Results 151 to 160 of about 92,071 (194)
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Protein folding and misfolding
Nature, 2003The manner in which a newly synthesized chain of amino acids transforms itself into a perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence and on multiple contributing influences from the crowded cellular milieu.
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Nature Reviews Drug Discovery, 2010
Two recent deals highlight growing interest in therapeutically targeting protein misfolding to treat both rare and common diseases.
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Two recent deals highlight growing interest in therapeutically targeting protein misfolding to treat both rare and common diseases.
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Protein misfolding in neurodegenerative diseases
Neuropathology and Applied Neurobiology, 2004A common pathogenic mechanism shared by diverse neurodegenerative disorders, like Alzheimer's disease, Parkinson's disease, Huntington's disease and transmissible spongiform encephalopathies, may be altered protein homeostasis leading to protein misfolding and aggregation of a wide variety of different proteins in the form of insoluble fibrils ...
E I, Agorogiannis +3 more
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Protein degradation, aggregation, and misfolding
Movement Disorders, 2010AbstractThe cellular surveillance systems guarantee proper removal of altered components from inside cells. Alterations of these systems in neurons have been proposed to be involved in the pathogenesis of different neurodegenerative disorders. In this review, we comment on the advances in our current understanding of how changes in the intracellular ...
Ana Maria, Cuervo +2 more
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Principles of Protein Misfolding
2008Publisher Summary This chapter discusses the principles of protein misfolding. The process of incorrect folding is called “protein misfolding.” It is associated with a number of pathological states in humans, collectively termed “protein-misfolding diseases.” Among these protein-misfolding diseases, amyloid diseases are characterized by the presence ...
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Atherosclerosis: another protein misfolding disease?
Trends in Molecular Medicine, 2002The secondary structure and conformation of apo-B 100 in low-density lipoproteins (LDL) are imposed by lipid-protein interactions and dynamics, and affected by the introduction or removal of lipids during the course of lipoprotein metabolism. Following an alteration of the water-lipid interface as a result of, for example, oxidation of lipids, the ...
URSINI, FULVIO +4 more
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Protein Misfolding and Human Disease
Annual Review of Genomics and Human Genetics, 2006Protein misfolding is a common event in living cells. In young and healthy cells, the misfolded protein load is disposed of by protein quality control (PQC) systems. In aging cells and in cells from certain individuals with genetic diseases, the load may overwhelm the PQC capacity, resulting in accumulation of misfolded proteins.
Gregersen, Niels +3 more
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Annual Review of Biochemistry, 2017
The majority of protein molecules must fold into defined three-dimensional structures to acquire functional activity. However, protein chains can adopt a multitude of conformational states, and their biologically active conformation is often only marginally stable.
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The majority of protein molecules must fold into defined three-dimensional structures to acquire functional activity. However, protein chains can adopt a multitude of conformational states, and their biologically active conformation is often only marginally stable.
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Nanoimaging for protein misfolding diseases
WIREs Nanomedicine and Nanobiotechnology, 2010AbstractMisfolding and aggregation of proteins are widespread phenomena leading to the development of numerous neurodegenerative disorders such as Parkinson's, Alzheimer's, and Huntington's diseases. Each of these diseases is linked to structural misfolding and aggregation of a particular protein.
Lyubchenko, Yuri L. +3 more
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Protein misfolding, evolution and disease
Trends in Biochemical Sciences, 1999I acknowledge very valuable discussions on this article with John Ellis and Carol Robinson. I am grateful to Jose Jiminez and Helen Saibil for providing Figure 3Figure 3 and to Adam Rostom for producing Figure 1Figure 1. This paper is a contribution from the Oxford Centre for Molecular Sciences, which is funded by the BBSRC, EPSRC and MRC. The research
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