PDF Ebook Alzheimer's Disease: Insights into Low Molecular Weight and Cytotoxic Aggregates from In Vitro and Computer Experiments - Molecular Basis o
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Alzheimer's disease is the most common form of senile dementia, affecting more than 24 million people worldwide. It is characterised pathologically by abnormally high levels of neurofibrillary tangles resulting from the accumulation of tau protein in dead and dying neurons, and by elevated numbers of senile plaques in the cortex and hippocampus of the brain. The major component of senile plaques is a small protein of 39-43 amino acids called amyloid- (A ). Thus far, no treatment has been shown to slow the progression of sporadic and familial Alzheimer's disease.
A large body of evidence points, however, to the early A -formed oligomers as the primary toxic species in Alzheimer's disease. A powerful strategy for developing pharmaceutical treatments against Alzheimer's is to elucidate the pathways of oligomer formation and determine the structures of the toxic aggregates.
This book provides a panoramic view across recent in vitro and in vivo studies along with state-of-the-art computer simulations, designed to increase the readers' understanding of A oligomerisation and fibril formation. At the same time, the book delves into the pathogenesis of familial and sporadic Alzheimer's disease at the atomic level of detail.
Written by leading authors in their respective fields, this book will be valuable to all scientists working on Alzheimer's disease.
Readership: General public, PhD students, postdocs, as well as all scientists working in the following fields: Alzheimer's disease, amyloids, neuroscience, oligomers, protofibrils, fibrils, toxicity, structures, dynamics, kinetics, thermodynamics, all-atom and coarse grained simulations, biophysics, memory, learning, transgenic mouse models, metal ions, membrane, nanoparticles, computational chemistry, drug design and bioinformatics.
- Sales Rank: #8979251 in Books
- Published on: 2013-03-06
- Original language: English
- Number of items: 1
- Dimensions: 9.10" h x 1.00" w x 6.10" l, .0 pounds
- Binding: Hardcover
- 464 pages
From the Inside Flap
Alzheimer's disease is the most common form of senile dementia, affecting more than 24 million people worldwide. It is characterised pathologically by abnormally high levels of brain lesions (senile plaques) in dead and dying neurons, and by elevated numbers of amyloid deposits in the walls of cerebral blood vessels. The major component of senile plaques is a small protein of 39 43 amino acids called amyloid- (A ). Thus far, no treatment has been shown to slow the progression of sporadic and familial Alzheimer's disease.
A large body of evidence points to the early A oligomers as the primary toxic species in Alzheimer's disease. A powerful strategy for developing pharmaceutical treatments against Alzheimer's is to elucidate the pathways of oligomer formation and determine the structures of the toxic aggregates.
This book provides a panoramic view across recent in vitro and in vivo studies along with state-of-the-art computer simulations, designed to increase the readers' understanding of A oligomerisation and fibril formation. At the same time, the book delves into the pathogenesis of familial and sporadic Alzheimer's disease at the atomic level of detail.
Written by leading authors in their respective fields, this book will be valuable to all scientists working with Alzheimer's disease.
Most helpful customer reviews
0 of 0 people found the following review helpful.
Essential Reading
By David Richards
This is a great book and the subject matter is well presented. It's very technical and as a clinician rather than an academic I found some areas heavy going, but it's well worth working though it. There's no opinion just simply facts and data, which are extremely well researched. You'd need a fair understanding of the subject to be able to appreciate the information so if your looking for an introduction this is not for you. But if you're interested in the mechanics this is a well balanced read.
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