(Q44538958)

3 December 2017

title

Presenilin-1 interacts directly with the beta-site amyloid protein precursor cleaving enzyme (BACE1). (English)

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3 December 2017

1

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3 December 2017

2

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3 December 2017

Valérie Bourdages

3

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3 December 2017

Chantal Godin

4

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3 December 2017

Mélissa Ferland

5

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3 December 2017

Madeleine Carreau

6

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3 December 2017

Georges Lévesque

7

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3 December 2017

publication date

1 August 2003

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3 December 2017

published in

Neurobiology of Disease

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3 December 2017

volume

13

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3 December 2017

issue

3

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3 December 2017

page(s)

238-245

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Endogenous beta-amyloid production in presenilin-deficient embryonic mouse fibroblasts

3 December 2017

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Nicastrin binds to membrane-tethered Notch

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aph-1 and pen-2 are required for Notch pathway signaling, gamma-secretase cleavage of betaAPP, and presenilin protein accumulation

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BACE1 interacts with nicastrin

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Presenilin-1 affects trafficking and processing of betaAPP and is targeted in a complex with nicastrin to the plasma membrane

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Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP

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Presenilin 1 is required for maturation and cell surface accumulation of nicastrin

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Alzheimer presenilins in the nuclear membrane, interphase kinetochores, and centrosomes suggest a role in chromosome segregation

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A presenilin-1/gamma-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions

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7 January 2021

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Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE

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7 January 2021

The transmembrane domain of the Alzheimer's beta-secretase (BACE1) determines its late Golgi localization and access to beta -amyloid precursor protein (APP) substrate

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7 January 2021

Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and betaAPP processing

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7 January 2021

Presenilins are required for gamma-secretase cleavage of beta-APP and transmembrane cleavage of Notch-1

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7 January 2021

Presenilin-1 protects against neuronal apoptosis caused by its interacting protein PAG

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7 January 2021

10.1016/S0969-9961(03)00035-4

Identifiers

DOI

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3 December 2017

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