The mechanism of γ-Secretase dysfunction in familial Alzheimer disease. - Wikidata - wikimedia - TriplyDB

The mechanism of γ-Secretase dysfunction in familial Alzheimer disease.

The mechanism of γ-Secretase dysfunction in familial Alzheimer disease.

http://www.wikidata.org/entity/Q36000134

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The amyloid hypothesis of Alzheimer's disease at 25 years Fluid Biomarkers in Clinical Trials of Alzheimer's Disease Therapeutics γ-Secretase inhibitors and modulators.Toward the structure of presenilin/γ-secretase and presenilin homologs Early etiology of Alzheimer's disease: tipping the balance toward autophagy or endosomal dysfunction?Proteolysis inside the Membrane Is a Rate-Governed Reaction Not Driven by Substrate Affinity Familial Alzheimer’s mutations within APPTM increase Aβ42 production by enhancing accessibility of ε-cleavage site Three dimensions of the amyloid hypothesis: time, space and 'wingmen'Genetic diagnosis and prognosis of Alzheimer's disease: challenges and opportunities Pathogenic Parkinson's disease mutations across the functional domains of LRRK2 alter the autophagic/lysosomal response to starvation Identification of the novel activity-driven interaction between synaptotagmin 1 and presenilin 1 links calcium, synapse, and amyloid beta Modulators of γ-secretase activity can facilitate the toxic side-effects and pathogenesis of Alzheimer's disease Allosteric regulation of rhomboid intramembrane proteolysis γ-secretase binding sites in aged and Alzheimer's disease human cerebrum: the choroid plexus as a putative origin of CSF Aβ Aβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments.Changed membrane integration and catalytic site conformation are two mechanisms behind the increased Aβ42/Aβ40 ratio by presenilin 1 familial Alzheimer-linked mutations.Increased in vivo amyloid-β42 production, exchange, and loss in presenilin mutation carriers Inferring data-specific micro-RNA function through the joint ranking of micro-RNA and pathways from matched micro-RNA and gene expression data.γ-Secretase Inhibitors and Modulators Induce Distinct Conformational Changes in the Active Sites of γ-Secretase and Signal Peptide Peptidase The familial Alzheimer's disease APPV717I mutation alters APP processing and Tau expression in iPSC-derived neurons.Identification and Preclinical Pharmacology of the γ-Secretase Modulator BMS-869780.Allosteric regulation of γ-secretase activity by a phenylimidazole-type γ-secretase modulator.Brain imaging and fluid biomarker analysis in young adults at genetic risk for autosomal dominant Alzheimer's disease in the presenilin 1 E280A kindred: a case-control study.A critique of the drug discovery and phase 3 clinical programs targeting the amyloid hypothesis for Alzheimer disease.Characterization of intermediate steps in amyloid beta (Aβ) production under near-native conditions.The FAM3 superfamily member ILEI ameliorates Alzheimer's disease-like pathology by destabilizing the penultimate amyloid-β precursor.The epigenetic dimension of Alzheimer's disease: causal, consequence, or curiosity?The Alzheimer disease protective mutation A2T modulates kinetic and thermodynamic properties of amyloid-β (Aβ) aggregation.Alzheimer presenilin-1 mutations dramatically reduce trimming of long amyloid β-peptides (Aβ) by γ-secretase to increase 42-to-40-residue Aβ.Discovery of a novel pharmacological and structural class of gamma secretase modulators derived from the extract of Actaea racemosa.The pathogenic aβ43 is enriched in familial and sporadic Alzheimer disease Mechanism of intramembrane cleavage of alcadeins by γ-secretase.Visualization and quantification of APP intracellular domain-mediated nuclear signaling by bimolecular fluorescence complementation.The dynamic conformational landscape of gamma-secretase.γ-Secretase processing and effects of γ-secretase inhibitors and modulators on long Aβ peptides in cells.Evidence of a novel mechanism for partial γ-secretase inhibition induced paradoxical increase in secreted amyloid β protein Cleavage of amyloid precursor protein by an archaeal presenilin homologue PSH Effect of potent γ-secretase modulator in human neurons derived from multiple presenilin 1-induced pluripotent stem cell mutant carriers.Presenilin-1 Dependent Neurogenesis Regulates Hippocampal Learning and Memory.Alzheimer's Disease: Lessons Learned from Amyloidocentric Clinical Trials.

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The mechanism of γ-Secretase dysfunction in familial Alzheimer disease.

http://www.wikidata.org/entity/Q36000134

description

2012 nî lūn-bûn

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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2012年论文

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2012年论文

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name

The mechanism of γ-Secretase dysfunction in familial Alzheimer disease.

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The mechanism of γ-Secretase dysfunction in familial Alzheimer disease.

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The mechanism of γ-Secretase dysfunction in familial Alzheimer disease.

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The mechanism of γ-Secretase dysfunction in familial Alzheimer disease.

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The mechanism of γ-Secretase dysfunction in familial Alzheimer disease.

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The mechanism of γ-Secretase dysfunction in familial Alzheimer disease.

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The EMBO Journal

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The mechanism of γ-Secretase dysfunction in familial Alzheimer disease.

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Annelies Vandersteen

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Eric Karran

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Frederic Rousseau

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Harrie Gijsen

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Hermann Esselmann

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Iryna Benilova

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Kerensa Broersen

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Leen Bammens

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Lucía Chávez-Gutiérrez

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Lujia Zhou

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P2860

Neurotoxicity of Alzheimer's disease Aβ peptides is induced by small changes in the Aβ42 to Aβ40 ratio

When loss is gain: reduced presenilin proteolytic function leads to increased Abeta42/Abeta40. Talking Point on the role of presenilin mutations in Alzheimer disease

Loss-of-function presenilin mutations in Alzheimer disease. Talking Point on the role of presenilin mutations in Alzheimer disease

The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics

Increased amyloid-beta42(43) in brains of mice expressing mutant presenilin 1

Interaction with telencephalin and the amyloid precursor protein predicts a ring structure for presenilins

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

Identification of distinct gamma-secretase complexes with different APH-1 variants

Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins

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

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2261-2274

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10.1038/EMBOJ.2012.79

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10

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31

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Bart De Strooper

Joost Schymkowitz

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2012-04-13T00:00:00Z

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224038799

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22505025

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Alzheimer's disease

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