Effect of valine on the efficiency and precision at S4 cleavage of the Notch-1 transmembrane domain
Author:
Publisher
Wiley
Subject
Cellular and Molecular Neuroscience
Reference20 articles.
1. Embryonic lethality in mice homozygous for a processing-deficient allele of Notch1
2. Nectin-1α, an Immunoglobulin-like Receptor Involved in the Formation of Synapses, Is a Substrate for Presenilin/γ-Secretase-like Cleavage
3. Presenilin-dependent Intramembrane Proteolysis of CD44 Leads to the Liberation of Its Intracellular Domain and the Secretion of an Aβ-like Peptide
4. Got RIP?
5. Presenilin-dependent γ-Secretase-like Intramembrane Cleavage of ErbB4
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1. Permissive Conformations of a Transmembrane Helix Allow Intramembrane Proteolysis by γ-Secretase;Journal of Molecular Biology;2023-09
2. Conformationally Flexible Sites within the Transmembrane Helices of Amyloid Precursor Protein and Notch1 Receptor;Biochemistry;2019-07-02
3. Proteolytic Cleavage of Notch: “HIT and RUN”;Current Molecular Medicine;2011-06-01
4. Pharmacological Analysis of Drosophila melanogaster γ-Secretase with Respect to Differential Proteolysis of Notch and APP;Molecular Pharmacology;2010-01-11
5. The insulin-like growth factor 1 (IGF-1) receptor is a substrate for γ-secretase-mediated intramembrane proteolysis;Biochemical and Biophysical Research Communications;2007-07
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