[HTML][HTML] Rapid appearance and local toxicity of amyloid-β plaques in a mouse model of Alzheimer's disease

M Meyer-Luehmann, TL Spires-Jones, C Prada… - Nature, 2008 - nature.com
amyloid imaging agent, methoxy-XO4, would not report amyloid-β deposits that do not
contain β-pleated sheets, we compared immunostaining for amyloid-β and methoxy-XO4 in …

Four-dimensional multiphoton imaging of brain entry, amyloid binding, and clearance of an amyloid-β ligand in transgenic mice

BJ Bacskai, GA Hickey, J Skoch… - Proceedings of the …, 2003 - National Acad Sciences
… In separate experiments, PIB-labeled amyloid-β deposits were detectable up to 3 days after
a single … This graph illustrates the rapid appearance of fluorescent dye in blood vessels, the …

Amyloid-β forms fibrils by nucleated conformational conversion of oligomers

J Lee, EK Culyba, ET Powers, JW Kelly - Nature chemical biology, 2011 - nature.com
… To provide further evidence for the rapid formation of amyloid-β 1–40 oligomers, we
recorded dynamic light scattering time courses (Fig. 3a). We incubated monomerized CC-…

Small non-fibrillar assemblies of amyloid β-protein bearing the Arctic mutation induce rapid neuritic degeneration

BM Whalen, DJ Selkoe, DM Hartley - Neurobiology of disease, 2005 - Elsevier
… Recent studies suggest that soluble intermediates formed during amyloid β-protein (Aβ) …
Neurons exposed to Arctic Aβ showed a progressive degeneration that was much more rapid

Rapid assembly of amyloid-β peptide at a liquid/liquid interface produces unstable β-sheet fibers

MR Nichols, MA Moss, DK Reed, JH Hoh… - Biochemistry, 2005 - ACS Publications
… of insoluble fibrillar amyloid aggregates in the brain parenchyma and cerebral vessels (see
ref 1). The primary component of these amyloid deposits is the amyloid-β peptide (Aβ). Aβ is …

Amyloid-β (1− 42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsulfate

V Rangachari, BD Moore, DK Reed, LK Sonoda… - Biochemistry, 2007 - ACS Publications
… conversion to a predominant β-structured conformation in 2 mM SDS which does not
proceed to amyloid fibrils. The conformational change is instead rapidly followed by the near …

Amyloid β-protein dimers rapidly form stable synaptotoxic protofibrils

B O'Nuallain, DB Freir, AJ Nicoll, E Risse… - Journal of …, 2010 - Soc Neuroscience
… Nonfibrillar, water-soluble low-molecular weight assemblies of the amyloid β-protein (Aβ) …
more rapidly than either AβS26C or wild-type monomers and formed parastable β-sheet rich…

Structural and kinetic features of amyloid β-protein fibrillogenesis

DB Teplow - Amyloid, 1998 - Taylor & Francis
… first applied to the P-amyloid QLS is an optical technique for the rapid, non-invasive,
quantitative … upon peptide dissolution and the rapid polymerization of AD made determination of …

Alzheimer's disease and the amyloid-β peptide

MP Murphy, H LeVine III - Journal of Alzheimer's disease, 2010 - content.iospress.com
… [104] and is surprisingly rapid in that system and includes vascular amyloid [105]. Although
this … Not all pools of Aβ in the human brain may participate in this rapid exchange of monomer …

Rapidly progressive Alzheimer's disease features distinct structures of amyloid-β

ML Cohen, C Kim, T Haldiman, M ElHag, P Mehndiratta… - Brain, 2015 - academic.oup.com
… The primary goal of the study was to establish conformational structural characteristics of
amyloid-β in neuropathologically verified rapidly and slowly progressive Alzheimer’s disease …