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Modulation of the PSENEN trafficking pathway might be a potential target for the development of Abeta42-lowering Alzheimer disease therapeutics
No mutation that was likely to be pathogenic for acne inversa was found in PSEN1 or PSENEN in any participant.
The present study further expands the spectrum of PSENEN mutations associated with HS-DDD and suggests a role for Notch signalling in the pathogenesis of this intriguing combined disorder.
High gamma-secretase expression is associated with head and neck squamous cell carcinoma.
APP substrate occupancy of these three pockets of gamma-secretase occurs after initial substrate binding but precedes catalysis, suggesting a conformational change in substrate may be required for cleavage.
PSENEN mutations can indeed cause a comanifestation of Dowling-Degos disease and acne inversa (AI) that is likely triggered by predisposing factors for AI.
zinc, copper inhibited Abeta production by directly targeting the subunits presenilin and nicastrin in the gamma-secretase complex
PSENEN may play a crucial role in the progression of atopic dermatitis by participating in the Notch signaling pathway.
Remarkably, PEN-2 was identified besides nicastrin as additional substrate-binding subunit.
Results suggest deltaOR-Phe27Cys variation modulates beta- and gamma-secretase activity in late-stage Alzheimer's disease likely via post-translational mechanisms
TRPC6 specifically interacts with APP leading to inhibition of its cleavage by gamma-secretase and reduction in Abeta production.
secondary mutations in presenilin 1 alone activated the gamma-secretase activity.
Both human PS2V and zebrafish PS1IV can stimulate gamma-secretase activity despite extreme structural divergence
Data indicate that familial Alzheimer's disease (FAD) and control brain samples had similar overall gamma-secretase activity levels, and therefore, loss of overall (endopeptidase) gamma-secretase function cannot be an essential part of the pathogenic mechanism.
We for the first time identify PEN-2 as the causative gene of familial comedones.
The first hydrophobic domain of Pen-2 forms a structure similar to a reentrant loop while the second hydrophobic domain spans the lipid bilayer.
shedding of BCMA by gamma-secretase controls plasma cells in the bone marrow and yields a potential biomarker for B-cell involvement in human autoimmune diseases
Tumor necrosis factor-alpha and interleukin-10 levels were elevated in acne inversa patients with nicastrin or presenilin enhancer mutation.
SLC2A13 is a novel gamma-secretase associated protein that regulates amyloid beta production without affecting Notch cleavage.
Brain proteins showing neuron-specific interactions with gamma-secretase
The PSENEN gene is down-regulated in bovine intramuscular fibroblast cells during differentiation into adipocytes.
Using knockout cell lines in combination with siRNA and immunoprecipitation approaches, our data clearly demonstrated that the Pen-2 and PS1 are sufficient to form a functionally active gamma-secretase that is capable of catalyzing the processing of Notch. This finding strongly suggests that Pen-2 is the most crucial component in gamma-secretase complex in addition to presenilin that functions as the catalytic subunit.
Cleavage of the Interleukin-11 receptor induces processing of its C-terminal fragments by the gamma-secretase and the proteasome.
the G206D mutation reduced presenilin-1-presenilin enhancer 2 interaction, but did not abolish gamma-secretase formation and presenilin-1 endoproteolysis
Data show that the expression level of presenilin enhancer-2 (Pen-2) is relatively high in central nervous system at the early stages of postnatal development, but declines, gradually in adult mice.
rather than solely being a catalyst for gamma-secretase endoproteolysis, Pen-2 may also stabilize the complex prior to PS1 endoproteolysis, allowing time for full assembly and proper trafficking.
Pen-2, as well as nicastrin and Aph-1alpha, is dispensable for presenilin endoproteolysis
Nct has a critical role in the stability and proper intracellular trafficking of other components of the PS1/ gamma-secretase complex but not in maintaining the association of PEN-2, APH-1, and full-length PS1
APH-1 stabilizes the presenilin holoprotein in the complex, whereas PEN-2 is required for endoproteolytic processing of presenilin and conferring gamma-secretase activity to the complex.
presenilin, nicastrin, APH-1, and PEN-2, are present and enriched on phagosome membranes from both murine macrophages and Drosophila S2 phagocytes
Both human PS2V and zebrafish PS1IV can stimulate gamma-secretase activity despite extreme structural divergence.
Presenilins, which are components of the gamma-secretase protein complex, are required for intramembranous processing of some type I transmembrane proteins, such as the Notch proteins and the beta-amyloid precursor protein. Signaling by Notch receptors mediates a wide range of developmental cell fates. Processing of the beta-amyloid precursor protein generates neurotoxic amyloid beta peptides, the major component of senile plaques associated with Alzheimer's disease. This gene encodes a protein that is required for Notch pathway signaling, and for the activity and accumulation of gamma-secretase.
gamma-secretase subunit PEN-2
, hematopoietic stem/progenitor cells protein MDS033
, presenilin enhancer protein 2
, presenilin enhancer 2
, LRRGT00140 mRNA
, liver regeneration-related protein LRRGT00140
, presenilin enhancer 2 homolog
, presenilin enhancer gamma secretase subunit S homeolog
, Presenilin enhancer protein 2 homolog
, presenilin enhancer protein 2 homolog