Results 311 to 320 of about 120,218 (348)

Sequestration of amyloid beta-peptide.

Annals of the New York Academy of Sciences, 1993
Amyloid beta-protein, or beta/A4, is a 4-kilodalton peptide that forms poorly soluble extracellular depositions of amyloid in brains and leptomeninges of patients with Alzheimer's disease (AD), Down's syndrome (DS), and hereditary cerebral hemorrhage with amyloidosis-Dutch type (HCHWA-D).
D, Goldgaber, A I, Schwarzman, R, Bhasin, L, Gregori, D, Schmechel, A M, Saunders, A D, Roses, W J, Strittmatter   +7 more
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Intracellular biology of Alzheimer's disease amyloid beta peptide

European Archives of Psychiatry and Clinical Neuroscience, 1999
Strong evidence links excess production of a small peptide and the pathogenesis of Alzheimer's disease (AD). Originally this peptide, beta-amyloid 42 (Abeta42), was assumed to be released by a pathogenic event; it is now well established that Abeta42 is released from cells during normal cellular metabolism of the Alzheimer amyloid precursor protein ...
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In vitroOligomerization and Fibrillogenesis of Amyloid-beta Peptides

2012
The amyloid beta Ab(1-40) and Ab(1-42) peptides are the main components of the fibrillar plaques characteristically found in the brains affected by Alzheimer's disease. Fibril formation has been thoroughly studied in vitro using synthetic amyloid peptides and has been described to be a nucleation dependent polymerization process.
Núria, Benseny-Cases, Oksana, Klementieva, Josep, Cladera   +2 more
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Radiolabeling of Amyloid-β Peptides

2005
Nowadays, a wide variety of protocols for labeling proteins is available. However, radiolabeling remains one of the most powerful, sensitive and accurate methods to trace and quantitate proteins. Additionally, radiolabeling techniques are steadily gaining importance for diagnosis and treatment in nuclear medicine.
Miguel, Calero, Jorge, Ghiso
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Brain membrane cholesterol domains, aging and amyloid beta-peptides

Neurobiology of Aging, 2002
Lipids are essential for the structural and functional integrity of membranes. Membrane lipids are not randomly distributed but are localized in different domains. These domains consist of the exofacial and cytofacial leaflets, cholesterol pools, annular lipids, and lipid rafts.
W Gibson, Wood, Friedhelm, Schroeder, Urule, Igbavboa, Nicolai A, Avdulov, Svetlana V, Chochina   +4 more
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Monitoring the amyloid beta-peptide in vivo – caveat emptor

Drug Discovery Today, 2009
As a wave of 'disease modifying' (DM) therapies for Alzheimer's disease (AD) progresses towards the later stages of clinical development, an evaluation of our ability to measure relevant pharmacodynamic effects of such therapies is warranted. Reducing accumulation of amyloid beta (Abeta)-peptide in the brain parenchyma is the primary objective of most ...
Paul W, Thompson, Andrew, Lockhart
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Interfacial Effects on the Conformation of Amyloid-Beta Peptide

Protein & Peptide Letters, 2009
We examined the effects of air-water and water-sevoflurane interfaces on conformational properties of amyloid-beta peptide (ABP). Fractions were extracted from sub-interfacial (air-water) and supra-interfacial (water-sevoflurane) layers and compared with aqueous bulk layers using fluorescence properties of ABP provided by a single tyrosine.
Norbert W, Seidler, Joshua D, Eklund
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Amyloid beta-peptide: the inside story.

Current Alzheimer research, 2005
The amyloid beta-peptide (Abeta) plays an early and critical role in the pathogenic cascade leading to Alzheimer's disease (AD). Abeta is typically found in extracellular amyloid plaques that occur in specific brain regions in the AD and Down syndrome brain.
Bertrand P, Tseng, Masashi, Kitazawa, Frank M, LaFerla   +2 more
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Interaction of Calreticulin with Amyloid Beta Peptide 1-42

Protein & Peptide Letters, 2008
The interaction of calreticulin with amyloid beta (Abeta) was investigated using solid phase and solution binding assays. Calreticulin bound Abeta 1-42 in a time and concentration dependent fashion. The binding was optimal at pH 5 and was stimulated by Ca2+ and inhibited by Zn2+ at pH 7.
Duus, K., Hansen, Paul Robert, Houen, G.
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Amyloid beta peptide-activated signal pathways in human platelets

European Journal of Pharmacology, 2008
Amyloid beta peptide (amyloid-beta), which accumulates in the cerebral microvessels in an age-dependent manner, plays a key role in the pathogenesis of cerebral amyloid angiopathy. Platelets are an important cellular element in vasculopathy of various causes. Amyloid-beta may activate or potentiate platelet aggregation.
Ming Y, Shen, George, Hsiao, Tsorng H, Fong, Hui M, Chen, Duen S, Chou, Chien H, Lin, Joen R, Sheu, Chung Y, Hsu   +7 more
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