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

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

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

http://www.wikidata.org/entity/Q28290934

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Current Insights into Molecular Mechanisms of Alzheimer Disease and Their Implications for Therapeutic Approaches Gamma-secretase activating protein is a therapeutic target for Alzheimer's disease Neurotoxicity of Alzheimer's disease Aβ peptides is induced by small changes in the Aβ42 to Aβ40 ratio Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b Familial Alzheimer disease-linked mutations specifically disrupt Ca2+ leak function of presenilin 1 Role of presenilin 1 in structural plasticity of cortical dendritic spines in vivo Biological markers of amyloid beta-related mechanisms in Alzheimer's disease Protein aggregation in the brain: the molecular basis for Alzheimer's and Parkinson's diseases 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 Genes associated with Alzheimer's disease: an overview and current status Overview of Alzheimer's Disease and Some Therapeutic Approaches Targeting Aβ by Using Several Synthetic and Herbal Compounds The relevance of beta-amyloid on markers of Alzheimer's disease in clinically normal individuals and factors that influence these associations Meta-Review of CSF Core Biomarkers in Alzheimer's Disease: The State-of-the-Art after the New Revised Diagnostic Criteria Inconsistencies and controversies surrounding the amyloid hypothesis of Alzheimer's disease Epigenetics of Alzheimer's disease and frontotemporal dementia Physical exercise-induced adult neurogenesis: a good strategy to prevent cognitive decline in neurodegenerative diseases?Lysosome and calcium dysregulation in Alzheimer's disease: partners in crime The same gamma-secretase accounts for the multiple intramembrane cleavages of APP Phenylbutyric acid rescues endoplasmic reticulum stress-induced suppression of APP proteolysis and prevents apoptosis in neuronal cells Transgenic expression of the amyloid-beta precursor protein-intracellular domain does not induce Alzheimer's Disease-like traits in vivo Γ-secretase components as predictors of breast cancer outcome Synaptic activity prompts gamma-secretase-mediated cleavage of EphA4 and dendritic spine formation Generation and initial characterization of FDD knock in mice The canonical Notch signaling pathway: unfolding the activation mechanism.A beta oligomers - a decade of discovery Changed membrane integration and catalytic site conformation are two mechanisms behind the increased Aβ42/Aβ40 ratio by presenilin 1 familial Alzheimer-linked mutations.The Psen1-L166P-knock-in mutation leads to amyloid deposition in human wild-type amyloid precursor protein YAC transgenic mice.Gamma-secretase-dependent and -independent effects of presenilin1 on beta-catenin.Tcf-4 transcriptional activity Molecular mechanisms for Alzheimer's disease: implications for neuroimaging and therapeutics.Alzheimer's disease-linked mutations in presenilin-1 result in a drastic loss of activity in purified γ-secretase complexes.Modulation of gamma-secretase specificity using small molecule allosteric inhibitors.Distinct cerebrospinal fluid amyloid beta peptide signatures in sporadic and PSEN1 A431E-associated familial Alzheimer's disease.The large hydrophilic loop of presenilin 1 is important for regulating gamma-secretase complex assembly and dictating the amyloid beta peptide (Abeta) Profile without affecting Notch processing.Current status on Alzheimer disease molecular genetics: from past, to present, to future.Presenilin 1 mutants impair the self-renewal and differentiation of adult murine subventricular zone-neuronal progenitors via cell-autonomous mechanisms involving notch signaling.Presenilin/γ-secretase regulates neurexin processing at synapses Genetics and biology of Alzheimer's disease and frontotemporal lobar degeneration A presenilin-1 mutation identified in familial Alzheimer disease with cotton wool plaques causes a nearly complete loss of gamma-secretase activity Reexamining Alzheimer's disease: evidence for a protective role for amyloid-beta protein precursor and amyloid-beta

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

http://www.wikidata.org/entity/Q28290934

description

2006 nî lūn-bûn

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2006 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի փետրվարին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

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

@ast

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

@en

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

@nl

type

label

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

@ast

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

@en

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

@nl

prefLabel

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

@ast

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

@en

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

@nl

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J.1471-4159.2005.03578.X

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Journal of Neurochemistry

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

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Alexandra Tolia

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Hermann Esselmann

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Jan Verhamme

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Jens Wiltfang

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Katrien Horré

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Mostafa Bentahir

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Omar Nyabi

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P2860

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

Notch signaling: from the outside in

A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain

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

Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid beta-protein in both transfected cells and transgenic mice

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

Presenilin 1 mediates the turnover of telencephalin in hippocampal neurons via an autophagic degradative pathway

Coordinated and widespread expression of gamma-secretase in vivo: evidence for size and molecular heterogeneity

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732-42

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10.1111/J.1471-4159.2005.03578.X

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3

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96

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Bart De Strooper

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7365557

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