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Showing 1-30 of 357 results for "A8717" within Papers
Barbara Bettegazzi et al.
Cell death & disease, 12(8), 769-769 (2021-08-06)
Alzheimer's disease (AD) is the most common age-related neurodegenerative disorder. Increased Aβ production plays a fundamental role in the pathogenesis of the disease and BACE1, the protease that triggers the amyloidogenic processing of APP, is a key protein and a
Steven Klein et al.
Annals of neurology, 80(3), 456-460 (2016-07-17)
Dominant missense mutations in the amyloid β (Aβ) precursor protein (APP) gene have been implicated in early onset Alzheimer disease. These mutations alter protein structure to favor the pathologic production of Aβ. We report that homozygous nonsense mutations in APP
Tatiana Melnikova et al.
Neurobiology of disease, 96, 171-185 (2016-10-19)
Sex differences are a well-known phenomenon in Alzheimer's disease (AD), with women having a higher risk for AD than men. Many AD mouse models display a similar sex-dependent pattern, with females showing earlier cognitive deficits and more severe neuropathology than
Xiaoqi Hong et al.
Human molecular genetics, 23(4), 1056-1072 (2013-10-10)
Alzheimer's disease (AD) is a progressive neurodegenerative disorder characterized by a severe decline of memory performance. A widely studied AD mouse model is the APPswe/PSEN1ΔE9 (APP/PS1) strain, as mice exhibit amyloid plaques as well as impaired memory capacities. To test
Joshua H K Tam et al.
PloS one, 11(10), e0161445-e0161445 (2016-10-25)
The amyloid hypothesis posits that the production of β-amyloid (Aβ) aggregates leads to neurodegeneration and cognitive decline associated with AD. Aβ is produced by sequential cleavage of the amyloid precursor protein (APP) by β- and γ-secretase. While nascent APP is
Airong Li et al.
Human molecular genetics, 16(21), 2626-2639 (2007-08-21)
UBQLN1 variants have been associated with increased risk for late-onset Alzheimer's disease (AD). We produced transgenic Drosophila models that either silence (by RNAi) or overexpress the Drosophila ortholog of human UBQLN1, dUbqln. Silencing of dUbqln in the central nervous system
Ning Bai et al.
Cell reports, 40(2), 111062-111062 (2022-07-14)
Aging is a primary risk factor for neurodegenerative diseases, such as Alzheimer's disease (AD). SIRT2, an NAD+(nicotinamide adenine dinucleotide)-dependent deacetylase, accumulates in the aging brain. Here, we report that, in the amyloid precursor protein (APP)/PS1 transgenic mouse model of AD
Takahide Matsushima et al.
The Journal of biological chemistry, 287(23), 19715-19724 (2012-04-19)
Amyloid β-precursor protein (APP) is primarily cleaved by α- or β-secretase to generate membrane-bound, C-terminal fragments (CTFs). In turn, CTFs are potentially subject to a second, intramembrane cleavage by γ-secretase, which is active in a lipid raft-like membrane microdomain. Mature
YuHong Fu et al.
Brain communications, 4(3), fcac120-fcac120 (2022-05-28)
Alzheimer's disease is a devastating neurodegenerative disease that affects more women than men. The pathomechanism underlying the sex disparity, especially in the brain, is unclear. ABCA7 is one of the strongest susceptibility genes for Alzheimer's disease. It mediates the transport
Stefano Benvegnù et al.
Oncotarget, 8(52), 89439-89450 (2017-11-23)
Altered processing of the Amyloid Precursor Protein (APP) is a well-recognized central pathogenic mechanism in Alzheimer's Disease (AD), and regulation of APP processing is a major focus of research in the AD field. However, how age-associated cellular and molecular changes
Monica Gireud-Goss et al.
Molecular and cellular neurosciences, 108, 103542-103542 (2020-08-26)
The extracellular accumulation of amyloid β (Aβ) fragments of amyloid precursor protein (APP) in brain parenchyma is a pathological hallmark of Alzheimer's disease (AD). APP can be cleaved into Aβ on late endosomes/multivesicular bodies (MVBs). E3 ubiquitin ligases have been
Yoshinori Hiraoka et al.
Journal of neurochemistry, 102(5), 1595-1605 (2007-06-09)
Amyloid-beta (Abeta) peptide, the principal component of senile plaques in the brains of patients with Alzheimer's disease, is derived from proteolytic cleavage of amyloid precursor protein (APP) by beta- and gamma-secretases. Alternative cleavage of APP by alpha-secretase occurs within the
Weixi Feng et al.
Alzheimer's research & therapy, 12(1), 125-125 (2020-10-04)
Soluble beta-amyloid (Aβ) can be cleared from the brain through various mechanisms including enzymatic degradation, glial cell phagocytosis, transport across the blood-brain barrier, and glymphatic clearance. However, the relative contribution of each clearance system and their compensatory effects in delaying
Genetic studies in Alzheimer's disease.
Tang YP and Gershon E
Dialogues in Clinical Neuroscience, 5(1), 17-26 (2003)
Sven Lammich et al.
The Journal of biological chemistry, 286(52), 45063-45072 (2011-11-09)
Anti-amyloidogenic processing of the amyloid precursor protein APP by α-secretase prevents formation of the amyloid-β peptide, which accumulates in senile plaques of Alzheimer disease patients. α-Secretase belongs to the family of a disintegrin and metalloproteases (ADAMs), and ADAM10 is the
Marta Pera et al.
