Cargando…

Independent Relationship between Amyloid Precursor Protein (APP) Dimerization and γ-Secretase Processivity

Altered production of β-amyloid (Aβ) from the amyloid precursor protein (APP) is closely associated with Alzheimer’s disease (AD). APP has a number of homo- and hetero-dimerizing domains, and studies have suggested that dimerization of β-secretase derived APP carboxyl terminal fragment (CTFβ, C99) i...

Descripción completa

Detalles Bibliográficos
Autores principales:	Jung, Joo In, Premraj, Sasha, Cruz, Pedro E., Ladd, Thomas B., Kwak, Yewon, Koo, Edward H., Felsenstein, Kevin M., Golde, Todd E., Ran, Yong
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Public Library of Science 2014
Materias:	Research Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4211736/ https://www.ncbi.nlm.nih.gov/pubmed/25350374 http://dx.doi.org/10.1371/journal.pone.0111553

Ejemplares similares

γ-Secretase Modulators and APH1 Isoforms Modulate γ-Secretase Cleavage but Not Position of ε-Cleavage of the Amyloid Precursor Protein (APP)
por: Lessard, Christian B., et al.
Publicado: (2015)

Complex Relationships between Substrate Sequence and Sensitivity to Alterations in γ-Secretase Processivity Induced by γ-Secretase Modulators
por: Jung, Joo In, et al.
Publicado: (2014)

γ-Secretase modulators exhibit selectivity for modulation of APP cleavage but inverse γ-secretase modulators do not
por: Lessard, Christian B., et al.
Publicado: (2020)

Differential Inhibition of Signal Peptide Peptidase Family Members by Established γ-Secretase Inhibitors
por: Ran, Yong, et al.
Publicado: (2015)

Cholestenoic acid, an endogenous cholesterol metabolite, is a potent γ-secretase modulator
por: Jung, Joo In, et al.
Publicado: (2015)

Dimerization of the transmembrane domain of amyloid precursor protein is determined by residues around the γ-secretase cleavage sites
por: Yan, Yan, et al.
Publicado: (2017)

γ‐Secretase modulators show selectivity for γ‐secretase–mediated amyloid precursor protein intramembrane processing
por: Weber, Tobias A., et al.
Publicado: (2021)

γ‐Secretase inhibitors in cancer clinical trials are pharmacologically and functionally distinct
por: Ran, Yong, et al.
Publicado: (2017)

Modulation of Aβ42 in vivo by γ-secretase modulator in primates and humans
por: Ling, I-Fang, et al.
Publicado: (2015)

A thermodynamic investigation of amyloid precursor protein processing by human γ-secretase
por: Lu, Xiaoli, et al.
Publicado: (2022)

The discrepancy between presenilin subcellular localization and γ-secretase processing of amyloid precursor protein
por: Cupers, Philippe, et al.
Publicado: (2001)

Sortilin, SorCS1b, and SorLA Vps10p sorting receptors, are novel γ-secretase substrates
por: Nyborg, Andrew C, et al.
Publicado: (2006)

Secretases Related to Amyloid Precursor Protein Processing
por: Liu, Xiaoling, et al.
Publicado: (2021)

Familial Alzheimer’s disease mutations in amyloid protein precursor alter proteolysis by γ-secretase to increase amyloid β-peptides of ≥45 residues
por: Devkota, Sujan, et al.
Publicado: (2021)

Modulation of amyloid precursor protein cleavage by γ-secretase activating protein through phase separation
por: Jin, Chen, et al.
Publicado: (2022)

α-Synuclein increases β-amyloid secretion by promoting β-/γ-secretase processing of APP
por: Roberts, Hazel L., et al.
Publicado: (2017)

Molecular mechanism of the intramembrane cleavage of the β-carboxyl terminal fragment of amyloid precursor protein by γ-secretase
por: Morishima-Kawashima, Maho
Publicado: (2014)

Verteporfin is a substrate-selective γ-secretase inhibitor that binds the amyloid precursor protein transmembrane domain
por: Castro, Manuel A., et al.
Publicado: (2022)

Dimeric Transmembrane Orientations of APP/C99 Regulate γ-Secretase Processing Line Impacting Signaling and Oligomerization
por: Perrin, Florian, et al.
Publicado: (2021)

