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 26 for “"Prion-like"”.
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The prion-like properties of assembled human alpha-synuclein
… suggested that some misfolded proteins resemble prions. Thus, aggregated alpha-synuclein shares features of PrPSc, the scrapie form of the prion protein. The aim of this thesis was to further characterize the prion-like properties of aggregated alpha-synuclein by studying the pathways of seeded …
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Single Molecule Fluorescence Studies of Prions and Prion-like Proteins
Prions are infectious agents that cause fatal neurodegenerative diseases in the brain. The wide-accepted protein-only hypothesis states that the misfolded form of prion protein (PrP) is the sole constituent of prions, and the self-propagating process of PrP is considered to play a central role in …
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Characterizing unique features of prion-like domains recruited to stress granules
… of the interactions in this separated phase. Prion-like domains (PrLDs) are domains that compositionally resemble yeast prion domains. Some PrLDs can form solid-state assemblies; however, PrLDs have also been associated with the formation of more liquid-like biomolecular condensates. …
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Prion-like properties of the N-terminal domains of the rat and human FoxG1 transcription factors
… of this study was to investigate the possible prion-like properties of the N-terminal domains of the winged-helix transcription factor FoxG1.
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The Life of Prion: an investigation into the physiological role of a prion-like protein in the nematode Caenorhabditis elegans
For centuries, the threat of prion disease has plagued populations – whether it be in the form of scrapie ravaging through the sheep populations of Spain in the eighteenth century, fatal familial insomnia afflicting families in Italy, or an outbreak of Creutzfeldt-Jakob disease in the UK triggered …
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Prion biology in the context of bacteria
Prions are infectious amyloid aggregates first described in the context of mammalian neurodegenerative diseases collectively known as the transmissible spongiform encephalopathies. Prions have also been uncovered in yeast, where they function as protein-based units of heredity that confer unique …
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Investigating the molecular environments and interactions of pathological TDP-43 filaments
… assembly of native TDP-43, a phenomenon known as prion-like propagation. However, the underlying molecular mechanisms are largely unknown. An understanding of these mechanisms may yield therapeutic strategies to intervene with pathological TDP-43 filament formation to slow or prevent disease …
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Development of the new yeast-based assays for prion properties
Prion is an infectious isoform of a normal cellular protein which is capable of converting the non-prion form of the same protein into the alternative prion form. Mammalian prion protein PrP is responsible for prion formation in mammals, causing a series of fatal and incurable prion diseases. (1) …
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Characterization of Tau Oligomeric Strains: Implications for Disease Phenotypes
… found that small, oligomeric aggregates are likely the most toxic species. I found that toxic tau oligomers are elevated in progressive supranuclear palsy, traumatic brain injury and synucleinopathy models and reversal of toxicity can be achieved with treatment of a tau oligomer-specific …
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Characterization of The Roles of Carma3 and Bcl10 In Virus-Triggered Rig-I/Mavs Signaling Pathway
… by mitochondrial protein MAVS, which forms a prion-like structure to recruit TBK1and IKK complex to activate IRF3 and NF-κB, respectively. Herein, we revealed the important roles of CARMA3 and BCL10 in RIG-I/MAVS signaling pathway for the first time. CARMA3 or BCL10 deficient cells exhibited …
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Molecular Basis of Mammalian Prion Protein Misfolding
Prions are aberrantly folded proteins that are able to self-propagate their abnormal conformation using the normally folded protein as substrate. In mammals, the only known prion protein is PrP. The misfolding of PrP is a key event underlying Transmissible Spongiform Encephalopaties (TSEs), fatal …
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Parallels and Divergences in Multisystem Proteinopathy Genes: Stress Granules, Autophagy, and Myogenic Deficits
… autophagy adaptors (SQSTM1, VCP, OPTN) and prion-like domain containing stress granule proteins (HNRNPA2B1, HNRNPA1, MATR3, TIA1). Previous studies identified that a non-pathogenic variant of the non-classical MSP protein, TIA1 N357S , can act as a phenotype modifier with SQSTM1P392L leading …
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Interaction studies of the cellular prion protein
Prion diseases are rare but fatal neurodegenerative diseases which occur both in humans and mammals caused by the prion protein (PrP) which is well conserved among the species. In this thesis the biochemical properties and the function of prion protein were investiagted using different methods. The …
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Role of Drosophila Orb2 (CPEB) in Synaptic Protein Synthesis
… biophysical properties that are associated with prion-like proteins. They exist in two distinct physical states: a monomeric and a dominant self-sustaining amyloidogenic aggregated state. This suggested a model in which a transient experience creates persistence molecular alteration in the …
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The Mechanisms of Tau Entry to the Cytosol
… to transit between cells of the brain in a ‘prion-like’ manner, resulting in templated aggregation of native tau in recipient neurons. Interactions between tau assemblies, surface receptor LRP1 and heparan sulphate proteoglycans promote the uptake of tau assemblies to membrane-bound vesicles. …
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Biomolecular Condensates Through a Computational Microscope Design, Mechanisms and Implications
… of the resulting coaservates. By examining prion-like domains, I show how specific residue identities modulate the phase behaviour by altering the interaction landscape. Similarly, in CTPR-based constructs and chromatin arrays, valency also emerges as a key determinant of stability, linking …
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Chemical Footprinting of Polymeric Structure of hnRNPA2 Low Complexity Domain
… number of amino acids and have been termed prion-like, intrinsically disordered or low complexity domains. These low complexity sequences have been shown to induce phase transition in low salt buffer. When incubated at high concentration, certain of these low complexity domains polymerize …
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Mechanism of aggregation of oxidation-mimicking mutants of human [gamma]D-crystallin
… aggregation of wild-type or undamaged ones in a prion-like manner, we examined aggregation in WT/mutant mixtures. Surprisingly, the result was "inverse prion" behavior: WT [gamma]D crystallin specifically promoted aggregation of its W42Q/R mutants without detectably coaggregating with them. …
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A genetic platform for the study of protein perturbation and prion-based inheritance
… or degradation. I applied yTRAP to track yeast prions, which have previously been difficult to study due to a lack of simple and reliable reporters. Prions are protein-based elements of inheritance that have profound implications for the evolution of single-celled organisms. I first utilized …
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Discovery and characterization of prions in Saccharomyces cerevisiae
… reaction. These aggregates, or prions, are the infectious agents behind diseases like Kuru and mad-cow disease. In yeast, however, prions act as epigenetic elements that confer heritable alternative phenotypes. Prion-forming proteins create bistable molecular systems whose …
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