The EMBO journal, 36(22), 3356-3371 (2017-10-12)
In the amyloidogenic pathway associated with Alzheimer disease (AD), the amyloid precursor protein (APP) is cleaved by β-secretase to generate a 99-aa C-terminal fragment (C99) that is then cleaved by γ-secretase to generate the β-amyloid (Aβ) found in senile plaques.
Xibin Liang et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 25(44), 10180-10187 (2005-11-04)
Epidemiological studies demonstrate that chronic use of nonsteroidal anti-inflammatory drugs (NSAIDs) in normal aging populations reduces the risk of developing Alzheimer's disease (AD). NSAIDs inhibit the enzymatic activity of cyclooxygenase-1 (COX-1) and inducible COX-2, which catalyze the first committed step
Angélica Maria Sabogal-Guáqueta et al.
Pharmacological research, 129, 128-138 (2017-12-13)
Alzheimer's disease (AD) is a progressive neurodegenerative disorder that is pathologically characterized by the deposition of β-amyloid (βA) peptides in senile plaques and neurofibrillary tangles in the brain. Flavonoids have recently been used to prevent and treat a variety of
Jack T Rogers et al.
Journal of neurochemistry, 138(3), 479-494 (2016-05-22)
Iron supplementation ameliorates the neurotoxicity of the environmental contaminant lead (Pb); however, the mechanism remains undefined. Iron is an essential nutrient but high levels are toxic due to the catalytic generation of destructive hydroxyl radicals. Using human neuroblastoma SH-SY5Y cells
Casandra M Cartagena et al.
PloS one, 11(7), e0158576-e0158576 (2016-07-20)
Traumatic brain injury (TBI) is an established risk factor for the development of Alzheimer's disease (AD). Here the effects of severe penetrating TBI on APP and tau cleavage processing were investigated in a rodent model of penetrating ballistic-like brain injury
Hyo-Jin Park et al.
The EMBO journal, 34(12), 1674-1686 (2015-05-13)
The biological underpinnings linking stress to Alzheimer's disease (AD) risk are poorly understood. We investigated how corticotrophin releasing factor (CRF), a critical stress response mediator, influences amyloid-β (Aβ) production. In cells, CRF treatment increases Aβ production and triggers CRF receptor
Maria Merezhko et al.
PloS one, 9(6), e98619-e98619 (2014-06-17)
Amyloid-β precursor protein (APP) plays a central role in pathogenesis of Alzheimer's disease. APP has a short half-life and undergoes complex proteolytic processing that is highly responsive to various stimuli such as changes in cellular lipid or energy homeostasis. Cellular
R E Tanzi et al.
Science (New York, N.Y.), 235(4791), 880-884 (1987-02-20)
The amyloid beta protein has been identified as an important component of both cerebrovascular amyloid and amyloid plaques of Alzheimer's disease and Down syndrome. A complementary DNA for the beta protein suggests that it derives from a larger protein expressed
Qi-Xin Wen et al.
Traffic (Copenhagen, Denmark), 24(1), 20-33 (2022-11-23)
AP2S1 is the sigma 2 subunit of adaptor protein 2 (AP2) that is essential for endocytosis. In this study, we investigated the potential role of AP2S1 in intracellular processing of amyloid precursor protein (APP), which contributes to the pathogenesis of
Margarita Brilkova et al.
Cell reports, 40(13), 111433-111433 (2022-09-29)
Age-related neurodegenerative diseases (NDDs) are associated with the aggregation and propagation of specific pathogenic protein species (e.g., Aβ, α-synuclein). However, whether disruption of synaptic homeostasis results from protein misfolding per se rather than accumulation of a specific rogue protein is
Hua Zhang et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 43(8), 1441-1454 (2023-01-11)
It is well established that ryanodine receptors (RyanRs) are overactive in Alzheimer's disease (AD), and it has been suggested that inhibition of RyanR is potentially beneficial for AD treatment. In the present study, we explored a potential connection between basal
Zhong-Can Chen et al.
Science signaling, 10(488) (2017-07-20)
Mutations in LRRK2, which encodes leucine-rich repeat kinase 2, are the most common genetic cause of familial and sporadic Parkinson's disease (PD), a degenerative disease of the central nervous system that causes impaired motor function and, in advanced stages, dementia.
Runa Hamid et al.
Journal of neurochemistry, 102(4), 1264-1275 (2007-09-01)
Consecutive cleavages of amyloid precursor protein (APP) generate APP intracellular domain (AICD). Its cellular function is still unclear. In this study, we investigated the functional role of AICD in cellular Ca(2+) homeostasis. We could confirm previous observations that endoplasmic reticulum
Sanghamitra Bandyopadhyay et al.
PloS one, 8(7), e65978-e65978 (2013-08-13)
We reported that iron influx drives the translational expression of the neuronal amyloid precursor protein (APP), which has a role in iron efflux. This is via a classic release of repressor interaction of APP mRNA with iron-regulatory protein-1 (IRP1) whereas
Jenna M Ramaker et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 33(24), 10165-10181 (2013-06-14)
Amyloid precursor protein (APP) belongs to a family of evolutionarily conserved transmembrane glycoproteins that has been proposed to regulate multiple aspects of cell motility in the nervous system. Although APP is best known as the source of β-amyloid fragments (Aβ)
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