Nuclear translocation and signalling of L1-CAM in human carcinoma cells requires ADAM10 and presenilin/gamma-secretase activity

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Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: Online-Ressource

Language: Englisch

Bibliographic citation: In: Biochemical Journal, 420.2009, S. 391–402 ; doi:10.1042/BJ20081625

Keyword: Krebs
Onkologie

Event: Veröffentlichung

(where): Frankfurt am Main

(who): Universitätsbibliothek Johann Christian Senckenberg

(when): 2009

Creator: Riedle, Svenja
Kiefel, Helena
Gast, Daniela
Bondong, Sandra
Wolterink, Silke
Gutwein, Paul
Altevogt, Peter

URN: urn:nbn:de:hebis:30-71056

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 15.08.2025, 7:28 AM CEST

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Associated

Riedle, Svenja
Kiefel, Helena
Gast, Daniela
Bondong, Sandra
Wolterink, Silke
Gutwein, Paul
Altevogt, Peter
Universitätsbibliothek Johann Christian Senckenberg

Time of origin

2009

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Identification of a beta-secretase activity, which truncates amyloid beta-peptide after its presenilin-dependent generation

Three-amino acid spacing of presenilin endoproteolysis suggests a general stepwise cleavage of gamma-secretase-mediated intramembrane proteolysis

Presenilin 1 deficiency suppresses autophagy in human neural stem cells through reducing γ-secretase-independent ERK/CREB signaling

Neuroprotection by ADAM10 inhibition requires TrkB signaling in the Huntington’s disease hippocampus

Changes in γ-secretase activity and specificity caused by the introduction of consensus aspartyl protease active motif in Presenilin 1

Periplasmic chitooligosaccharide-binding protein requires a three-domain organization for substrate translocation

Differential gene expression in ADAM10 and mutant ADAM10 transgenic mice

Inhibition of γ-Secretase Leads to an Increase in Presenilin-1

α-Secretase nonsense mutation (ADAM10 Tyr167*) in familial Alzheimer’s disease

The metalloproteinase ADAM10 requires its activity to sustain surface expression

The presenilin C-terminus is required for ER-retention, nicastrin-binding and gamma-secretase activity

Identification of a beta-secretase activity, which truncates amyloid beta-peptide after its presenilin-dependent generation

Three-amino acid spacing of presenilin endoproteolysis suggests a general stepwise cleavage of gamma-secretase-mediated intramembrane proteolysis

Presenilin 1 deficiency suppresses autophagy in human neural stem cells through reducing γ-secretase-independent ERK/CREB signaling

Neuroprotection by ADAM10 inhibition requires TrkB signaling in the Huntington’s disease hippocampus

Changes in γ-secretase activity and specificity caused by the introduction of consensus aspartyl protease active motif in Presenilin 1

Periplasmic chitooligosaccharide-binding protein requires a three-domain organization for substrate translocation

Differential gene expression in ADAM10 and mutant ADAM10 transgenic mice

Inhibition of γ-Secretase Leads to an Increase in Presenilin-1

α-Secretase nonsense mutation (ADAM10 Tyr167*) in familial Alzheimer’s disease

The metalloproteinase ADAM10 requires its activity to sustain surface expression

The presenilin C-terminus is required for ER-retention, nicastrin-binding and gamma-secretase activity

Identification of a beta-secretase activity, which truncates amyloid beta-peptide after its presenilin-dependent generation

Three-amino acid spacing of presenilin endoproteolysis suggests a general stepwise cleavage of gamma-secretase-mediated intramembrane proteolysis

Presenilin 1 deficiency suppresses autophagy in human neural stem cells through reducing γ-secretase-independent ERK/CREB signaling

Neuroprotection by ADAM10 inhibition requires TrkB signaling in the Huntington’s disease hippocampus

Changes in γ-secretase activity and specificity caused by the introduction of consensus aspartyl protease active motif in Presenilin 1

