Presenilin is the molecular target of acidic γ-secretase modulators in living cells. - Wikidata - awgldk - TriplyDB

Presenilin is the molecular target of acidic γ-secretase modulators in living cells.

Presenilin is the molecular target of acidic γ-secretase modulators in living cells.

http://www.wikidata.org/entity/Q34125419

about

Toward the structure of presenilin/γ-secretase and presenilin homologs Identification and Preclinical Pharmacology of the γ-Secretase Modulator BMS-869780.A subset of membrane-altering agents and γ-secretase modulators provoke nonsubstrate cleavage by rhomboid proteases Independent relationship between amyloid precursor protein (APP) dimerization and γ-secretase processivity.Amyloid-PET predicts inhibition of de novo plaque formation upon chronic γ-secretase modulator treatment Cholestenoic acid, an endogenous cholesterol metabolite, is a potent γ-secretase modulator.Modulation of Aβ42 in vivo by γ-secretase modulator in primates and humans.Second generation γ-secretase modulators exhibit different modulation of Notch β and Aβ production.γ-Secretase modulator (GSM) photoaffinity probes reveal distinct allosteric binding sites on presenilin.Efficacy of SPI-1865, a novel gamma-secretase modulator, in multiple rodent models.Robust Translation of γ-Secretase Modulator Pharmacology across Preclinical Species and Human Subjects.Development and mechanism of γ-secretase modulators for Alzheimer's disease.Complex relationships between substrate sequence and sensitivity to alterations in γ-secretase processivity induced by γ-secretase modulators APP processing in human pluripotent stem cell-derived neurons is resistant to NSAID-based γ-secretase modulation.Development of Sulfonamide Photoaffinity Inhibitors for Probing Cellular γ-Secretase.γ-Secretase Modulators: Can We Combine Potency with Safety?Competition between homodimerization and cholesterol binding to the C99 domain of the amyloid precursor protein.

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Presenilin is the molecular target of acidic γ-secretase modulators in living cells.

http://www.wikidata.org/entity/Q34125419

description

2012 nî lūn-bûn

@nan

2012 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2012年の論文

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2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Presenilin is the molecular target of acidic γ-secretase modulators in living cells.

@ast

Presenilin is the molecular target of acidic γ-secretase modulators in living cells.

@en

Presenilin is the molecular target of acidic γ-secretase modulators in living cells.

@nl

type

label

Presenilin is the molecular target of acidic γ-secretase modulators in living cells.

@ast

Presenilin is the molecular target of acidic γ-secretase modulators in living cells.

@en

Presenilin is the molecular target of acidic γ-secretase modulators in living cells.

@nl

prefLabel

Presenilin is the molecular target of acidic γ-secretase modulators in living cells.

@ast

Presenilin is the molecular target of acidic γ-secretase modulators in living cells.

@en

Presenilin is the molecular target of acidic γ-secretase modulators in living cells.

@nl

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JOURNAL.PONE.0030484

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Presenilin is the molecular target of acidic γ-secretase modulators in living cells.

@en

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Andreas Rennhack

http://www.w3.org/2001/XMLSchema#string

Bruno Bulic

http://www.w3.org/2001/XMLSchema#string

Claus U Pietrzik

http://www.w3.org/2001/XMLSchema#string

Julia Ness

http://www.w3.org/2001/XMLSchema#string

Sandra Baches

http://www.w3.org/2001/XMLSchema#string

Sascha Weggen

http://www.w3.org/2001/XMLSchema#string

Thorsten Jumpertz

http://www.w3.org/2001/XMLSchema#string

P2860

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

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

Signal peptide peptidase: biochemical properties and modulation by nonsteroidal antiinflammatory drugs

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

Evidence that nonsteroidal anti-inflammatory drugs decrease amyloid beta 42 production by direct modulation of gamma-secretase activity.

Modulation of gamma-secretase reduces beta-amyloid deposition in a transgenic mouse model of Alzheimer's disease.

Beta-amyloid precursor protein mutants respond to gamma-secretase modulators

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

Amyloid beta 42 peptide (Abeta42)-lowering compounds directly bind to Abeta and interfere with amyloid precursor protein (APP) transmembrane dimerization.

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

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e30484

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scholarly article

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10.1371/JOURNAL.PONE.0030484

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1

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7

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2012-01-06T00:00:00Z

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221741649

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22238696

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3253113

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