Results 41 to 50 of about 6,021 (217)

Gamma-secretase composed of PS1/Pen2/Aph1a can cleave notch and amyloid precursor protein in the absence of nicastrin [PDF]

open access: yes, 2010
γ-secretase is a multiprotein intramembrane-cleaving protease with a growing list of protein substrates including the Notch receptors and the amyloid precursor protein.
Ilagan, Ma. Xenia G   +3 more
core   +2 more sources

Hidradenitis Suppurativa: A Systematic Review Integrating Inflammatory Pathways Into a Cohesive Pathogenic Model

open access: yesFrontiers in Immunology, 2018
Background: The pathogenesis of hidradenitis suppurativa (HS) is not fully understood. This systematic review examined the latest evidence for molecular inflammatory pathways involved in HS as a chronic inflammatory skin disease.Methods: A systematic ...
Allard R. J. V. Vossen   +2 more
doaj   +1 more source

Increased expression of PS1 is sufficient to elevate the level and activity of γ-secretase in vivo. [PDF]

open access: yesPLoS ONE, 2011
Increase in the generation and deposition of amyloid-β (Aβ) plays a central role in the development of Alzheimer's Disease (AD). Elevation of the activity of γ-secretase, a key enzyme required for the generation for Aβ, can thus be a potential risk ...
Tong Li   +5 more
doaj   +1 more source

The very many faces of presenilins and the γ-secretase complex [PDF]

open access: yes, 2013
Presenilin is a central, catalytic component of the γ-secretase complex which conducts intramembrane cleavage of various protein substrates. Although identified and mainly studied through its role in the development of amyloid plaques in Alzheimer ...
Michalina Smolarkiewicz   +2 more
core   +1 more source

In silico Analysis of Gamma-Secretase-Complex Mutations in Hidradenitis Suppurativa Demonstrates Disease-Specific Substrate Recognition and Cleavage Alterations

open access: yesFrontiers in Medicine, 2019
Background: Familial Hidradenitis Suppurativa and Familial Alzheimer's Disease are both associated with Gamma-Secretase Complex mutations; however, the two diseases are not epidemiologically associated. Understanding the molecular differences between the
John W. Frew   +2 more
doaj   +1 more source

Magnesium Ions Inhibit the Expression of Tumor Necrosis Factor α and the Activity of γ-Secretase in a β-Amyloid Protein-Dependent Mechanism in APP/PS1 Transgenic Mice

open access: yesFrontiers in Molecular Neuroscience, 2018
Alzheimer’s disease (AD) is a neurodegenerative disease characterized by cognitive impairment. The neuropathological features of AD are the aggregation of extracellular amyloid β-protein (Aβ) and tau phosphorylation.
Xin Yu   +6 more
doaj   +1 more source

Maternal High Fat Diet Anticipates the AD-like Phenotype in 3xTg-AD Mice by Epigenetic Dysregulation of Aβ Metabolism

open access: yesCells, 2023
Maternal overnutrition has been reported to affect brain plasticity of the offspring by altering gene expression, regulating both synaptic plasticity and adult neurogenesis.
Francesca Natale   +6 more
doaj   +1 more source

Different types of γ-secretes complexes and their effect on substrate processing [PDF]

open access: yes, 2012
The γ-secretase complex is a transmembrane aspartyl protease that generates the Alzheimer disease (AD) related amyloid β-peptide (Aβ) from the amyloid precursor protein (APP). The γ- secretase complex cleaves APP at two different sites (γ- and ε-sites)
Pamrén, Annelie
core   +1 more source

The γ-secretase complex: from structure to function

open access: yesFrontiers in Cellular Neuroscience, 2014
One of the most critical pathological features of Alzheimer’s disease (AD) is the accumulation of β-amyloid (Aβ) peptides that form extracellular senile plaques in the brain. Aβ is derived from β-amyloid precursor protein through sequential cleavage by β-
Xian eZhang   +4 more
doaj   +1 more source

Proteomic Profiling of γ-Secretase Substrates and Mapping of Substrate Requirements [PDF]

open access: yes, 2011
The presenilin/γ-secretase complex, an unusual intramembrane aspartyl protease, plays an essential role in cellular signaling and membrane protein turnover.
Elias, Joshua E   +3 more
core   +1 more source

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