Cellular prion (PrP(c)) undergoes a regulated α-secretase-like cleavage by the disintegrin ADAM17 similar to the one taking place on β-amyloid precursor protein (βAPP). Because these cleavages give rise to biologically active fragments, understanding their regulation could be of importance. We have established that the Extracellular Regulated...
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January 1, 2013 (v1)Journal articleUploaded on: December 4, 2022
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January 1, 2012 (v1)Journal article
Cellular prion (PrP (c) ) undergoes a regulated α-secretase-like cleavage by the disintegrin ADAM17 similar to the one taking place on β-Amyloid Precursor Protein (βAPP). Because these cleavages give rise to biologically active fragments, understanding their regulation could be of importance. We have established that the Extracellular Regulated...
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December 2002 (v1)Journal article
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January 2012 (v1)Journal article
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January 2012 (v1)Journal article
The amyloid-β precursor protein (βAPP) undergoes several cleavages by enzymatic activities called secretases. Numerous studies aimed at studying the biogenesis and catabolic fate of Aβ peptides, the proteinaceous component of the senile plaques that accumulate in Alzheimer's disease-affected brains. Relatively recently, another...
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January 1, 2008 (v1)Book section
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October 2021 (v1)Journal article
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April 11, 2008 (v1)Journal article
Beta-amyloid (Abeta) peptides that accumulate in Alzheimer disease are generated from the beta-amyloid precursor protein (betaAPP) by cleavages by beta-secretase BACE1 and by presenilin-dependent gamma-secretase activities. Very few data document a putative cross-talk between these proteases and the regulatory mechanisms underlying such...
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January 2021 (v1)Journal article
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February 1997 (v1)Journal article
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December 2002 (v1)Journal article
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August 1996 (v1)Journal article
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2011 (v1)Journal article
Proteolytic degradation has emerged as a key pathway involved in controlling levels of the Alzheimer's disease (AD)-associated amyloid-β peptides (Aβ) in the brain. The ectopeptidase, neprilysin (NEP), has been reported as the major Aβ-degrading enzyme in mice and human brains. We have previously shown that NEP expression and activity are...
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August 15, 1996 (v1)Journal article
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July 2009 (v1)Journal articlePharmacological evidences for DFK167-sensitive presenilin-independent gamma-secretase-like activity.
Amyloid-beta (Abeta) peptides production is thought to be a key event in the neurodegenerative process ultimately leading to Alzheimer's disease (AD) pathology. A bulk of studies concur to propose that the C-terminal moiety of Abeta is released from its precursor beta-amyloid precursor protein by a high molecular weight enzymatic complex...
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August 2000 (v1)Journal article
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2010 (v1)Journal article
Amyloid beta-peptides is the generic term for a set of hydrophobic peptides that accumulate in Alzheimer's disease (AD)-affected brains. These amyloid-beta peptide fragments are mainly generated by an enzymatic machinery referred to as gamma-secretase complex that is built up by the association of four distinct proteins, namely presenilin 1...
Uploaded on: December 3, 2022