Changes in gamma-secretase activity and specificity caused by the introduction of consensus aspartyl protease active motif in Presenilin 1.

Photoactivated gamma-secretase inhibitors directed to the active site covalently label presenilin 1.

Presenilin clinical mutations can affect gamma-secretase activity by different mechanisms.

Presenilin-1 and presenilin-2 exhibit distinct yet overlapping gamma-secretase activities.

Conserved "PAL" sequence in presenilins is essential for gamma-secretase activity, but not required for formation or stabilization of gamma-secretase complexes.

Generation of Abeta38 and Abeta42 is independently and differentially affected by familial Alzheimer disease-associated presenilin mutations and gamma-secretase modulation.

Insensitivity to Abeta42-lowering nonsteroidal anti-inflammatory drugs and gamma-secretase inhibitors is common among aggressive presenilin-1 mutations.

Familial Alzheimer disease-linked presenilin 1 variants enhance production of both Abeta 1-40 and Abeta 1-42 peptides that are only partially sensitive to a potent aspartyl protease transition state inhibitor of "gamma-secretase".

Intracellular site of gamma-secretase cleavage for Abeta42 generation in neuro 2a cells harbouring a presenilin 1 mutation.

The transmembrane aspartates in presenilin 1 and 2 are obligatory for gamma-secretase activity and amyloid beta-protein generation.

Cell surface presenilin-1 participates in the gamma-secretase-like proteolysis of Notch.

A presenilin-independent aspartyl protease prefers the gamma-42 site cleavage.

Characterization of the reconstituted gamma-secretase complex from Sf9 cells co-expressing presenilin 1, nicastrin [correction of nacastrin], aph-1a, and pen-2.

Low density lipoprotein receptor-related protein (LRP) interacts with presenilin 1 and is a competitive substrate of the amyloid precursor protein (APP) for gamma-secretase.

Genes and mechanisms involved in beta-amyloid generation and Alzheimer's disease.

Conserved residues within the putative active site of gamma-secretase differentially influence enzyme activity and inhibitor binding.

Aspartyl protease inhibitor pepstatin binds to the presenilins of Alzheimer's disease.

Presenilin 1 mutations activate gamma 42-secretase but reciprocally inhibit epsilon-secretase cleavage of amyloid precursor protein (APP) and S3-cleavage of notch.

Identification of gamma-secretase inhibitor potency determinants on presenilin.