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 163 for “"misfolding"”.
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Investigation Into Protein Folding and Misfolding
… into its native structure and the second is misfolding into an amyloid fibril structure. In the first-half of this work, we investigated the folding of the BI domain of the <em>Streptococcal</em> immunoglobulin-binding domain of protein G (GB1) as our model system. Using bioinformatics …
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Understanding collagen-l folding and misfolding
Chapter One: Introduction to Type I Collagen and Osteogenesis Imperfecta Collagen-I is the primary proteinaceous component of skin, bone, and tendon. Disruptions in collagen-I homeostasis, typically due to non-synonymous mutations in collagen-- encoding genes, cause a variety of severe incurable …
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Molecular Basis of Mammalian Prion Protein Misfolding
… the only known prion protein is PrP. The misfolding of PrP is a key event underlying Transmissible Spongiform Encephalopaties (TSEs), fatal neurological disorders that affect many mammalian species. A self-propagating abnormally folded PrP is believed to be the essential component within …
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Chemical Modification Methods for Protein Misfolding Studies
Protein misfolding is the basis of various human diseases, including Parkinson’s disease, Alzheimer’s disease and Type 2 diabetes. When a protein misfolds, it adopts the wrong three dimensional structures that are dysfunctional and sometime pathological. Little structural details are known about …
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On the Kinetics of Protein Misfolding and Aggregation
Protein (mis)folding into highly ordered, fibrillar structures, amyloid fibrils, is a hallmark of several, mainly neurodegenerative, disorders. The mechanism of this supra-molecular self-assembly reaction, as well as its relationship to protein folding are not well understood. In particular, the …
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Thiol-Based Misfolding: Linking Redox Balance to Cytosolic Proteostasis
… proteins identified as redox-active are prone to misfolding and aggregation by thiol-specific stress. Perhaps these redox-sensitive proteins are those unknown targets. My work has determined that changes in cytosolic redox balance via thiol-specific stresses including cadmium, diamide, and glucose …
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Transthyretin Amyloidosis: Proteolytic cleavage accelerates G53A TTR misfolding and aggregation
… detected in vivo, suggesting alternative TTR misfolding and aggregation mechanisms. The main component of the fibrils was the residue 49-127 fragment. In the proceeding studies, the misfolding and aggregation of G53A TTR, whose mutation is nearby the K48-T49 peptide bond and also associated …
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Understanding protein misfolding diseases through the development of biophysical methods
… This disease is associated with the aberrant misfolding and aggregation of the Aβ peptide into amyloid plaques in the brains of affected individuals. Despite substantial progress in the understanding of the mechanism of aggregation of Aβ, the variety of ways in which imbalances in brain …
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Drug discovery for misfolding diseases using structure-based iterative learning
… I then sought to expand into other protein misfolding areas to demonstrate their generalisability as described in Chapter 5. The aggregation of tau into amyloid fibrils is associated with Alzheimer’s disease and related tauopathies. Similarly to synucleinopathies, different tauopathies are …
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Protein misfolding toxicity and inclusion formation in cellular models of neurodegeneration
Protein misfolding characterizes most neurodegenerative diseases. Protein misfolding is the conversion of specific proteins from their normal, often soluble, and native three-dimensional conformation into an aberrant, often insoluble, non-functional conformation. Protein inclusions and aggregates …
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Deciphering The Role of Hsp110 Chaperones In Diseases of Protein Misfolding
<p>Molecular chaperones maintain protein homeostasis (proteostasis) by ensuring the proper folding of polypeptides. Loss of proteostasis has been linked to the onset of numerous neurodegenerative disorders including Alzheimer’s, Parkinson’s, and Huntington’s disease. Hsp110 is a member of the Hsp70 …
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Regulation of the redox homeostasis during polyglutamine misfolding in Huntington’s Disease
… diseases that are associated with protein misfolding, aggregation and oxidative stress. While several changes in the redox homeostasis have been shown to occur in HD animal models and HD brains, the formal relationships between intracellular protein misfolding that occurs in HD, redox …
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The unfolded protein response and HLA-B27 misfolding: implications for ankylosing spondylitis
The unfolded protein response (UPR) detects the presence of misfolded proteins in the endoplasmic reticulum (ER) and subsequently relieves ER stress by increasing the folding capacity of the ER. The secretory pathway substrate HLA-B27 is highly associated with the chronic inflammatory disease …
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Molecular origins of tissue vulnerability to aberrant aggregation in protein misfolding diseases
… the potential to be applied to other protein misfolding diseases, in the brain and beyond.
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Using cannabidiol and trazodone to treat protein misfolding neurodegenerative disease in C. elegans
Alzheimer's disease is one of the most common neurodegenerative disorders and is typically characterized by the accumulation of the misfolded proteins Amyloid-Beta (Aβ1-42) and/or hyperphosphorylation of Tau (p-Tau). Despite the lack of a cure for the disease, it is well known that targeting …
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Use of the Protein Misfolding Cyclic Amplification for food safety and drug discovery
… fatal neurodegenerative disorders caused by the misfolding of the normal prion protein (PrP<sup>C</sup>) into its infectious form (PrP<sup>Sc</sup>). While the zoonotic potential of chronic wasting disease (CWD) remains uncertain, the presence of prions in food products raises public health …
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Protein Misfolding and Aggregation in Neurodegeneration: In Vitro And In Vivo Study Cases
… intracellular and extracellular protein misfolding and accumulation appears as a common pathological pathway. In the present thesis work I analyzed two cases of toxic protein deposition involved in ALS and AD. First, I looked at SOD1-G93A mutant protein, whose neuronal deposit is …
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The Role of Apolipoprotein E in Pregnancy-Associated Protein Misfolding and Risk of Preeclampsia
… others has identified preeclampsia as a protein misfolding disorder marked by an accumulation of abnormal conformations of misfolded proteins (including β-amyloid) in urine, serum, and placenta. Protein misfolding and aggregation have been studied extensively in prototype protein conformational …
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The Molecular Interaction Between Type Ii Diabetes and Alzheimer’S Disease Through Cross-Seeding of Protein Misfolding
… complications. T2D and AD are considered protein misfolding disorders (PMDs). PMDs are characterized by the presence of misfolded protein aggregates, such as in T2D pancreas (islet amyloid polypeptide - IAPP) and in AD brain (amyloid– Aβ) of affected individuals. The misfolding and accumulation of …
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Protein structure and interaction under environmental stress : from quality control recognition to evolution of collective behavior
… intracellular conditions, leading to protein misfolding - i.e. the inability of a protein to reach or maintain its native conformation. Since many proteins interact with each other, protein misfolding and cellular stress response must be examined both on the scale of individual protein …
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