Results 31 to 40 of about 160,241 (252)

Nucleation of Polymorphic Amyloid Fibrils [PDF]

open access: yesBiophysical Journal, 2015
One and the same protein can self-assemble into amyloid fibrils with different morphologies. The phenomenon of fibril polymorphism is relevant biologically because different fibril polymorphs can have different toxicity, but there is no tool for predicting which polymorph forms and under what conditions.
openaire   +4 more sources

Significance of Oligomeric and Fibrillar Species in Amyloidosis: Insights into Pathophysiology and Treatment

open access: yesMolecules, 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

The Association of an Elastase with Amyloid Fibrils

open access: yesExperimental 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]

open access: yes, 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   +15 more
core   +1 more source

Quercetin Disaggregates Prion Fibrils and Decreases Fibril-Induced Cytotoxicity and Oxidative Stress

open access: yesPharmaceutics, 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

An Imaging and Systems Modeling Approach to Fibril Breakage Enables Prediction of Amyloid Behavior [PDF]

open access: yes, 2013
Delineating the nanoscale properties and the dynamic assembly and disassembly behaviors of amyloid fibrils is key for technological applications that use the material properties of amyloid fibrils, as well as for developing treatments of amyloid ...
Xue, Wei-Feng   +3 more
core   +1 more source

Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers

open access: yesMolecular 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

Bacterial inclusion bodies contain amyloid-like structure. [PDF]

open access: yesPLoS 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
doaj   +1 more source

Illuminating amyloid fibrils: Fluorescence-based single-molecule approaches

open access: yesComputational 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
doaj   +1 more source

Amyloid tracers detect multple binding sites in Alzheimer´s disease brain tissue. [PDF]

open access: yes, 2013
Imaging fibrillar amyloid-β deposition in the human brain in vivo by positron emission tomography has improved our understanding of the time course of amyloid-β pathology in Alzheimer’s disease. The most widely used amyloid-β imaging tracer so far is 11C-
Nordberg, A,   +9 more
core   +1 more source

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