Results 81 to 90 of about 337,024 (290)

Generation and initial characterization of FDD knock in mice. [PDF]

open access: yesPLoS ONE, 2009
BACKGROUND:Mutations in the integral membrane protein 2B, also known as BRI(2), a type II trans-membrane domain protein cause two autosomal dominant neurodegenerative diseases, Familial British and Danish Dementia.
Luca Giliberto   +4 more
doaj   +1 more source

Strong positive light chain immunostaining in a patient with transthyretin amyloidosis

open access: yesHematology, 2023
The two most common systemic amyloidosis types are immunoglobulin light chain (AL) and amyloid transthyretin (ATTR) amyloidosis, in which the precursor proteins responsible for amyloidosis are light chain and transthyretin, respectively.
Jiao Chen   +5 more
doaj   +1 more source

Destruxin E Decreases Beta-Amyloid Generation by Reducing Colocalization of Beta-Amyloid-Cleaving Enzyme 1 and Beta-Amyloid Protein Precursor [PDF]

open access: yes, 2009
Alzheimer-disease-associated beta-amyloid (A beta) is produced by sequential endoproteolysis of beta-amyloid protein precursor (beta APP): the extracellular portion is shed by cleavage in the juxtamembrane region by beta-amyloid-cleaving enzyme (BACE ...
Dohi, Keiji   +27 more
core   +1 more source

A guide to selecting high-performing antibodies for amyloid-beta precursor protein for use in Western Blot, immunoprecipitation and immunofluorescence [version 2; peer review: 2 approved, 1 approved with reservations]

open access: yesF1000Research
The amyloid-beta precursor protein is a transmembrane protein expressed in many tissues and highly concentrated in the brain. The protein is of significant interest due to its involvement in the generation of amyloidogenic β-amyloid peptides, prone to ...
Carl Laflamme   +4 more
doaj   +1 more source

Soluble pre-fibrillar tau and β-amyloid species emerge in early human Alzheimer’s disease and track disease progression and cognitive decline [PDF]

open access: yes, 2016
Acknowledgments We would like to gratefully acknowledge all donors and their families for the tissue provided for this study. Human tissue samples were supplied by the Brains for Dementia Research programme, jointly funded by Alzheimer’s Research UK, the
Cranston, Anna   +5 more
core   +3 more sources

Deposition of amyloid fibrils promotes cell-surface accumulation of amyloid β precursor protein

open access: yesNeurobiology of Disease, 2004
Amyloid β protein (Aβ) deposition and neuronal degeneration are characteristic pathological features of Alzheimer's disease (AD). In vitro, Aβ fibrils (fAβ) induce neuronal degeneration reminiscent to AD, but the mechanism of neurotoxicity is unknown ...
Lorena Heredia   +5 more
doaj   +1 more source

Dysregulation of Na+/K+ ATPase by amyloid in APP+PS1 transgenic mice [PDF]

open access: yes, 2005
BACKGROUND: The pathology of Alzheimer's disease (AD) is comprised of extracellular amyloid plaques, intracellular tau tangles, dystrophic neurites and neurodegeneration. The mechanisms by which these various pathological features arise are under intense
Dickey, Chad A   +5 more
core   +3 more sources

Insights into the physiological function of the β-amyloid precursor protein: beyond Alzheimer's disease

open access: yesJournal of Neurochemistry, 2014
The β‐amyloid precursor protein (APP) has been extensively studied for its role as the precursor of the β‐amyloid protein (Aβ) of Alzheimer's disease. However, the normal function of APP remains largely unknown.
E. Dawkins, D. Small
semanticscholar   +1 more source

Copper Promotes the Trafficking of the Amyloid Precursor Protein [PDF]

open access: yesJournal of Biological Chemistry, 2011
Accumulation of the amyloid β peptide in the cortical and hippocampal regions of the brain is a major pathological feature of Alzheimer disease. Amyloid β peptide is generated from the sequential protease cleavage of the amyloid precursor protein (APP). We reported previously that copper increases the level of APP at the cell surface.
Ashley I. Bush   +11 more
openaire   +4 more sources

NeuroAiD® (MLC601) and Amyloid Precursor Protein Processing [PDF]

open access: yesCerebrovascular Diseases, 2013
<b><i>Background:</i></b> Amyloid precursor protein (APP) undergoes cleavage under physiological conditions, predominantly by α- and &#947;-secretases, to form the nonpathogenic sAPPα and p3 fragments. By contrast, amyloid-beta (Aβ) is produced via proteolytic cleavage by β- and &#947;-secretases. In Alzheimer's disease (
Lim, YA, Murray, LA, Lai, MKP, Chen, C
openaire   +3 more sources

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