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.
Results
Showing 1 to 20 of 85 for “"Protein misfolding"”.
-
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 …
-
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 …
-
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 …
-
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 …
-
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 …
-
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 …
-
Molecular origins of tissue vulnerability to aberrant aggregation in protein misfolding diseases
… clear that, although the aggregation of specific proteins, including amyloid β (Aβ) and tau in AD and α-synuclein in PD, hallmark these disorders, such behaviour is a consequence of a wider, system-level disruption of protein homeostasis. In order to identify the genetic factors contributing to …
-
Using cannabidiol and trazodone to treat protein misfolding neurodegenerative disease in C. elegans
… 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 signaling pathways involved in reactive oxygen species (ROS) or the unfolded protein response …
-
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 …
-
Protein Misfolding and Aggregation in Neurodegeneration: In Vitro And In Vivo Study Cases
… and morbidity, 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 …
-
The Role of Apolipoprotein E in Pregnancy-Associated Protein Misfolding and Risk of Preeclampsia
… lab and 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 …
-
The Molecular Interaction Between Type Ii Diabetes and Alzheimer’S Disease Through Cross-Seeding of Protein Misfolding
… other 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 …
-
Development of A High-Throughput System For Screening of Anti-Prion Molecules
<p>The misfolded prion protein causes and transmits disease in both humans and animals. As other infectious agents, prions display strain variation, which can generate different pathological outcomes in affected individuals. Unfortunately, there are no known therapies for these diseases, which at …
-
Protein structure and interaction under environmental stress : from quality control recognition to evolution of collective behavior
A protein's function in the cell depends on its structure, which in turn depends on the intracellular environment. Stress like heat shock or nutrient starvation can alter intracellular conditions, leading to protein misfolding - i.e. the inability of a protein to reach or maintain its native …
-
Disordered Protein Aggregates Are Linked to Changes in the Histone Post-Translational Modification Landscape in Disease and Non-Disease Models
<p>Proper protein folding is a delicate balance that is crucial for normal biological function. In mammals, protein misfolding and aggregation leads to loss of function of the original protein while in many cases being associated with neurodegenerative diseases, eventually leading to death of the …
-
Physical biology of biomembranes and biomolecules (PHYBIOM)
… of binding. The functional group structures of protein folding (e.g. RBCs membrane protein) have been investigated using classical quantum biology based on infrared spectroscopy in polar groups capable of forming hydrogen bonds. The equivalence of infrared radiant energy and the bending energy …
-
Topographical Differences in Stress Vulnerability in Experimental Parkinson's Disease
… is characterized by the progressive spread of protein misfolding stress, or proteotoxicity, across the brain. During this protracted process, the allocortex of the temporal lobe develops protein inclusions before the neocortex in the frontal and parietal lobes. In the present study we tested …
-
The Role of Sacsin as a Molecular Chaperone
… this loss of neurons appears to be related to protein misfolding, comprising a large public health burden. For example, the two most common neurodegenerative diseases, Alzheimer’s and Parkinson’s diseases, possess protein misfolding as a core component of their pathology. In order to properly …
-
Methods to study protein folding and evolution in vivo
… and quality control factors which maintain protein homeostasis (proteostasis) by actively monitoring protein folding processes in an organelle-specific and dealing with protein misfolding in a stress-responsive manner. While we know that these "proteostasis networks" are capable of …
-
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 …
Page 1 of 5