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BACE: Lead Target for Orchestrated Therapy of Alzheimer's Disease
By: Varghese JohneBook Publisher: John Wiley & Sons
Imprint: John Wiley & Sons
Format: Adobe Encrypted (DRM)
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BACE inhibitors and their use in the treatment of Alzheimer's Disease
BACE (β-site of APP cleaving enzyme) is a critical component in Alzheimer's Disease (AD), and the development of BACE inhibitors shows great potential as a therapy for the disease. BACE: Lead Target for Orchestrated Therapy of Alzheimer's Disease covers virtually all aspects of BACE from initial identification, discovery of inhibitors, and challenges in clinical development, while providing a global understanding essential for productive and successful drug discovery.
This book details the story of the discovery of BACE and its role in AD and comprehensively discusses:
The development of BACE inhibitors as therapeutics for Alzheimer's disease
The research that led to the identification of BACE
New BACE inhibitors currently being clinically tested
ADME (absorption, distribution, metabolism, excretion) and clinical trial design—topics not addressed in current field literature
Cutting-edge technology such as high-throughput screening, structure-based drug design, and QSAR in context of BACE inhibitors and Alzheimer's drug discovery
Other approaches to BACE inhibition based on interaction with the precursor protein APP
By enhancing the reader's understanding of the various aspects of the BACE drug-discovery process, this much-needed reference will serve as a key resource for all scientists involved in Alzheimer's research—and inspire new approaches to treatment of AD.
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| Title of eBook: BACE: Lead Target for Orchestrated Therapy of Alzheimer's Disease | |
| Release Date: 03-05-2010 | |
| Publisher: John Wiley & Sons |
This eBook download is available in the following formats:
| Parent title | BACE: Lead Target for Orchestrated... |
|---|---|
| Encrypted (DRM) | Yes |
| SKU | 9780470594070 |
| File size | 11171 |
| Security | n/a |
| Printing | Not allowed |
| Copying | Not allowed |
| Read aloud | No Sys requirements Download reader |
| Devices | Samsung Tablet, Apple Ipad & Iphone, Barnes & Noble Nook, Kobo eReader, Aluratek Libre, Iliad, Nokia, Blackberry, Hanlin |
| Note | Excellent navigation features are available via Adobe such as bookmarks and a quick access table of contents. Text search is easily accessible. An Adobe DRM-protected file is different than a pdf file in that it uses Adobe DRM (Digital Rights Management) technology, which authors and publishers use to protect their content from illegal online distribution and to set certain privileges such as restrictions on copying and printing. |
BACE: Lead Target for Orchestrated Therapy of Alzheimer's Disease
Chapter One
BACE, APP PROCESSING, AND SIGNAL TRANSDUCTION IN ALZHEIMER'S DISEASEDale E. Bredesen and Edward H. Koo
1.1 INTRODUCTION
Alzheimer's disease (AD) is a remarkably, and to date inexplicably, common disease, affecting over five million Americans at a national cost of approximately $150billion annually - a cost that does not begin to address the impact of the disease on families, individuals, and society. With the graying of America, the prediction is for approximately 13million cases by 2050 and, given the late appearance of symptoms in the pathogenic process, many more pre-Alzheimer's cases, including both mild cognitive impairment (MCI) and pre-MCI conditions. Thus, AD is unfolding as one of the most important global health concerns.
Since the first description of the disease just over 100years ago, extensive clinical, pathological, genetic, and biochemical data have been accumulated, implicating the amyloid-beta (A[beta]) peptides, especially A[beta]1-42, as key mediators in the pathogenesis of this disorder, the so-called amyloid cascade hypothesis. However, the physiological role of these peptides remains unknown, as does the mechanism(s) of their neurodegenerative effect.
The A[beta] peptides are derived proteolytically from the [beta]-amyloid precursor protein (APP) by [beta]-site APP cleaving enzyme (BACE) (or [beta]-secretase) cleavage of the extracellular domain, followed by [gamma]-secretase cleavage of the transmembrane domain. However, APP is also cleaved at other sites, for example, at the [alpha]-site by [alpha]-secretase (with ADAM10 being the mos
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