Global ETD Search
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Showing 1 to 20 of 35 for “"Amyloid formation"”.
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Exploring SOD1 electron transfer, heterodimerization, and hetero-amyloid formation.
… center, (ii) subunit swapping, and (iii) hetero-amyloid formation. In chapter two, I use an analytical method, “protein charge ladders”, to distinguish between electron transfer (ET) and proton-coupled electron transfer (PCET) in a binuclear copper center by directly measuring the change in …
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Discovery and Mechanisms of Small Molecule Amyloid Formation Inhibitors
Current dogma suggests modulating or preventing amyloid assembly will prove critical to the armamentarium of therapeutic interventions that will likely be required to overcome the multifaceted pathology associated with amyloid diseases. The work described in this dissertation reveals substantial …
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On transient assemblies in amyloid formation: mechanistic insights and therapeutic strategies
… disorders. While the accumulation of amyloid fibrils hallmarks diagnoses of these conditions, pre-fibrllar oligomers are increasingly recognised as the major toxic agents. However, these assemblies pose significant experimental difficulties due to their transient nature, structural …
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Thermodynamic signatures for hexapeptides with propensity for phase separation and amyloid formation
… a variety of functions by adopting different conformations. The IDPs are also an important constituent of membraneless organelles that are formed by phase separation of proteins. Some IDPs can also aggregate and form amyloids. The occurrence of these amyloids in vivo is a hallmark of various …
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Mechanistic studies of beta protein amyloid formation in Alzheimer's disease : identification and characterization of protofibril intermediates
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 1998.
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Using yeast to study neurodegenerative diseases : amyloid formation as a protective mechanism and a new Alzheimer's disease model
… characterized by idiosyncratic protein amyloid inclusions. Not surprisingly amyloid fibrils have long been proposed to be the toxic protein species in these neurodegenerative diseases. However, more recent work has begun to suggest that the formation of ordered inclusions serves a …
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Mechanistic studies of beta protein and NAC amyloid formation in Alzheimer's disease and biochemical probes of NACP function
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 1996.
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Genetic Reduction of Cholesterol Synthesis in the Mouse Brain Does Not Affect Amyloid Formation in an Alzheimer’s Disease Model, but Does Extend Lifespan
… content or synthesis affect the cleavage of amyloid precursor protein (APP) to amyloidogenic peptides characteristic of Alzheimer’s disease (AD). To determine whether a decrease in cholesterol synthesis would affect APP processing in vivo, we crossed cholesterol 24-hydroxylase knockout (KO) …
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Insulin based inhibitors of human islet amyloid polypeptide (hIAPP) and their effect on aggregation of hIAPP in the treatment of type II diabetes
<p>Human islet amyloid polypeptide protein (hIAPP) is secreted by the pancreas along with insulin and is assumed to play a role in pathological development of type II diabetes. It has 37 amino acids in its sequence. Amyloid is formed due to misfolding of the protein, which is cytotoxic to beta …
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The Role of Force-Sensitive Interactions in Amyloid Assembly by Fungal Adhesins
… segment of their sequence, termed the amyloid-forming region (AFR). At the core of these adhesin aggregates are parallel or anti-parallel β-sheet arrays, which can layer onto other adhesin β-sheets by sidechain–sidechain interactions to form highly stable amyloid fibrils. The Als …
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Bayesian Approaches for the Mechanistic Analysis of Protein Aggregation Kinetics
The formation of amyloid fibrils is a hallmark of a wide range of prevalent and devastating human disorders, including Alzheimer’s disease and Parkinson’s disease. With effective treatments generally lacking, these conditions not only cause tremendous personal suffering but also impose a …
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On the Kinetics of Protein Misfolding and Aggregation
… 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 molecular origin …
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Mechanistic insights into the aggregation of [beta]-amyloid
Many of the fundamental characteristics of amyloid formation are still unknown, largely due to the limitations present in currently available techniques. This is particularly problematic for disease-associated amyloid-forming species such as betaamyloid (A/3) , due to the tremendous impact that …
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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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Prediction of parallel in-register amyloidogenic beta-structures In highly beta-rich protein sequences by pairwise propensity analysis
Amyloids and prion proteins are clinically and biologically important beta-structures, whose supersecondary structures are difficult to determine by standard experimental or computational means. In addition, significant conformational heterogeneity is known or suspected to exist in many amyloid …
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Fundamental efforts for improving the sensitivity of magnetic resonance force microscopy
… all the more valuable to understanding the conformational complexities of protein misfolding diseases and amyloid formation phenomena , caused by complex networks of structural transition reactions linking the monomeric, oligomeric, and polymorphic fibrillar forms of disease-causing proteins, …
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Mechanistic Investigation into the Regulation of Amyloid Motifs in Tau Aggregation and Disease
Amyloid formation of tau protein is a unifying theme in a multitude of neurodegenerative diseases, collectively called tauopathies. Missense mutations in the tau gene (MAPT) correlate with aggregation propensity and cause dominantly inherited tauopathies, but the molecular mechanism of how they …
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Molecular mechanism of Abeta recognition and neuroprotection by the glycoconjugate beta-sheet-breaker peptide Ac-LPFFD-Th
Inhibition of amyloid formation may represent a promising therapeutic approach for the treatment of neurodegenerative diseases. To this regard, peptide-based inhibitors of Abeta aggregation have been widely investigated with a particular emphasis to those derived from original amyloid sequences. …
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Electrostatic control of Cu, Zn superoxide dismutase aggregation in Amyotrophic Lateral Sclerosis : from lysine modification to interaction with lipid membranes.
… death within a few years. The deposition of SOD1 amyloid fibrils (i.e., gain of toxic function) in axons leads to selective death of motor neurons and neurodegeneration. In this dissertation, I use various bioanalytical and biophysical techniques to study aggregation of wild-type (WT) and …
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Protein MAS NMR methodology and structural analysis of protein assemblies
… peptides and proteins in crystalline form to amyloid fibrils and whole bacterial organelles are reported. The methods presented include novel pulse sequences and optimized pulse sequence elements, experimental approaches designed for multiple-spin systems, a protocol for efficient sequential …
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