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Rosana A Mesa et al.
F1000Research, 8, 1211-1211 (2020-05-16)
Nicastrin (NCSTN) is a transmembrane glycoprotein that is part of the gamma-secretase complex. Gamma-secretase is a protease complex that cleaves type-I single-pass transmembrane proteins. There are many potential substrates for this complex, including NOTCH receptors and amyloid precursor proteins (APP).
Sunmin Jung et al.
Journal of neurochemistry, 137(5), 770-781 (2016-03-01)
Amyloid beta peptide (Aβ) is a pathological hallmark of Alzheimer's disease (AD) and is generated through the sequential cleavage of amyloid precursor protein (APP) by β- and γ-secretases. Hypoxia is a known risk factor for AD and stimulates Aβ generation
Hanna Laudon et al.
Journal of neurochemistry, 89(1), 44-53 (2004-03-20)
The enzyme gamma-secretase catalyzes the intramembrane proteolytic cleavage that generates the amyloid beta-peptide from the beta-amyloid precursor protein. The presenilin (PS) protein is one of the four integral membrane protein components of the mature gamma-secretase complex. The PS protein is
Allen C Chen et al.
The Journal of cell biology, 211(6), 1157-1176 (2015-12-24)
Many single-transmembrane proteins are sequentially cleaved by ectodomain-shedding α-secretases and the γ-secretase complex, a process called regulated intramembrane proteolysis (RIP). These cleavages are thought to be spatially and temporally separate. In contrast, we provide evidence for a hitherto unrecognized multiprotease
Jing Lu et al.
PloS one, 12(3), e0173240-e0173240 (2017-03-03)
Although levodopa is the first-line medication for the treatment of Parkinson's disease (PD) showing unsurpassable efficiency, its chronic use causes dyskinesia. Accordingly, dopamine agonists are increasingly employed as monotherapy or in combination with levodopa to reduce the risk of motor
Jay H Chyung et al.
The Journal of biological chemistry, 280(6), 4383-4392 (2004-12-01)
Research on Alzheimer's disease led to the identification of a novel proteolytic mechanism in all metazoans, the presenilin/gamma-secretase complex. This unique intramembrane-cleaving aspartyl protease is required for the normal processing of Notch, Jagged, beta-amyloid precursor protein (APP), E-cadherin, and many
Keiro Shirotani et al.
Journal of neurochemistry, 89(6), 1520-1527 (2004-06-11)
Gamma-secretase is a high molecular mass aspartyl protease complex composed of presenilin (PS1 or PS2), nicastrin (Nct), anterior pharynx-defective-1 (APH-1) and presenilin enhancer-2 (PEN-2). The complex mediates the intramembraneous proteolysis of beta-secretase cleaved beta-amyloid precursor protein (APP) leading to the
Camilla A Hansson et al.
The Journal of biological chemistry, 279(49), 51654-51660 (2004-10-01)
Mitochondria are central in the regulation of cell death. Apart from providing the cell with ATP, mitochondria also harbor several death factors that are released upon apoptotic stimuli. Alterations in mitochondrial functions, increased oxidative stress, and neurons dying by apoptosis
Benedikt Kretner et al.
Journal of neurochemistry, 125(1), 144-156 (2012-12-15)
γ-Secretase plays a central role in the generation of the Alzheimer disease-causing amyloid β-peptide (Aβ) from the β-amyloid precursor protein (APP) and is thus a major Alzheimer's disease drug target. As several other γ-secretase substrates including Notch1 and CD44 have
Ji-Yeun Hur et al.
The FEBS journal, 275(6), 1174-1187 (2008-02-13)
Several lines of evidence suggest that polymerization of the amyloid beta-peptide (Abeta) into amyloid plaques is a pathogenic event in Alzheimer's disease (AD). Abeta is produced from the amyloid precursor protein as the result of sequential proteolytic cleavages by beta-secretase
Regina Fluhrer et al.
Biological chemistry, 392(11), 995-1001 (2011-08-19)
Nicastrin is a type I transmembrane glycoprotein, which is part of the high molecular weight γ-secretase complex. γ-Secretase is one of the key players associated with the generation of Alzheimer's disease pathology, since it liberates the neurotoxic amyloid β-peptide. Four
Matthias Voss et al.
The EMBO journal, 33(24), 2890-2905 (2014-10-31)
Protein N-glycosylation is involved in a variety of physiological and pathophysiological processes such as autoimmunity, tumour progression and metastasis. Signal peptide peptidase-like 3 (SPPL3) is an intramembrane-cleaving aspartyl protease of the GxGD type. Its physiological function, however, has remained enigmatic
Stefan Prokop et al.
The Journal of biological chemistry, 279(22), 23255-23261 (2004-03-25)
Gamma-secretase is a protease complex composed of presenilin (PS), nicastrin (NCT), APH-1, and PEN-2, which catalyzes intramembrane cleavage of several type I transmembrane proteins including the Alzheimer's disease-associated beta-amyloid precursor protein. We generated stable RNA interference-mediated PEN-2 knockdown cells to
Stefan Prokop et al.
Journal of neurochemistry, 94(1), 57-62 (2005-06-15)
Gamma-secretase is an aspartyl protease complex that catalyzes the intramembrane cleavage of a subset of type I transmembrane proteins including the beta-amyloid precursor protein (APP) implicated in Alzheimer's disease. Presenilin (PS), nicastrin (NCT), anterior pharynx defective (APH-1) and presenilin enhancer-2
Yasuhiro Teranishi et al.
The FEBS journal, 282(17), 3438-3451 (2015-06-23)
γ-Secretase is a transmembrane protease complex that is responsible for the processing of a multitude of type 1 transmembrane proteins, including the amyloid precursor protein and Notch. γ-Secretase processing of amyloid precursor protein results in the release of the amyloid
Kiwami Kidana et al.
