(Q44287879)

English

Selecting cells with different Alzheimer's disease gamma-secretase activity using FACS. Differential effect on presenilin exon 9 gamma- and epsilon-cleavage

scientific article published in February 2003

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Europe PubMed Central

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1 December 2017

Selecting cells with different Alzheimer's disease gamma-secretase activity using FACS. Differential effect on presenilin exon 9 gamma- and epsilon-cleavage (English)

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Europe PubMed Central

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1 December 2017

Alzheimer's disease

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Jose A. Villadangos

4

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Europe PubMed Central

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1 December 2017

7

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Europe PubMed Central

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1 December 2017

Konrad Beyreuther

5

object named as

Konrad Beyreuther

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Europe PubMed Central

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1 December 2017

Colin L. Masters

6

object named as

Colin L Masters

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1 December 2017

author name string

M Fleur Sernee

1

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Europe PubMed Central

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1 December 2017

Geneviève Evin

2

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1 December 2017

Janetta G Culvenor

3

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1 December 2017

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publication date

1 February 2003

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1 December 2017

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1 December 2017

270

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1 December 2017

3

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1 December 2017

495-506

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1 December 2017

Regulation of APP cleavage by alpha-, beta- and gamma-secretases

1 reference

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Biogenesis and metabolism of Alzheimer's disease Abeta amyloid peptides

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Alzheimer's disease. A firm base for drug development.

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Characterization of a presenilin-mediated amyloid precursor protein carboxyl-terminal fragment gamma. Evidence for distinct mechanisms involved in gamma -secretase processing of the APP and Notch1 transmembrane domains

1 reference

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21 January 2018

A novel epsilon-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing

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Mechanism of the cleavage specificity of Alzheimer's disease gamma-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein

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Biochemical detection of Abeta isoforms: implications for pathogenesis, diagnosis, and treatment of Alzheimer's disease

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Notch and presenilin: a proteolytic mechanism emerges

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Activity-dependent isolation of the presenilin- gamma -secretase complex reveals nicastrin and a gamma substrate

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PEN-2 is an integral component of the gamma-secretase complex required for coordinated expression of presenilin and nicastrin

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APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos

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

1 reference

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21 January 2018

Mammalian APH-1 interacts with presenilin and nicastrin and is required for intramembrane proteolysis of amyloid-beta precursor protein and Notch

1 reference

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Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity

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A loss of function mutation of presenilin-2 interferes with amyloid beta-peptide production and notch signaling

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Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene

1 reference

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A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain

1 reference

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21 January 2018

A common enzyme connects notch signaling and Alzheimer's disease

1 reference

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Presenilins mediate a dual intramembranous gamma-secretase cleavage of Notch-1.

1 reference

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21 January 2018

Notch signaling: from the outside in

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Transcription activation by the adenovirus E1a protein

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Analysis of heterogeneous A4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay.

1 reference

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Presenilin 2 expression in neuronal cells: induction during differentiation of embryonic carcinoma cells.

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The C-terminal fragment of the Alzheimer's disease amyloid protein precursor is degraded by a proteasome-dependent mechanism distinct from gamma-secretase

1 reference

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L-685,458, an aspartyl protease transition state mimic, is a potent inhibitor of amyloid beta-protein precursor gamma-secretase activity

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21 January 2018

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

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A substrate-based difluoro ketone selectively inhibits Alzheimer's gamma-secretase activity.

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Release of signal peptide fragments into the cytosol requires cleavage in the transmembrane region by a protease activity that is specifically blocked by a novel cysteine protease inhibitor

1 reference

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21 January 2018

The intramembrane cleavage site of the amyloid precursor protein depends on the length of its transmembrane domain

1 reference

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Alternative, non-secretase processing of Alzheimer's beta-amyloid precursor protein during apoptosis by caspase-6 and -8.

1 reference

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Proteolytic processing of the Alzheimer's disease amyloid precursor protein within its cytoplasmic domain by caspase-like proteases.

1 reference

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GAL4-VP16 is an unusually potent transcriptional activator

1 reference

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gamma-secretase cleavage is distinct from endoplasmic reticulum degradation of the transmembrane domain of the amyloid precursor protein

1 reference

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21 January 2018

Presenilin-dependent gamma-secretase processing of beta-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch

1 reference

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Complex N-linked glycosylated nicastrin associates with active gamma-secretase and undergoes tight cellular regulation

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Identification of a novel family of presenilin homologues

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Identification of signal peptide peptidase, a presenilin-type aspartic protease

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The biological and pathological function of the presenilin-1 Deltaexon 9 mutation is independent of its defect to undergo proteolytic processing

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A sensitive and quantitative assay for measuring cleavage of presenilin substrates

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Notch receptor cleavage depends on but is not directly executed by presenilins

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Proteasome inhibitors reduce luciferase and beta-galactosidase activity in tissue culture cells

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Generation of C-terminally truncated amyloid-beta peptides is dependent on gamma-secretase activity.

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Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation

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Multiple effects of aspartate mutant presenilin 1 on the processing and trafficking of amyloid precursor protein

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

1 reference

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Separation of presenilin function in amyloid beta-peptide generation and endoproteolysis of Notch

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Linear non-competitive inhibition of solubilized human gamma-secretase by pepstatin A methylester, L685458, sulfonamides, and benzodiazepines

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gamma -Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase

1 reference

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Presenilin-dependent gamma-secretase-like intramembrane cleavage of ErbB4.

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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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Proteolytic processing of low density lipoprotein receptor-related protein mediates regulated release of its intracellular domain

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Presenilin-dependent intramembrane proteolysis of CD44 leads to the liberation of its intracellular domain and the secretion of an Abeta-like peptide

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A Novel γ-Secretase Assay Based on Detection of the Putative C-terminal Fragment-γ of Amyloid β Protein Precursor

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gamma-Secretase, evidence for multiple proteolytic activities and influence of membrane positioning of substrate on generation of amyloid beta peptides of varying length

1 reference

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A novel substrate for analyzing Alzheimer's disease gamma-secretase

1 reference

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Distinct intramembrane cleavage of the beta-amyloid precursor protein family resembling gamma-secretase-like cleavage of Notch

1 reference

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Peptidomimetic probes and molecular modeling suggest that Alzheimer's gamma-secretase is an intramembrane-cleaving aspartyl protease

1 reference

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21 January 2018

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10.1046/J.1432-1033.2003.03405.X

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

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