Modulating Hinge Flexibility in the APP Transmembrane Domain Alters γ-Secretase Cleavage-Reference-Cited by-同舟云学术

Modulating Hinge Flexibility in the APP Transmembrane Domain Alters γ-Secretase Cleavage

Published:2019-06 Issue:11 Volume:116 Page:2103-2120
ISSN:0006-3495
Container-title:Biophysical Journal
language:en
Short-container-title:Biophysical Journal

Author:

Götz Alexander,Mylonas Nadine,Högel Philipp,Silber Mara,Heinel Hannes,Menig Simon,Vogel Alexander,Feyrer Hannes,Huster Daniel,Luy Burkhard,Langosch Dieter,Scharnagl Christina,Muhle-Goll Claudia,Kamp Frits,Steiner Harald

Funder

Deutsche Forschungsgemeinschaft

VERUM Foundation

Gauss Centre for Supercomputing

Leibniz Supercomputing Center

Publisher

Elsevier BV

Subject

Biophysics

Reference112 articles.

1. Intramembrane-cleaving proteases;Wolfe;J. Biol. Chem,2009

2. Structural biology of intramembrane proteases: mechanistic insights from rhomboid and S2P to γ-secretase;Sun;Curr. Opin. Struct. Biol,2016

3. Update 1 of: proteases universally recognize β strands in their active sites;Madala;Chem. Rev,2010

4. Structural and kinetic determinants of protease substrates;Timmer;Nat. Struct. Mol. Biol,2009

5. Sequence-derived structural features driving proteolytic processing;Belushkin;Proteomics,2014

Cited by 35 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Substrate Selection Criteria in Regulated Intramembrane Proteolysis;ACS Chemical Neuroscience;2024-03-25

2. Emerging structures and dynamic mechanisms of γ-secretase for Alzheimer’s disease;Neural Regeneration Research;2024-03-01

3. C-terminal amino acids in the type I transmembrane domain of L-type lectin VIP36 affect γ-secretase susceptibility;Biochemical and Biophysical Research Communications;2024-02

4. Cleavage efficiency of the intramembrane protease γ‐secretase is reduced by the palmitoylation of a substrate's transmembrane domain;The FASEB Journal;2024-01-26

5. Structure and function of SPP/SPPL proteases: insights from biochemical evidence and predictive modeling;The FEBS Journal;2023-10-13