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Attributes of “Protein Folding Disorders of the Central Nervous System PDF”
This exciting new book explores the dark side of the molecular protein assembly bringing an updated view of how failures in the homeostatic mechanisms that efficiently regulate protein folding leads to the accumulation of structurally abnormal pathogenic assemblies, encompassing an emerging group of diseases collectively known as “Protein Folding Disorders.” This complex and diverse group of chronic and progressive entities are bridged together by their relationship to structural transitions in the native state of specific proteinaceous components, which for reasons poorly understood, convert into polymeric aggregates that generate poorly soluble tissue deposits and which are considered today the culprit of the disease pathogenesis in their respective diseases. Despite the diversity in the amino acid sequence of the different proteins involved in these heterogeneous disorders, all the pathologic conformers can trigger cascades of events ultimately resulting in cell dysfunction and death with devastating clinical consequences in many of the most precious aspects of human existence including personality, cognition, memory, and skilled movements. This book, which is composed of a compilation of chapters authored by outstanding and well-published scientists in the respective fields currently performing active investigations at world renowned universities and research centers, focuses on the growing number of diseases associated with protein misfolding in the central nervous system. Individual chapters are dedicated to the most common neurodegenerative diseases associated with protein aggregation/fibrillization focusing on the nature of the pathogenic species and the cellular pathways involved in the molecular pathogenesis of Alzheimer’s, Parkinson’s, and Huntington’s diseases as well as in Amyotrophic Lateral Sclerosis, and Prion disorders. A group of contributions is centered on the current knowledge of the intracellular pathways and subcellular organelles affected by the different disease conditions, while others are focused in the emerging pathogenic role of misfolded subunits assembled into neurotoxic soluble oligomers, and in the novel notion of the transmissibility of the protein misfolded species, an innovative concept until recently only accepted for Prion diseases. Lastly, a different set of chapters is dedicated to the evaluation of novel therapeutic strategies for these devastating diseases. Protein Folding Disorders of the Central Nervous System PDF
Readership: Graduate students and researchers in neuroscience, neurology, neurobiology and biochemistry.
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Illustrations of “Protein Folding Disorders of the Central Nervous System PDF”
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The Writers
Jorge Ghiso (Author, Editor), Agueda Rostagno (Editor)
Dr Jorge A Ghiso is a Professor in the Departments of Pathology and Psychiatry at New York University School of Medicine. He has a long-standing interest in the molecular pathogenic mechanisms of sporadic and hereditary disorders associated with protein misfolding, with particular emphasis in systemic and cerebral forms of amyloidosis. His laboratory has developed biochemical and proteomic approaches that pioneered the isolation and identification of multiple amyloid subunits linked to systemic and cerebral disease in humans. In the field of Alzheimer’s disease, he concentrated his efforts in physiologic and pathologic aspects of amyloid-β (Aβ), exploring the association of this peptide with lipidated apolipoproteins, the role of the blood-brain barrier in modulating Aβ uptake and clearance, and the discovery of a systemic pathway of Aβ catabolism with physiological relevance. The finding of non-Aβ cerebral amyloidoses with neuropathological features similar, if not identical, to those of Alzheimer’s disease provided an alternative model to study neurodegeneration and the process of fibrillization in the brain. His current research explores the clearance mechanisms governing Aβ homeostasis and the complex dynamic balance regulating amyloid deposition and removal in the brain.
Dr Agueda Rostagno is an Associate Professor in the Department of Pathology at New York University School of Medicine. Her research interests are centered on the molecular pathogenesis of cerebral amyloidoses, particularly those forms associated with cerebral hemorrhage and neurodegeneration. Her work has been focused in structural-functional correlations aimed at deciphering common roles of unrelated amyloid assemblies in the modulation of cellular mechanisms and signaling pathways that trigger cellular dysfunction and alter the functionality of the neurovascular unit. Over the years, her laboratory has unveiled novel receptors through which pathogenic amyloid assemblies trigger pro-apoptotic mechanisms and has identified the engagement of mitochondrial-mediated pathways and oxidative stress mechanisms in cells composing the neurovascular unit. Her work conveys the notion that comparable oligomeric assemblies, regardless of the primary structure of the amyloid subunit involved in the formation of the pathogenic conformers, have the capability to elicit common pathological mechanisms and argues for the likely applicability of shared translational approaches for these disorders.
Proportions of “Protein Folding Disorders of the Central Nervous System PDF”
- Publisher : World Scientific Publishing Co Pte Ltd; 1st edition (November 26, 2017)
Language : English
Hardcover : 336 pages
International Standard Book Number-10 : 9813222956
International Standard Book Number-13 : 978-9813222953
Item Weight : 1.35 pounds
Dimensions : 6 x 0.75 x 9 inches - Protein Folding Disorders of the Central Nervous System PDF
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