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- Publications
- Influence
Involvement of Caspases in Proteolytic Cleavage of Alzheimer’s Amyloid-β Precursor Protein and Amyloidogenic Aβ Peptide Formation
- F. Gervais, D. Xu, +16 authors D. Nicholson
- Biology
- Cell
- 30 April 1999
Abstract The amyloid-β precursor protein (APP) is directly and efficiently cleaved by caspases during apoptosis, resulting in elevated amyloid-β (Aβ) peptide formation. The predominant site of… Expand
L-685,458, an Aspartyl Protease Transition State Mimic, Is a Potent Inhibitor of Amyloid β-Protein Precursor γ-Secretase Activity
- M. Shearman, D. Beher, +7 authors J. L. Castro
- Chemistry
- 6 July 2000
Progressive cerebral amyloid β-protein (Aβ) deposition is believed to play a central role in the pathogenesis of Alzheimer's disease (AD). Elevated levels of Aβ(42) peptide formation have been linked… Expand
Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1
- Y. Li, Min Xu, +15 authors S. J. Gardell
- Biology
- Nature
- 8 June 2000
Cleavage of amyloid precursor protein (APP) by the β- and γ-secretases generates the amino and carboxy termini, respectively, of the Aβ amyloidogenic peptides Aβ40 and Aβ42—the major constituents of… Expand
Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-beta precursor protein and amyloidogenic A beta peptide formation.
- F. Gervais, D. Xu, +16 authors D. Nicholson
- Medicine
- Cell
- 1999
The amyloid-beta precursor protein (APP) is directly and efficiently cleaved by caspases during apoptosis, resulting in elevated amyloid-beta (A beta) peptide formation. The predominant site of… Expand
Amyloid-β Hypothesis of Alzheimer’s Disease
- M. Shearman
- Biology
- 1998
Recent progress in understanding the molecular basis of Alzheimer’s disease (AD) can be attributed mainly to linkage analysis and positional cloning of gene mutations associated with familial AD… Expand
Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of beta-amyloid-mediated cell death.
- M. Shearman, C. I. Ragan, L. Iversen
- Biology, Medicine
- Proceedings of the National Academy of Sciences…
- 15 February 1994
An in vitro tissue culture cell model system for investigating the biochemical mechanisms involved in the neurodegenerative actions of beta-amyloid has been established. Using rat pheochromocytoma… Expand
L-685,458, an aspartyl protease transition state mimic, is a potent inhibitor of amyloid beta-protein precursor gamma-secretase activity.
- M. Shearman, D. Beher, +7 authors J. L. Castro
- Medicine
- Biochemistry
- 2000
Progressive cerebral amyloid beta-protein (A beta) deposition is believed to play a central role in the pathogenesis of Alzheimer's disease (AD). Elevated levels of A beta(42) peptide formation have… Expand
Photoactivated gamma-secretase inhibitors directed to the active site covalently label presenilin 1.
- Y. Li, M. Xu, +15 authors S. J. Gardell
- Medicine
- Nature
- 2000
Cleavage of amyloid precursor protein (APP) by the beta- and gamma-secretases generates the amino and carboxy termini, respectively, of the A beta amyloidogenic peptides A beta40 and A beta42--the… Expand
The toxicity in vitro of beta-amyloid protein.
- L. Iversen, R. Mortishire-Smith, S. Pollack, M. Shearman
- Chemistry, Medicine
- The Biochemical journal
- 1 October 1995
Fenton chemistry and oxidative stress mediate the toxicity of the β-amyloid peptide in a Drosophila model of Alzheimer’s disease
- T. Rival, R. M. Page, +10 authors D. Lomas
- Biology, Medicine
- The European journal of neuroscience
- 1 April 2009
The mechanism by which aggregates of the β‐amyloid peptide (Aβ) mediate their toxicity is uncertain. We show here that the expression of the 42‐amino‐acid isoform of Aβ (Aβ1–42) changes the… Expand