(Q40165328)

English

Abeta42 overproduction associated with structural changes in the catalytic pore of gamma-secretase: common effects of Pen-2 N-terminal elongation and fenofibrate

scientific article published on 28 February 2007

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

18 September 2017

Abeta42 overproduction associated with structural changes in the catalytic pore of gamma-secretase: common effects of Pen-2 N-terminal elongation and fenofibrate (English)

1 reference

Europe PubMed Central

PubMed publication ID

18 September 2017

8

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Europe PubMed Central

PubMed publication ID

18 September 2017

author name string

Noriko Isoo

1

1 reference

Europe PubMed Central

PubMed publication ID

18 September 2017

Chihiro Sato

2

1 reference

Europe PubMed Central

PubMed publication ID

18 September 2017

Hiroyuki Miyashita

3

1 reference

Europe PubMed Central

PubMed publication ID

18 September 2017

Mitsuru Shinohara

4

1 reference

Europe PubMed Central

PubMed publication ID

18 September 2017

Nobumasa Takasugi

5

1 reference

Europe PubMed Central

PubMed publication ID

18 September 2017

Yuichi Morohashi

6

1 reference

Europe PubMed Central

PubMed publication ID

18 September 2017

Shoji Tsuji

7

1 reference

Europe PubMed Central

PubMed publication ID

18 September 2017

Takeshi Iwatsubo

9

1 reference

Europe PubMed Central

PubMed publication ID

18 September 2017

language of work or name

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publication date

28 February 2007

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Europe PubMed Central

PubMed publication ID

18 September 2017

number of pages

9

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based on heuristic

inferred from page(s)

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

18 September 2017

282

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Europe PubMed Central

PubMed publication ID

18 September 2017

17

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Europe PubMed Central

PubMed publication ID

18 September 2017

12388-12396

1 reference

Europe PubMed Central

PubMed publication ID

18 September 2017

gamma-secretase as a therapeutic target for treatment of Alzheimer's disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Gamma-secretase: proteasome of the membrane?

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

The gamma-secretase complex: membrane-embedded proteolytic ensemble

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Reconstitution of gamma-secretase activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

The role of presenilin cofactors in the gamma-secretase complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Selective reconstitution and recovery of functional gamma-secretase complex on budded baculovirus particles

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Structure of the catalytic pore of gamma-secretase probed by the accessibility of substituted cysteines.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Nicastrin functions as a gamma-secretase-substrate receptor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Assembly of the gamma-secretase complex involves early formation of an intermediate subcomplex of Aph-1 and nicastrin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Aph-1 contributes to the stabilization and trafficking of the gamma-secretase complex through mechanisms involving intermolecular and intramolecular interactions.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

A sequence within the first transmembrane domain of PEN-2 is critical for PEN-2-mediated endoproteolysis of presenilin 1.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Pen-2 is incorporated into the gamma-secretase complex through binding to transmembrane domain 4 of presenilin 1

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Evidence that the "NF" motif in transmembrane domain 4 of presenilin 1 is critical for binding with PEN-2.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Requirement of PEN-2 for stabilization of the presenilin N-/C-terminal fragment heterodimer within the gamma-secretase complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Both the sequence and length of the C terminus of PEN-2 are critical for intermolecular interactions and function of presenilin complexes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Length and overall sequence of the PEN-2 C-terminal domain determines its function in the stabilization of presenilin fragments

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

The mechanism of gamma-secretase activities through high molecular weight complex formation of presenilins is conserved in Drosophila melanogaster and mammals

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

PEN-2 enhances gamma-cleavage after presenilin heterodimer formation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

The presenilin 2 mutation (N141I) linked to familial Alzheimer disease (Volga German families) increases the secretion of amyloid beta protein ending at the 42nd (or 43rd) residue

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Sulindac sulfide is a noncompetitive gamma-secretase inhibitor that preferentially reduces Abeta 42 generation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Secretion of the Notch-1 Abeta-like peptide during Notch signaling

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

A subset of NSAIDs lower amyloidogenic Abeta42 independently of cyclooxygenase activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Diverse compounds mimic Alzheimer disease-causing mutations by augmenting Abeta42 production

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Nonsteroidal anti-inflammatory drugs lower Abeta42 and change presenilin 1 conformation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Familial Alzheimer's disease presenilin 1 mutations cause alterations in the conformation of presenilin and interactions with amyloid precursor protein.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Selected non-steroidal anti-inflammatory drugs and their derivatives target gamma-secretase at a novel site. Evidence for an allosteric mechanism.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Membrane topology of gamma-secretase component PEN-2.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Pen-2 is sequestered in the endoplasmic reticulum and subjected to ubiquitylation and proteasome-mediated degradation in the absence of presenilin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Electron microscopic structure of purified, active gamma-secretase reveals an aqueous intramembrane chamber and two pores

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

The initial substrate-binding site of gamma-secretase is located on presenilin near the active site

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

C-terminal Fragment of Presenilin Is the Molecular Target of a Dipeptidic γ-Secretase-specific Inhibitor DAPT (N-[N-(3,5-Difluorophenacetyl)-L-alanyl]-S-phenylglycinet-Butyl Ester)

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Three-dimensional structure of the γ-secretase complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M611549200

21 January 2018

Identifiers

10.1074/JBC.M611549200

1 reference

Europe PubMed Central

PubMed publication ID

18 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

18 September 2017

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