Results 41 to 50 of about 288,605 (343)
Comparing the folding and misfolding energy landscapes of phosphoglycerate kinase. [PDF]
, 2011 Partitioning of polypeptides between protein folding and amyloid formation is of outstanding pathophysiological importance. Using yeast phosphoglycerate kinase as model, here we identify the features of the energy landscape that decide the fate of the ...
Gottfried Köhler +8 more
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Molecules, 2021 Amyloidosis is a term referring to a group of various protein-misfolding diseases wherein normally soluble proteins form aggregates as insoluble amyloid fibrils.
Haruki Koike +3 more
doaj +1 more source
Bacterial inclusion bodies contain amyloid-like structure. [PDF]
PLoS Biology, 2008 Protein aggregation is a process in which identical proteins self-associate into imperfectly ordered macroscopic entities. Such aggregates are generally classified as amorphous, lacking any long-range order, or highly ordered fibrils. Protein fibrils can
Lei Wang +4 more
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Illuminating amyloid fibrils: Fluorescence-based single-molecule approaches
Computational and Structural Biotechnology Journal, 2021 The aggregation of proteins into insoluble filamentous amyloid fibrils is a pathological hallmark of neurodegenerative diseases that include Parkinson’s disease and Alzheimer’s disease.
Lauren J. Rice +2 more
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The Association of an Elastase with Amyloid Fibrils
Experimental Biology and Medicine, 1986 The fibrils of all systemic forms of amyloid (primary, AL; secondary, AA; and hereditary, AF) that had been isolated by the water extraction procedure demonstrated elastolytic enzyme activity when examined in a specific assay using tritiated elastin.
M, Skinner +5 more
openaire +2 more sources
Aggregation modulators interfere with membrane interactions of beta2-microglobulin fibrils. [PDF]
, 2013 Amyloid fibril accumulation is a pathological hallmark of several devastating disorders, including Alzheimer's disease, prion diseases, type II diabetes, and others.
Xue, Wei-Feng +16 more
core +1 more source
Quercetin Disaggregates Prion Fibrils and Decreases Fibril-Induced Cytotoxicity and Oxidative Stress
Pharmaceutics, 2020 Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases caused by misfolding and aggregation of prion protein (PrP). Previous studies have demonstrated that quercetin can disaggregate some amyloid fibrils, such as amyloid β ...
Kun-Hua Yu, Cheng-I Lee
doaj +1 more source
Supersaturation-Dependent Formation of Amyloid Fibrils
Molecules, 2022 The supersaturation of a solution refers to a non-equilibrium phase in which the solution is trapped in a soluble state, even though the solute’s concentration is greater than its thermodynamic solubility. Upon breaking supersaturation, crystals form and the concentration of the solute decreases to its thermodynamic solubility. Soon after the discovery
Yuji Goto +3 more
openaire +3 more sources
Molecular Neurodegeneration, 2007 Background Amyloid-related degenerative diseases are associated with the accumulation of misfolded proteins as amyloid fibrils in tissue. In Alzheimer disease (AD), amyloid accumulates in several distinct types of insoluble plaque deposits, intracellular
Rasool Suhail +13 more
doaj +1 more source
Proceedings of the National Academy of Sciences of the United States of America, 2019 Significance Lewy bodies (LBs), which mainly consist of α-syn, are neuropathological hallmarks of patients with Parkinson’s disease (PD). Recently, it has been reported that aggregates of α-syn with cross-β structures are capable of propagating within ...
Katsuya Araki +8 more
semanticscholar +1 more source