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2016
When proteins do not fold correctly, it can lead to very serious diseases. One such group of diseases is the amyloid diseases, of which Alzheimer’s disease (AD), Parkinson’s disease, and type 2 diabetes mellitus (T2DM) are members. The amyloid diseases are characterized by the aggregation of a specific protein into amyloid fibrils. During this process,
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When proteins do not fold correctly, it can lead to very serious diseases. One such group of diseases is the amyloid diseases, of which Alzheimer’s disease (AD), Parkinson’s disease, and type 2 diabetes mellitus (T2DM) are members. The amyloid diseases are characterized by the aggregation of a specific protein into amyloid fibrils. During this process,
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Amyloid Oligomers, Protofibrils and Fibrils
2019Amyloid diseases are of major concern all over the world due to a number of factors including: (i) aging population, (ii) increasing life span and (iii) lack of effective pharmacotherapy options. The past decade has seen intense research in discovering disease-modifying multi-targeting small molecules as therapeutic options.
Mohammad Khursheed, Siddiqi +4 more
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Amyloid Neuropathy: Relationship between Amyloid Fibrils and Macrophages
Ultrastructural Pathology, 1984A case of amyloid neuropathy associated with a multiple myeloma IgG light chain is reported. Under light microscopy the peripheral nerve exhibited several amyloid deposits. Electron microscopy revealed numerous amyloid deposits; at their periphery, macrophagic histiocytes were observed, containing a few tufts of parallel fibrils in their cytoplasm.
A, Vital, C, Vital
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Mesoscopic Properties of Semiflexible Amyloid Fibrils
Langmuir, 2004We have determined the contour length, persistence length, bending rigidity, and critical percolation concentration for semiflexible amyloid fibrils formed from the globular proteins beta-lactoglobulin, bovine serum albumin, and ovalbumin. The persistence length was estimated using an adjusted random contact model for highly charged semiflexible chains.
Sagis, L.M.C. +2 more
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Biotechnological applications of amyloid fibrils
Protein aggregates and amyloid fibrils have special qualities and are used in a variety of biotechnological applications. They are extensively employed in bioremediation, biomaterials, and biocatalysis. Because of their capacity to encapsulate and release pharmaceuticals and their sensitivity to certain molecules, respectively, they are also used in ...Mohsen, Nabi Afjadi +3 more
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Inhibitors of amyloid fibril formation
Many diseases are caused by misfolded and denatured proteins, leading to neurodegenerative diseases. In recent decades researchers have developed a variety of compounds, including polymeric inhibitors and natural compounds, antibodies, and chaperones, to inhibit protein aggregation, decrease the toxic effects of amyloid fibrils, and facilitate ...Elaheh, Tavili +2 more
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Factors influencing amyloid fibril formation
Protein aggregation is a complex process with several stages that lead to the formation of complex structures and shapes with a broad variability in stability and toxicity. The aggregation process is affected by various factors and environmental conditions that disrupt the protein's original state, including internal factors like mutations, expression ...Fereshteh Ramezani, Khorsand +2 more
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Amyloid fibrils in FTLD-TDP are composed of TMEM106B and not TDP-43
Nature, 2022Yi Xiao Jiang, Qin Cao, Michael R Sawaya
exaly