Modulation of gamma-secretase specificity using small molecule allosteric inhibitors. - Wikidata - awgldk - TriplyDB

Modulation of gamma-secretase specificity using small molecule allosteric inhibitors.

Modulation of gamma-secretase specificity using small molecule allosteric inhibitors.

http://www.wikidata.org/entity/Q33515793

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Allosteric regulation of rhomboid intramembrane proteolysis Targeting the γ-/β-secretase interaction reduces β-amyloid generation and ameliorates Alzheimer's disease-related pathogenesis Allosteric regulation of protease activity by small molecules.Modulation of gamma-secretase reduces beta-amyloid deposition in a transgenic mouse model of Alzheimer's disease.γ-Secretase Inhibitors and Modulators Induce Distinct Conformational Changes in the Active Sites of γ-Secretase and Signal Peptide Peptidase Central angiotensin II stimulation promotes β amyloid production in Sprague Dawley rats.Characterization of an atypical gamma-secretase complex from hematopoietic origin Dual role of alpha-secretase cleavage in the regulation of gamma-secretase activity for amyloid production.Activation and intrinsic gamma-secretase activity of presenilin 1.Long-range enhancer activity determines Myc sensitivity to Notch inhibitors in T cell leukemia Amyloid precursor protein selective gamma-secretase inhibitors for treatment of Alzheimer's disease.Substrate docking to γ-secretase allows access of γ-secretase modulators to an allosteric site.The dynamic conformational landscape of gamma-secretase.Nontranscriptional role of Hif-1α in activation of γ-secretase and notch signaling in breast cancer.Genomics of Dementia: APOE- and CYP2D6-Related Pharmacogenetics.Familial Alzheimer disease presenilin-1 mutations alter the active site conformation of γ-secretase Substrate recruitment of γ-secretase and mechanism of clinical presenilin mutations revealed by photoaffinity mapping.A novel high throughput 1536-well Notch1 γ -secretase AlphaLISA assay Identifying and characterizing promiscuous targets: implications for virtual screening.Protein fibrillation and nanoparticle interactions: opportunities and challenges.Development and mechanism of γ-secretase modulators for Alzheimer's disease.Intramembrane proteases as drug targets.Cell "vision": complementary factor of protein corona in nanotoxicology.Development of Sulfonamide Photoaffinity Inhibitors for Probing Cellular γ-Secretase.Piperidine acetic acid based γ-secretase modulators directly bind to Presenilin-1.Development of CBAP-BPyne, a probe for γ-secretase and presenilinase.Inhibition of notch signaling in glioblastoma targets cancer stem cells via an endothelial cell intermediate.Reciprocal relationship between APP positioning relative to the membrane and PS1 conformation.Development of clickable active site-directed photoaffinity probes for γ-secretase.Structure-activity relationships in peptide modulators of β-amyloid protein aggregation: variation in α,α-disubstitution results in altered aggregate size and morphology In vivo manifestation of Notch related phenotypes in zebrafish treated with Alzheimer's amyloid reducing gamma-secretase inhibitors.Targeting cancer stem cells: a new therapy to cure cancer patients.BMS-708,163 targets presenilin and lacks notch-sparing activity.Competition between homodimerization and cholesterol binding to the C99 domain of the amyloid precursor protein.Allosteric Modulation of Intact γ-Secretase Structural Dynamics.Stepwise processing analyses of the single-turnover PCSK9 protease reveal its substrate sequence specificity and link clinical genotype to lipid phenotype.Toward a general predictive QSAR model for gamma-secretase inhibitors.Structural and Chemical Biology of Presenilin Complexes.What the halted phase III γ-secretase inhibitor trial may (or may not) be telling us.Future Trends in the Pharmacogenomics of Brain Disorders and Dementia: Influence of APOE and CYP2D6 Variants.

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Modulation of gamma-secretase specificity using small molecule allosteric inhibitors.

http://www.wikidata.org/entity/Q33515793

description

2009 nî lūn-bûn

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2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2009 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

Modulation of gamma-secretase specificity using small molecule allosteric inhibitors.

@ast

Modulation of gamma-secretase specificity using small molecule allosteric inhibitors.

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Modulation of gamma-secretase specificity using small molecule allosteric inhibitors.

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type

label

Modulation of gamma-secretase specificity using small molecule allosteric inhibitors.

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Modulation of gamma-secretase specificity using small molecule allosteric inhibitors.

@en

Modulation of gamma-secretase specificity using small molecule allosteric inhibitors.

@nl

prefLabel

Modulation of gamma-secretase specificity using small molecule allosteric inhibitors.

@ast

Modulation of gamma-secretase specificity using small molecule allosteric inhibitors.

@en

Modulation of gamma-secretase specificity using small molecule allosteric inhibitors.

@nl

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PNAS.0910757106

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Proceedings of the National Academy of Sciences of the United States of America

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Modulation of gamma-secretase specificity using small molecule allosteric inhibitors.

@en

P2093

Christopher C Shelton

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

Deming Chau

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

Hakim Djaballah

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

Hui Zheng

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

Lei Zhu

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

Li Yang

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

Rong Wang

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Yue-Ming Li

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P2860

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

Gleevec inhibits beta-amyloid production but not Notch cleavage

On the size of the active site in proteases. I. Papain

Alzheimer's disease: genes, proteins, and therapy

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

Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans

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

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

Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain

Presenilin clinical mutations can affect gamma-secretase activity by different mechanisms

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20228-20233

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10.1073/PNAS.0910757106

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48

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106

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2009-11-11T00:00:00Z

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38083502

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19906985

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allosteric inhibitor

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2787169

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