Dimeric Transmembrane Orientations of APP/C99 Regulate γ-Secretase Processing Line Impacting Signaling and Oligomerization
por: Perrin, Florian, et al.
Publicado: (2020)

Specific Mutations near the Amyloid Precursor Protein Cleavage Site Increase γ-Secretase Sensitivity and Modulate Amyloid-β Production
por: Suzuki, Ryota, et al.
Publicado: (2023)

Effect of Metal Chelators on γ-Secretase Indicates That Calcium and Magnesium Ions Facilitate Cleavage of Alzheimer Amyloid Precursor Substrate
por: Ho, Michael, et al.
Publicado: (2010)

Presenilin 1 Controls γ-Secretase Processing of Amyloid Precursor Protein in Pre-Golgi Compartments of Hippocampal Neurons
por: Annaert, Wim G., et al.
Publicado: (1999)

Perturbations of the Straight Transmembrane α-Helical Structure of the Amyloid Precursor Protein Affect Its Processing by γ-Secretase
por: Lemmin, Thomas, et al.
Publicado: (2014)

Brain Ischemia Activates β- and γ-Secretase Cleavage of Amyloid Precursor Protein: Significance in Sporadic Alzheimer’s Disease
por: Pluta, Ryszard, et al.
Publicado: (2012)

Effects of presenilin-1 familial Alzheimer’s disease mutations on γ-secretase activation for cleavage of amyloid precursor protein
por: Do, Hung N., et al.
Publicado: (2023)

γ-Secretase-Dependent Proteolysis of Transmembrane Domain of Amyloid Precursor Protein: Successive Tri- and Tetrapeptide Release in Amyloid β-Protein Production
por: Takami, Mako, et al.
Publicado: (2012)

Substrate interaction inhibits γ-secretase production of amyloid-β peptides
por: Zhao, Jing, et al.
Publicado: (2020)

Substrate docking to γ-secretase allows access of γ-secretase modulators to an allosteric site
por: Uemura, Kengo, et al.
Publicado: (2010)

Enzyme–substrate interface targeting by imidazole‐based γ‐secretase modulators activates γ‐secretase and stabilizes its interaction with APP
por: Petit, Dieter, et al.
Publicado: (2022)

ApoER2 expression increases Aβ production while decreasing Amyloid Precursor Protein (APP) endocytosis: Possible role in the partitioning of APP into lipid rafts and in the regulation of γ-secretase activity
por: Fuentealba, Rodrigo A, et al.
Publicado: (2007)

The amyloid-beta forming tripeptide cleavage mechanism of γ-secretase
por: Bolduc, David M, et al.
Publicado: (2016)

Results of Beta Secretase-Inhibitor Clinical Trials Support Amyloid Precursor Protein-Independent Generation of Beta Amyloid in Sporadic Alzheimer’s Disease
por: Volloch, Vladimir, et al.
Publicado: (2018)

Delta-secretase cleaves amyloid precursor protein and regulates the pathogenesis in Alzheimer's disease
por: Zhang, Zhentao, et al.
Publicado: (2015)

A γ-Secretase Inhibitor, but Not a γ-Secretase Modulator, Induced Defects in BDNF Axonal Trafficking and Signaling: Evidence for a Role for APP
por: Weissmiller, April M., et al.
Publicado: (2015)

APP substrate ectodomain defines amyloid‐β peptide length by restraining γ‐secretase processivity and facilitating product release
por: Koch, Matthias, et al.
Publicado: (2023)

Interplay between α-, β-, and γ-Secretases Determines Biphasic Amyloid-β Protein Level in the Presence of a γ-Secretase Inhibitor
por: Ortega, Fernando, et al.
Publicado: (2013)

Determination of the Proteolytic Cleavage Sites of the Amyloid Precursor-Like Protein 2 by the Proteases ADAM10, BACE1 and γ-Secretase
por: Hogl, Sebastian, et al.
Publicado: (2011)

Modulation of γ-secretase by EVP-0015962 reduces amyloid deposition and behavioral deficits in Tg2576 mice
por: Rogers, Kathryn, et al.
Publicado: (2012)

Amyloid precursor protein selective gamma-secretase inhibitors for treatment of Alzheimer's disease
por: Basi, Guriqbal S, et al.
Publicado: (2010)

Cannot write session to /tmp/vufind_sessions/sess_4q48av4gbcvtor4pegd2i5edg0