The amyloid-beta forming tripeptide cleavage mechanism of γ-secretase
Published 2016 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
The amyloid-beta forming tripeptide cleavage mechanism of γ-secretase
Authors
Keywords
-
Journal
eLife
Volume 5, Issue -, Pages -
Publisher
eLife Sciences Organisation, Ltd.
Online
2016-09-01
DOI
10.7554/elife.17578
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- The Many Substrates of Presenilin/γ-Secretase
- (2018) Annakaisa Haapasalo et al. JOURNAL OF ALZHEIMERS DISEASE
- Crystal Structures and Inhibition Kinetics Reveal a Two-Stage Catalytic Mechanism with Drug Design Implications for Rhomboid Proteolysis
- (2016) Sangwoo Cho et al. MOLECULAR CELL
- Nicastrin functions to sterically hinder γ-secretase–substrate interactions driven by substrate transmembrane domain
- (2015) David M. Bolduc et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Roles of the membrane-reentrant β-hairpin-like loop of RseP protease in selective substrate cleavage
- (2015) Koichiro Akiyama et al. eLife
- Lessons from a Failed γ-Secretase Alzheimer Trial
- (2014) Bart De Strooper CELL
- Alzheimer Presenilin-1 Mutations Dramatically Reduce Trimming of Long Amyloid β-Peptides (Aβ) by γ-Secretase to Increase 42-to-40-Residue Aβ
- (2014) Marty A. Fernandez et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Familial Alzheimer’s mutations within APPTM increase Aβ42 production by enhancing accessibility of ε-cleavage site
- (2014) Wen Chen et al. Nature Communications
- γ-Secretase inhibitors and modulators
- (2013) Todd E. Golde et al. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
- Proteolysis inside the Membrane Is a Rate-Governed Reaction Not Driven by Substrate Affinity
- (2013) Seth W. Dickey et al. CELL
- γ-Secretase Associated with Lipid Rafts
- (2013) Nobutaka Matsumura et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Characterization of Intermediate Steps in Amyloid Beta (Aβ) Production under Near-native Conditions
- (2013) Fredrik Olsson et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- A Phase 3 Trial of Semagacestat for Treatment of Alzheimer's Disease
- (2013) Rachelle S. Doody et al. NEW ENGLAND JOURNAL OF MEDICINE
- Alzheimer’s disease mutations in APP but not γ-secretase modulators affect epsilon-cleavage-dependent AICD production
- (2013) Mitko Dimitrov et al. Nature Communications
- γ-Secretase Modulators and Presenilin 1 Mutants Act Differently on Presenilin/γ-Secretase Function to Cleave Aβ42 and Aβ43
- (2013) Masayasu Okochi et al. Cell Reports
- The mechanism of γ-Secretase dysfunction in familial Alzheimer disease
- (2012) Lucía Chávez-Gutiérrez et al. EMBO JOURNAL
- Membrane immersion allows rhomboid proteases to achieve specificity by reading transmembrane segment dynamics
- (2012) Syed M Moin et al. eLife
- Dissociation between the Processivity and Total Activity of γ-Secretase: Implications for the Mechanism of Alzheimer's Disease-Causing Presenilin Mutations
- (2011) Omar Quintero-Monzon et al. BIOCHEMISTRY
- The α-Helical Content of the Transmembrane Domain of the British Dementia Protein-2 (Bri2) Determines Its Processing by Signal Peptide Peptidase-like 2b (SPPL2b)
- (2011) Regina Fluhrer et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- -Secretase: Successive Tripeptide and Tetrapeptide Release from the Transmembrane Domain of -Carboxyl Terminal Fragment
- (2009) M. Takami et al. JOURNAL OF NEUROSCIENCE
- Cryoelectron Microscopy Structure of Purified γ-Secretase at 12 Å Resolution
- (2008) Pamela Osenkowski et al. JOURNAL OF MOLECULAR BIOLOGY
- Genetic screening of Alzheimer's disease genes in Iberian and African samples yields novel mutations in presenilins and APP
- (2008) Rita Joao Guerreiro et al. NEUROBIOLOGY OF AGING
Create your own webinar
Interested in hosting your own webinar? Check the schedule and propose your idea to the Peeref Content Team.
Create NowBecome a Peeref-certified reviewer
The Peeref Institute provides free reviewer training that teaches the core competencies of the academic peer review process.
Get Started