By Philippe Derreumaux (ed.)
Alzheimer's sickness is the commonest type of senile dementia, affecting greater than 24 million humans all over the world. it truly is characterized pathologically via abnormally excessive degrees of neurofibrillary tangles caused by the buildup of tau protein in lifeless and death neurons, and by way of increased numbers of senile plaques within the cortex and hippocampus of the mind. the key section of senile plaques is a small protein of 39-43 amino acids known as amyloid- (A ). to this point, no therapy has been proven to gradual the development of sporadic and familial Alzheimer's disorder.
a wide physique of proof issues, in spite of the fact that, to the early A -formed oligomers because the fundamental poisonous species in Alzheimer's ailment. a strong technique for constructing pharmaceutical remedies opposed to Alzheimer's is to clarify the pathways of oligomer formation and ensure the constructions of the poisonous aggregates.
This e-book presents a wide ranging view throughout fresh in vitro and in vivo experiences in addition to cutting-edge laptop simulations, designed to extend the readers' knowing of A oligomerisation and fibril formation. whilst, the e-book delves into the pathogenesis of familial and sporadic Alzheimer's disorder on the atomic point of element.
Written by way of best authors of their respective fields, this booklet can be beneficial to all scientists engaged on Alzheimer's disorder.
Readership: basic public, PhD scholars, postdocs, in addition to all scientists operating within the following fields: Alzheimer's affliction, amyloids, neuroscience, oligomers, protofibrils, fibrils, toxicity, constructions, dynamics, kinetics, thermodynamics, all-atom and coarse grained simulations, biophysics, reminiscence, studying, transgenic mouse versions, steel ions, membrane, nanoparticles, computational chemistry, drug layout and bioinformatics.
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Extra info for Alzheimer's Disease
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B. W. (2004). Amyloid beta prevents activation of calcium/calmodulin-dependent protein kinase II and AMPA receptor phosphorylation during hippocampal long-term potentiation, J. , 92, 2853–2858. A. L. (2008). , 22, 246–260. November 26, 2012 10:0 9in x 6in Alzheimer’s Disease: Insights Into Low Molecular … b1377-chA2 2 Models of Wild-Type and Disease-Causing Mutant β-Amyloid Fibrils. Insights from Solid-State Nuclear Magnetic Resonance Spectroscopy Stephen C. , 1985). ) Aβ is derived from sequential proteolytic cleavage of a single transmembrane domain-containing protein, the Aβ precursor protein (β-APP, also called APP) by β-secretase (BACE1), followed by γ-secretase ∗ Department of Pathology, The University of Chicago, 5841 S.
2005). 3D structure of Alzheimer’s amyloidbeta(1-42) fibrils, Proc. Natl. Acad. Sci. , 102, 17342–17347. , Garcia-Abreu, J. T. (2008). Amyloid-beta binds to the extracellular cysteine-rich domain of Frizzled and inhibits Wnt/betacatenin signaling, J. Biol. , 283, 9359–9368. , Quinn, J. H. (2006). Mitochondria are a direct site of A beta accumulation in Alzheimer’s disease neurons: implications for free radical generation and oxidative damage in disease progression, Hum. Mol. , 15, 1437–1449. P.
Alzheimer's Disease by Philippe Derreumaux (ed.)