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Prostaglandin I2 accumulation in neuronal cells activates PKA/CREB (zeige CREB1 ELISA Kits) and JNK/c-Jun signaling pathways by phosphorylation, which results in APH-1alpha/1beta expression.
Thus, Leda-1/Pianp is constitutively processed by proprotein convertases, sheddases including MMPs and ADAM10 (zeige ADAM10 ELISA Kits)/17 and intramembrane protease gamma-secretase.
Abeta (zeige APP ELISA Kits) oligomers in the cerebrospinal fluid (CSF (zeige CSF2 ELISA Kits)) further promoted the expression of APH-1alpha/-1beta (by >2.5-fold), which enhances the gamma-cleavage of APP (zeige APP ELISA Kits) and Abeta (zeige APP ELISA Kits) deposition during AD progression
Upregulation of PS1 (zeige PSEN1 ELISA Kits)/gamma-secretase activity may be a risk factor for late onset sporadic Alzheimer's disease.
ficiency of beta-arrestin1 (zeige ARRB1 ELISA Kits) or inhibition of binding of beta-arrestin1 (zeige ARRB1 ELISA Kits) with APH-1 by small peptides reduced Abeta (zeige APP ELISA Kits) production without affecting Notch (zeige NOTCH1 ELISA Kits) processing
Pen-2 (zeige PSENEN ELISA Kits), as well as nicastrin (zeige NCSTN ELISA Kits) and Aph-1alpha, is dispensable for presenilin endoproteolysis
We propose a model that identifies critical TMDs of Aph-1 for associations with Nct (zeige NCSTN ELISA Kits) and PS for the stepwise assembly of gamma-secretase components.
Aph-1 associates directly with full-length and C-terminal fragments of gamma-secretase substrates
presenilin 1 (PS1 (zeige PSEN1 ELISA Kits))-derived fragments, mature nicastrin (zeige NCSTN ELISA Kits), APH-1, and PEN-2 (zeige PSENEN ELISA Kits), associate with cholesterol-rich detergent insoluble membrane (DIM) domains of non-neuronal cells and neurons
Our findings establish that APH-1a is the major mammalian APH-1 homolog present in presenilin-dependent gamma-secretase complexes during embryogenesis.
Using purified PSEN1 (zeige PSEN1 ELISA Kits)/Aph1A gamma-secretase and the APPC99-3XFLAG substrate, authors show that substrate shortening progressively destabilizes the consecutive enzyme-substrate complexes that characterize the sequential gamma-secretase processing of APP (zeige APP ELISA Kits); present a unifying model for how PSEN (zeige PSEN1 ELISA Kits) or APP (zeige APP ELISA Kits) mutations enhance amyloidogenic Abeta (zeige APP ELISA Kits) production, suggests that environmental factors may increase Alzheimer's Disease risk.
Data show that presenilin 1 (PS1 (zeige PSEN1 ELISA Kits))/anterior-pharynx-defective protein 1 (Aph1b (zeige aph1b ELISA Kits)), presenilin 2 (PS2 (zeige PSEN2 ELISA Kits))/Aph1aL, PS2 (zeige PSEN2 ELISA Kits)/Aph1aS and PS2 (zeige PSEN2 ELISA Kits)/anterior pharynx defective 1 homolog B (Aph1b (zeige aph1b ELISA Kits)) gamma-secretase produced amyloid beta peptide (Abeta (zeige APP ELISA Kits)) with a higher Abeta42+Abeta43-to-Abeta40 (Abeta42(43)/Abeta40) ratio than the other gamma-secretases.
Data show that presenilin 1 (PS1 (zeige PSEN1 ELISA Kits))-containing gamma-secretase complexes were targeted to the plasma membrane, whereas presenilin 2 (PS2 (zeige PSEN2 ELISA Kits))-containing ones were addressed to the trans-Golgi network, to recycling endosomes.
No statistically significant difference was detected either in APOE (zeige APOE ELISA Kits) or APH-1a polymorphisms, not suggesting a strong susceptibility to the development of Alzheimer disease.
analysis of how the conformation of presenilin, Pen-2 (zeige PSENEN ELISA Kits), Aph-1, and nicastrin (zeige NCSTN ELISA Kits) affect the function and mechanism of gamma-secretase
We demonstrate that extending the transmembrane domain of the amyloid precursor protein (zeige APP ELISA Kits)-derived C99 substrate in proximity to the cytosolic face strongly influences gamma-secretase cleavage specificity.
The -980C/G polymorphism in APH-1A promoter confers risk of Alzheimer's disease
Coexpression of wild-type or S-palmitoylation-deficient APH1aL and nicastrin (zeige NCSTN ELISA Kits) leads to marked stabilization of transgenic presenilin 1 (zeige PSEN1 ELISA Kits) in the brains of double-transgenic mice.
Endogenous Aph-1a and its proteolytic fragment have unique properties for cleavage control that may have implications for gamma-secretase regulation and intracellular distribution.
Co-overexpression of presenilin-1 or APH-1 abrogated gamma-secretase inhibition probably through prevention of the incorporation of CRB2 into the gamma-secretase complex
This gene encodes a component of the gamma secretase complex that cleaves integral membrane proteins such as Notch receptors and beta-amyloid precursor protein. The gamma secretase complex contains this gene product, or the paralogous anterior pharynx defective 1 homolog B (APH1B), along with the presenilin, nicastrin, and presenilin enhancer-2 proteins. The precise function of this seven-transmembrane-domain protein is unknown though it is suspected of facilitating the association of nicastrin and presenilin in the gamma secretase complex as well as interacting with substrates of the gamma secretase complex prior to their proteolytic processing. Polymorphisms in a promoter region of this gene have been associated with an increased risk for developing sporadic Alzheimer's disease. Alternative splicing results in multiple protein-coding and non-protein-coding transcript variants.
gamma-secretase subunit APH-1A
, anterior pharynx defective 1 homolog A
, anterior pharynx defective 1 homolog A (C. elegans)
, N-acylaminoacyl-peptide hydrolase
, acylamino-acid-releasing enzyme-like
, presenilin-stabilization factor
, anterior pharynx defective 1a homolog