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Title
Structural Biology of Presenilins and Signal Peptide Peptidases
Authors
Keywords
-
Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 288, Issue 21, Pages 14673-14680
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2013-04-13
DOI
10.1074/jbc.r113.463281
References
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Note: Only part of the references are listed.- Effect of Helical Conformation and Side Chain Structure on γ-Secretase Inhibition by β-Peptide Foldamers: Insight into Substrate Recognition
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- The intramembrane protease SPPL2a promotes B cell development and controls endosomal traffic by cleavage of the invariant chain
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- Identification of a tetratricopeptide repeat-like domain in the nicastrin subunit of -secretase using synthetic antibodies
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- γ-Secretase Inhibitors and Modulators for the Treatment of Alzheimer's Disease: Disappointments and Hopes
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- Phenylpiperidine-type γ-secretase modulators target the transmembrane domain 1 of presenilin 1
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- Structure of γ-Secretase and Its Trimeric Pre-activation Intermediate by Single-particle Electron Microscopy
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- Neutralization of the γ-secretase activity by monoclonal antibody against extracellular domain of nicastrin
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- Inhibition of γ-Secretase Activity by Helical β-Peptide Foldamers
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- Signal peptide peptidases: A family of intramembrane-cleaving proteases that cleave type 2 transmembrane proteins
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- Cryoelectron Microscopy Structure of Purified γ-Secretase at 12 Å Resolution
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- The C-Terminal PAL Motif and Transmembrane Domain 9 of Presenilin 1 Are Involved in the Formation of the Catalytic Pore of the -Secretase
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