alzheimer’s disease, Parkinson’s disease, Huntington’s disease ...
Cristóbal Marrero-Winkens +2 more
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Inhibition of IRE1α-mediated XBP1 mRNA cleavage by XBP1 reveals a novel regulatory process during the unfolded protein response [PDF]
, 2017 Background: The mammalian endoplasmic reticulum (ER) continuously adapts to the cellular secretory load by the activation of an unfolded protein response (UPR).
Bulleid, Neil J. +4 more
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Cotranslational folding of proteins on the ribosome.
, 2020 Many proteins in the cell fold cotranslationally within the restricted space of the polypeptide exit tunnel or at the surface of the ribosome. A growing body of evidence suggests that the ribosome can alter the folding trajectory in many different ways ...
Liutkute, M., Rodnina, M., Samatova, E.
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