Pen-2 Is Sequestered in the Endoplasmic Reticulum and Subjected to Ubiquitylation and Proteasome-mediated Degradation in the Absence of Presenilin-Reference-Cited by-同舟云学术

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Pen-2 Is Sequestered in the Endoplasmic Reticulum and Subjected to Ubiquitylation and Proteasome-mediated Degradation in the Absence of Presenilin

Published:2004-04 Issue:16 Volume:279 Page:16744-16753
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Bergman Anna,Hansson Emil M.,Pursglove Sharon E.,Farmery Mark R.,Lannfelt Lars,Lendahl Urban,Lundkvist Johan,Näslund Jan

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference32 articles.

1. Regulated Intramembrane Proteolysis

2. The Presenilins in Alzheimer's Disease--Proteolysis Holds the Key

3. Murine Notch Homologs (N1–4) Undergo Presenilin-dependent Proteolysis

4. Conservation of the biochemical mechanisms of signal transduction among mammalian Notch family members

5. Proteolytic release of CD44 intracellular domain and its role in the CD44 signaling pathway

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1. Pen2/ErbB4 signaling regulates stemness of pancreatic ductal carcinoma;Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease;2024-10

2. Functional and topological analysis of PSENEN, the fourth subunit of the γ-secretase complex;Journal of Biological Chemistry;2024-01

3. Functional and topological analysis of PSENEN, the fourth subunit of the γ-secretase complex;2023-07-28

4. The critical role of γ-secretase and its inhibitors in cancer and cancer therapeutics;International Journal of Biological Sciences;2023

5. The topology of pen-2, a γ-secretase subunit, revisited: evidence for a reentrant loop and a single pass transmembrane domain;Molecular Neurodegeneration;2015-08-22

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