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Full-Text Articles in Life Sciences
Amyloid Fibril Formation And Polymorphism : A Critical Role Of Sulfur-Containing Amino Acid Residues, Tatiana Quiñones-Ruiz
Amyloid Fibril Formation And Polymorphism : A Critical Role Of Sulfur-Containing Amino Acid Residues, Tatiana Quiñones-Ruiz
Legacy Theses & Dissertations (2009 - 2024)
Protein aggregation that results in the formation of amyloid fibrils has been linked to many neurodegenerative disorders, including Alzheimer’s disease and Parkinson’s disease. The sulfur atoms in methionine (Met) and cysteine (Cys) residues of proteins can be readily oxidized, significantly affecting their properties. Oxidation of sulfur-containing amino acids has recently been shown to affect protein fibrillation. This work presents novel findings on Cys and Met redox reactions that are related to the formation of amyloid fibrils and on the polymorphism of a model fibrillogenic protein, hen egg white lysozyme (HEWL). Biophysical techniques including Raman spectroscopy, atomic force microscopy, electron paramagnetic …
Ab42 Alters Glutamatergic Transmission In The Ca1 Region Of The Mouse Hippocampus, Patrick Harry Wehrle
Ab42 Alters Glutamatergic Transmission In The Ca1 Region Of The Mouse Hippocampus, Patrick Harry Wehrle
Legacy Theses & Dissertations (2009 - 2024)
Alzheimer’s disease (AD) is a neurodegenerative disease affecting 4.5 million people in the US, a number expected to increase 3-fold over the next 30 years. One of the hallmarks of AD is the extracellular accumulation of the protein Aß₄₂ throughout in the brain, particularly in limbic structures like the temporal cortex and hippocampus, key regions for learning and memory. Currently available animal models for AD aim to reproduce key genetic traits of the familial variant of the disease, but >90% of AD patients are affected by idiopathic AD. To overcome this potential limitation, we use a different approach to study …