Periplasmic chitooligosaccharide-binding protein requires a three-domain organization for substrate translocation

Differential gene expression in ADAM10 and mutant ADAM10 transgenic mice

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Nuclear translocation and signalling of L1-CAM in human carcinoma cells requires ADAM10 and presenilin/gamma-secretase activity

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Other Objects (12)

Inhibition of γ-Secretase Leads to an Increase in Presenilin-1

α-Secretase nonsense mutation (ADAM10 Tyr167*) in familial Alzheimer’s disease

The metalloproteinase ADAM10 requires its activity to sustain surface expression

The metalloproteinase ADAM10 requires its activity to sustain surface expression

The presenilin C-terminus is required for ER-retention, nicastrin-binding and gamma-secretase activity

Identification of a beta-secretase activity, which truncates amyloid beta-peptide after its presenilin-dependent generation

Three-amino acid spacing of presenilin endoproteolysis suggests a general stepwise cleavage of gamma-secretase-mediated intramembrane proteolysis

Presenilin 1 deficiency suppresses autophagy in human neural stem cells through reducing γ-secretase-independent ERK/CREB signaling

Neuroprotection by ADAM10 inhibition requires TrkB signaling in the Huntington’s disease hippocampus

Changes in γ-secretase activity and specificity caused by the introduction of consensus aspartyl protease active motif in Presenilin 1

Periplasmic chitooligosaccharide-binding protein requires a three-domain organization for substrate translocation

Differential gene expression in ADAM10 and mutant ADAM10 transgenic mice

Inhibition of γ-Secretase Leads to an Increase in Presenilin-1

α-Secretase nonsense mutation (ADAM10 Tyr167*) in familial Alzheimer’s disease

The metalloproteinase ADAM10 requires its activity to sustain surface expression

The metalloproteinase ADAM10 requires its activity to sustain surface expression

The presenilin C-terminus is required for ER-retention, nicastrin-binding and gamma-secretase activity

Identification of a beta-secretase activity, which truncates amyloid beta-peptide after its presenilin-dependent generation

Three-amino acid spacing of presenilin endoproteolysis suggests a general stepwise cleavage of gamma-secretase-mediated intramembrane proteolysis

Presenilin 1 deficiency suppresses autophagy in human neural stem cells through reducing γ-secretase-independent ERK/CREB signaling

Neuroprotection by ADAM10 inhibition requires TrkB signaling in the Huntington’s disease hippocampus

Changes in γ-secretase activity and specificity caused by the introduction of consensus aspartyl protease active motif in Presenilin 1

Periplasmic chitooligosaccharide-binding protein requires a three-domain organization for substrate translocation

Differential gene expression in ADAM10 and mutant ADAM10 transgenic mice

Inhibition of γ-Secretase Leads to an Increase in Presenilin-1

α-Secretase nonsense mutation (ADAM10 Tyr167*) in familial Alzheimer’s disease

The metalloproteinase ADAM10 requires its activity to sustain surface expression

The metalloproteinase ADAM10 requires its activity to sustain surface expression

The presenilin C-terminus is required for ER-retention, nicastrin-binding and gamma-secretase activity

Identification of a beta-secretase activity, which truncates amyloid beta-peptide after its presenilin-dependent generation

Three-amino acid spacing of presenilin endoproteolysis suggests a general stepwise cleavage of gamma-secretase-mediated intramembrane proteolysis

Presenilin 1 deficiency suppresses autophagy in human neural stem cells through reducing γ-secretase-independent ERK/CREB signaling

Neuroprotection by ADAM10 inhibition requires TrkB signaling in the Huntington’s disease hippocampus

Changes in γ-secretase activity and specificity caused by the introduction of consensus aspartyl protease active motif in Presenilin 1

Periplasmic chitooligosaccharide-binding protein requires a three-domain organization for substrate translocation

Differential gene expression in ADAM10 and mutant ADAM10 transgenic mice

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