(Q40708428)

22 September 2017

title

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

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22 September 2017

4

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22 September 2017

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Christian Haass

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Dieter Edbauer

3

object named as

Dieter Edbauer

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22 September 2017

Harald Steiner

1

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22 September 2017

Edith Winkler

2

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22 September 2017

Gabriele Basset

5

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22 September 2017

Aya Yamasaki

6

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22 September 2017

Marcus Kostka

7

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22 September 2017

language of work or name

English

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publication date

26 August 2002

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Journal of Biological Chemistry

22 September 2017

published in

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22 September 2017

volume

277

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22 September 2017

issue

42

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22 September 2017

page(s)

39062-39065

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Intramembrane proteolysis by presenilins

22 September 2017

cites work

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https://api.crossref.org/works/10.1074%2FJBC.C200469200

Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

Effects of PS1 deficiency on membrane protein trafficking in neurons

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

Total inactivation of gamma-secretase activity in presenilin-deficient embryonic stem cells.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

The Role of presenilins in gamma-secretase activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

Transition-state analogue inhibitors of gamma-secretase bind directly to presenilin-1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

Identification of a novel family of presenilin homologues

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

The Proteolytic Fragments of the Alzheimer's Disease-associated Presenilin-1 Form Heterodimers and Occur as a 100–150-kDa Molecular Mass Complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

The presenilin 1 protein is a component of a high molecular weight intracellular complex that contains beta-catenin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

Presenilin 1 is linked with gamma-secretase activity in the detergent solubilized state

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

Presenilin and nicastrin regulate each other and determine amyloid beta-peptide production via complex formation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

Nicastrin is required for gamma-secretase cleavage of the Drosophila Notch receptor

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

Notch signaling: from the outside in

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

Proteolytic processing of the Alzheimer disease-associated presenilin-1 generates an in vivo substrate for protein kinase C.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

Proteolytic fragments of the Alzheimer's disease associated presenilins-1 and -2 are phosphorylated in vivo by distinct cellular mechanisms

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

Mutation of the beta-amyloid precursor protein in familial Alzheimer's disease increases beta-protein production

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

Presenilin 2 deficiency causes a mild pulmonary phenotype and no changes in amyloid precursor protein processing but enhances the embryonic lethal phenotype of presenilin 1 deficiency

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

Amyloidogenic function of the Alzheimer's disease-associated presenilin 1 in the absence of endoproteolysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C200469200

21 January 2018

Identifiers

DOI

10.1074/JBC.C200469200

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22 September 2017

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