Results 51 to 60 of about 14,107 (263)

Alzheimer’s Disease: A Molecular View of β-Amyloid Induced Morbific Events

open access: yesBiomedicines, 2021
Amyloid-β (Aβ) is a dynamic peptide of Alzheimer’s disease (AD) which accelerates the disease progression. At the cell membrane and cell compartments, the amyloid precursor protein (APP) undergoes amyloidogenic cleavage by β- and γ-secretases and ...
Rajmohamed Mohamed Asik   +8 more
doaj   +1 more source

Hypoxic regulation of ion channel function and expression [PDF]

open access: yes, 2002
Acute hypoxia regulates the activity of specific ion channels in a rapid and reversible manner. Such effects underlie appropriate cellular responses to hypoxia which are designed to initiate cardiorespiratory reflexes and contribute importantly to other ...
Peers, C.
core   +1 more source

Apolipoprotein E modulates γ‐secretase cleavage of the amyloid precursor protein [PDF]

open access: yesJournal of Neurochemistry, 2004
AbstractPolymorphisms in the apolipoprotein E (APOE) gene affect the risk of Alzheimer disease and the amount of amyloid β‐protein (Aβ) deposited in the brain. The apoE protein reduces Aβ levels in conditioned media from cells in culture, possibly through Aβ clearance mechanisms.
Michael C, Irizarry   +9 more
openaire   +2 more sources

Emerging Alternative Proteinases in APP Metabolism and Alzheimer’s Disease Pathogenesis: A Focus on MT1-MMP and MT5-MMP

open access: yesFrontiers in Aging Neuroscience, 2019
Processing of amyloid beta precursor protein (APP) into amyloid-beta peptide (Aβ) by β-secretase and γ-secretase complex is at the heart of the pathogenesis of Alzheimer’s disease (AD).
Laura García-González   +3 more
doaj   +1 more source

The proton-pump inhibitor lansoprazole enhances amyloid beta production.

open access: yesPLoS ONE, 2013
A key event in the pathogenesis of Alzheimer's disease (AD) is the accumulation of amyloid-β (Aβ) species in the brain, derived from the sequential cleavage of the amyloid precursor protein (APP) by β- and γ-secretases.
Nahuai Badiola   +8 more
doaj   +1 more source

Inhibitory effect of a tyrosine-fructose Maillard reaction product, 2,4-bis(p-hydroxyphenyl)-2-butenal on amyloid-β generation and inflammatory reactions via inhibition of NF-κB and STAT3 activation in cultured astrocytes and microglial BV-2 cells [PDF]

open access: yes, 2011
Background Amyloidogenesis is linked to neuroinflammation. The tyrosine-fructose Maillard reaction product, 2,4-bis(p-hydroxyphenyl)-2-butenal, possesses anti-inflammatory properties in cultured macrophages, and in an arthritis animal model ...
Young-Jung Lee   +7 more
core   +2 more sources

P2Y2 Nucleotide Receptors Enhance α-Secretase-dependent Amyloid Precursor Protein Processing [PDF]

open access: yesJournal of Biological Chemistry, 2005
The amyloid precursor protein (APP) is proteolytically processed by beta- and gamma-secretases to release amyloid beta, the main component in senile plaques found in the brains of patients with Alzheimer disease. Alternatively, APP can be cleaved within the amyloid beta domain by alpha-secretase releasing the non-amyloidogenic product sAPP alpha, which
Jean M, Camden   +6 more
openaire   +2 more sources

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

A resorcinarene for inhibition of Aβ fibrillation. [PDF]

open access: yes, 2017
Amyloid-β peptides (Aβ) fibrillation is the hallmark of Alzheimer's disease (AD). However, it has been challenging to discover potent agents in order to inhibit Aβ fibrillation.
Han, Xu   +8 more
core   +1 more source

The Alzheimer’s Disease γ-Secretase Generates Higher 42:40 Ratios for β-Amyloid Than for p3 Peptides

open access: yesCell Reports, 2017
Alzheimer’s disease is characterized by intracerebral deposition of β-amyloid (Aβ). While Aβ40 is the most abundant form, neurotoxicity is mainly mediated by Aβ42.
Gabriele Siegel   +5 more
doaj   +1 more source

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