EMBO molecular medicine, 10(3) (2018-01-10)
Deposition of amyloid-β (Aβ) as senile plaques is one of the pathological hallmarks in the brains of Alzheimer's disease (AD) patients. In addition, glial activation has been found in AD brains, although the precise pathological role of astrocytes remains unclear.
Jing Lu et al.
PloS one, 11(11), e0166415-e0166415 (2016-11-12)
γ-secretase mediates the intramembranous proteolysis of amyloid precursor protein (APP) and determines the generation of Aβ which is associated with Alzheimer's disease (AD). Here we identified that an anti-Parkinson's disease drug, Istradefylline, could enhance Aβ generation in various cell lines
Yung Wen Chiu et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 34(6), 7661-7674 (2020-04-21)
The aberrant metabolism of amyloid β peptide (Aβ) has been implicated in the etiology of Alzheimer disease (AD). Aβ is produced via the sequential cleavage of amyloid precursor protein (APP) by β- and γ-secretases. However, the precise regulatory mechanism of
Benedikt Kretner et al.
EMBO molecular medicine, 8(5), 458-465 (2016-03-19)
As stated by the prevailing amyloid cascade hypothesis, Alzheimer's disease (AD) is caused by the aggregation and cerebral deposition of long amyloid-β peptide (Aβ) species, which are released from a C-terminal amyloid precursor protein fragment by γ-secretase. Mutations in its
Mark R Farmery et al.
The Journal of biological chemistry, 278(27), 24277-24284 (2003-04-17)
One characteristic feature of Alzheimer's disease is the deposition of amyloid beta-peptide (Abeta) as amyloid plaques within specific regions of the human brain. Abeta is derived from the amyloid beta-peptide precursor protein (beta-APP) by the intramembranous cleavage activity of gamma-secretase.
Harald Steiner et al.
The Journal of biological chemistry, 283(50), 34677-34686 (2008-09-20)
Gamma-secretase is an intramembrane cleaving aspartyl protease complex intimately implicated in Alzheimer disease pathogenesis. The protease is composed of the catalytic subunit presenilin (PS1 or PS2), the substrate receptor nicastrin (NCT), and two additional subunits, APH-1 (APH-1a, as long and
A-Ryeong Gwon et al.
Aging cell, 11(4), 559-568 (2012-03-13)
The cause of elevated level of amyloid β-peptide (Aβ42) in common late-onset sporadic [Alzheimer's disease (AD)] has not been established. Here, we show that the membrane lipid peroxidation product 4-hydroxynonenal (HNE) is associated with amyloid and neurodegenerative pathologies in AD
Alexandre Matz et al.
Journal of neurochemistry, 133(3), 409-421 (2014-12-03)
An important pathological hallmark of Alzheimer's disease (AD) is the deposition of amyloid-beta (Aβ) peptides in the brain parenchyma, leading to neuronal death and impaired learning and memory. The protease γ-secretase is responsible for the intramembrane proteolysis of the amyloid-β
Oliver Holmes et al.
Journal of neurochemistry, 131(1), 94-100 (2014-05-29)
The 19-transmembrane, multisubunit γ-secretase complex generates the amyloid β-peptide (Aβ) of Alzheimer's disease (AD) by an unusual intramembrane proteolysis of the β-amyloid precursor protein. The complex, which similarly processes many other type 1 transmembrane substrates, is composed of presenilin, Aph1
Sarah A Laurent et al.
Nature communications, 6, 7333-7333 (2015-06-13)
Survival of plasma cells is regulated by B-cell maturation antigen (BCMA), a membrane-bound receptor activated by its agonist ligands BAFF and APRIL. Here we report that γ-secretase directly cleaves BCMA, without prior truncation by another protease. This direct shedding is
Chen Hu et al.
Journal of Alzheimer's disease : JAD, 56(4), 1263-1269 (2017-02-25)
Presenilin-1 (PS1) or presenilin-2 (PS2), nicastrin (NCT), anterior pharynx-defective 1 (Aph-1), and presenilin enhancer-2 (Pen-2) have been considered the minimal essential subunits required to form an active γ-secretase complex. Besides PS, which has been widely believed to function as the
Keiro Shirotani et al.
The Journal of biological chemistry, 278(19), 16474-16477 (2003-03-20)
Gamma-secretase is a high molecular weight multicomponent protein complex with an unusual intramembrane-cleaving aspartyl protease activity. Gamma-secretase is intimately associated with Alzheimer disease because it catalyzes the proteolytic cleavage, which leads to the liberation of amyloid beta-peptide. At least presenilin
Liana Marengo et al.
Cellular and molecular life sciences : CMLS, 79(3), 168-168 (2022-03-03)
β-Site amyloid precursor protein (APP) cleaving enzyme-1 (BACE1) is the major described β-secretase to generate Aβ peptides in Alzheimer's disease (AD). However, all therapeutic attempts to block BACE1 activity and to improve AD symptoms have so far failed. A potential
Masaki Nishimura et al.
Journal of neurochemistry, 123(1), 21-28 (2012-07-24)
Age-dependent accumulation of the amyloid-β peptide (Aβ) in the brain is a pre-condition for development of Alzheimer's disease. A relative increase in the generation of longer Aβ species such as Aβ42 and Aβ43 is critical for Aβ deposition, but the
Sang Hun Lee et al.
Proceedings of the National Academy of Sciences of the United States of America, 111(24), 8973-8978 (2014-06-04)
Synaptic dysfunction is widely thought to play a key role in the pathogenesis of Alzheimer's disease (AD). Presenilins, the major gene products involved in familial AD, are essential for short- and long-term synaptic plasticity in mature neurons as well as
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