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 9 of 9 for “"Protein oligomers"”.
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Improving Biocompatibility By Controlling Protein Adsorption: Modification And Design Of Biomaterials Using Poly(Ethylene Glycol) Microgels And Microspheres
… responses are initially elicited and directed by proteins that adsorb from this multicomponent solution to form thin films on their surfaces. The identity, conformation, and quantity of adsorbed proteins are related to the properties of a material's surface. For example, hydrophobic surfaces tend …
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Neuronal Protection by a Novel C-terminal Hsp90 Modulator
… by accumulation of misfolded and aggregated proteins, indicating that the protein quality control machinery is compromised. Enhancing the activity of molecular chaperones such as the `heat shock' proteins (Hsp's) that re-fold or signal degradation of damaged proteins may help remove protein …
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Mechanisms Behind the Chaperone Activity of Nucleic Acids
… the interplay between nucleic acids and protein aggregation is integral to the understanding of proteostasis, aging, and neurodegenerative disease progression. Nucleic acids are known to modulate the aggregation of PrP, tau, ⍺-synuclein, and other disease relevant proteins. Although the …
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Mitigating protein aggregation to reduce the toxicity inherent to Parkinson’s and Alzheimer’s diseases
Protein deposition in the form of amyloid fibrils is the hallmark of more than 40 human pathologies, including Alzheimer’s disease (AD) and Parkinson’s disease (PD). Misfolded protein oligomers formed as intermediates during the aggregation process have been strongly implicated in the onset and …
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Proteomics studies of protein homeostasis and aggregation in ageing and neurodegeneration
Upon ageing, a progressive disruption of protein homeostasis often leads to extensive protein aggregation and neurodegeneration. It is therefore important to study at the proteome level the origins and consequences of such disruption, which so far have remained elusive. Addressing this problem has …
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Mechanisms of Adsorption and Surface-Mediated Aggregation of Intrinsically Disordered Protein Tau at Model Surfaces
… of an intrinsically disordered soluble protein, tau, into insoluble filaments is a defining hallmark of many neurodegenerative diseases, commonly referred to as tauopathies. In its native state, the protein tau’s function is to promote the assembly, and aid in the stabilization of …
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Molecular interactions and their impact on life sciences
… binding and thermodynamics of small heat shock proteins, such as clusterin, αB-crystallin and the Brichos chaperone domain, to aggregated forms of amyloid-beta and α-synuclein, protein aggregates that are associated with a wide range of neurodegenerative diseases. The three chaperones are …
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Drug discovery for misfolding diseases using structure-based iterative learning
… intermediate aggregate species, termed misfolded oligomers. Fibrils assume different structural polymorphs depending on the synucleinopathy, likely due to the different locations of the nervous system that these diseases occur within. Each tissue has an associated set of specific conditions which …
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Nanolithography and nanoscopy methods for the study of biological samples in confined spaces
… to the group of amyloid pathologies also called protein misfolding diseases. Since the first discovery of amyloid fibrils of the aggregated protein tau in inclusion of Alzheimer brains samples, research has focussed on how amyloids form and their biological relevance in neurodegenerative …