Global ETD Search
Search theses and dissertations gathered from participating repositories worldwide. Every result links back to the library that holds it. No account is needed.
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Showing 1 to 20 of 690 for “"amyloid"”.
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Insights into Mechanisms of Amyloid Toxicity: Molecular Dynamics Simulations of the Amyloid andbeta-peptide (Aandbeta) and Islet Amyloid Polypeptide (IAPP)
Aggregation of proteins into amyloid deposits is a common feature among dozens of diseases. Two such diseases that feature amyloid deposits are Alzheimer's disease (AD) and type 2 diabetes (T2D). AD toxicity has been associated with the aggregation and accumulation of the amyloid β-peptide (Aβ); Aβ …
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Role of Whey Protein Amyloid and Amyloid-Like Aggregates in Film Formation
… Umstrukturierung von Proteinen zu funktionellen amyloiden und amyloid-artigen Aggregaten durch thermische Behandlung im sauren Milieu führt zu verbesserten Eigenschaften dieser. Dadurch werden vorteilhafte Einsatzmöglichkeiten in Lebensmittelsystemen mit oberflächenaktiver Relevanz ermöglicht. …
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Cerebral Amyloid Angiopathy-Causing Beta-Amyloid Variants Have Altered Effects on the Clotting System
<p>Cerebral amyloid angiopathy (CAA), where beta-amyloid (Aβ) deposits around cerebral blood vessels, is a major contributor of vascular dysfunction in Alzheimer's disease (AD) patients. However, the molecular mechanism underlying CAA formation and CAA-induced cerebrovascular pathologies, including …
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Amyloid-β and amyloid associated proteins in the pathology and diagnosis of Alzheimer's disease
Contains fulltext : 156484.pdf (Publisher’s version ) (Open Access)
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Molecular Mechanisms in Amyloid Disorders. Novel Treatment Options in Hereditary Cystatin C Amyloid Angiopathy.
… process in Alzheimer’s disease and other amyloid disorders usually involves the transformation of a soluble monomeric protein via potentially toxic oligomers into amyloid fibrils. The structure and properties of the intermediary oligomers have been difficult to study due to their …
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Small Molecules as Amyloid Inhibitors: Molecular Dynamic Simulations with Human Islet Amyloid Polypeptide (IAPP)
Islet amyloid polypeptide (IAPP) is a 37-residue amyloidogenic hormone implicated in the progression of Type II Diabetes (T2D). T2D affects an estimated 422 million people yearly and is a co-morbidity with numerous diseases. IAPP forms toxic oligomers and amyloid fibrils that reduce pancreatic …
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Thermodynamic Characterisation of Amyloid Fibrils
Amyloid fibril related diseases include dementia, Alzheimer’s disease and Parkinsons disease and pose an increasingly large burden to global healthcare, due to the presence of an ageing population. Despite many healthcare advances, amyloid fibril diseases remain largely untreatable, with only …
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Unzipping Amyloid Fibrils: How a Novel Calcium-Binding Protein, NUCB1, Prevents the Formation of Amyloid Fibrils
… we also established novel and unique anti-amyloidogenic functional ability of sNUCB1. We show that Ca<sup>2+</sup>-free sNUCB1 can inhibit fibril formation by highly amyloidogenic human Islet Amyloid PolyPeptide (hIAPP) and Amyloid-β 42 (Aβ42) peptides, as relevant to Type-2 Diabetes and …
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Membrane fragmentation by a 20-29 fragment of human islet amyloid polypeptide and rat amyloid polypeptide
… of insulin-producing pancreatic beta cells. The amyloidogenic human Islet Amyloid Polypeptide (hIAPP, also known as human amylin) is believed to play a crucial role in this biological process. Previous studies have shown that hIAPP forms small aggregates that kill β-cells by disrupting the …
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Folding and aggregation of amyloid peptides
Aggregation of the Amyloid β (Aβ) peptide to amyloid fibrils is associated with the outbreak of Alzheimer’s disease. Early aggregation intermediates in form of soluble oligomers are of special interest as they are believed to be the major toxic components in the process. These oligomers are of …
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Amyloid Fibril Nucleation In Reverse Micelles
The 40-residue amyloid beta protein (Abeta) is the unstructured cleavage product of a common membrane protein that is produced in large quantities, but normally cleared from the brain before it exerts any apparent toxicity. Under some conditions, however, it undergoes a conformational change and …
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Modelling Early Events In Amyloid Aggregation
… of particular significance is the formation of amyloid plaques from normally soluble proteins in several neurodegenerative conditions including Alzheimer’s disease. Traditionally, attention has focused on the proliferation of macroscopic quantities of biofilaments, and experimentalists have …
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Amyloid fibril formation in Alzheimer's disease
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 1993.
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Self-Assembly of Large Amyloid Fibers
Functional amyloids found throughout nature have demonstrated that amyloid fibers are potential industrial biomaterials. This work introduces a new 'template plus adder' cooperative mechanism for the spontaneous self-assembly of micrometer sized amyloid fibers. A short hydrophobic template peptide …
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Nanoscale imaging and characterisation of Amyloid-β
… methods have been applied to the study of the amyloid peptide implicated in the pathogenesis of Alzheimer’s disease (AD). Amyloid-β (Aβ) undergoes a hierarchy of aggregation following a structural transition making it an ideal subject of studying with SPM. The application of SPM based …
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Growth and Toxicity of Amyloid β Polymorphs
… is the accumulation of the protein fragment amyloid β (Aβ) into soluble aggregates or insoluble β-sheet-rich fibrils and plaques in the brain. Limited success in targeting these fibrils and plaques stems from a lack of understanding of the intricate process of Aβ fibrillization. We …
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Biochemical and Structural Studies of Amyloid Proteins
Amyloidogenic neurodegenerative disorders such as Alzheimer’s disease (AD) and Parkinson’s disease (PD) are an important health issue. However, the underlying molecular mechanisms of the disease-related protein aggregates, that are present in humans, are only understood partially. I have used and …
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