Results 31 to 40 of about 86,542 (275)

Evaluation of Virtual Screening Strategies for the Identification of γ-Secretase Inhibitors and Modulators

open access: yesMolecules, 2021
γ-Secretase is an intramembrane aspartyl protease that is important in regulating normal cell physiology via cleavage of over 100 transmembrane proteins, including Amyloid Precursor Protein (APP) and Notch family receptors.
Alicia Ioppolo   +4 more
doaj   +1 more source

The role and therapeutic targeting of α-, β- and γ-secretase in Alzheimer's disease [PDF]

open access: yes, 2015
Alzheimer's disease (AD) is the most common form of dementia in the elderly and its prevalence is set to increase rapidly in coming decades. However, there are as yet no available drugs that can halt or even stabilize disease progression. One of the main
Baillie, George S.   +3 more
core   +1 more source

Specific Inhibition of β-Secretase Processing of the Alzheimer Disease Amyloid Precursor Protein

open access: yesCell Reports, 2016
Development of disease-modifying therapeutics is urgently needed for treating Alzheimer disease (AD). AD is characterized by toxic β-amyloid (Aβ) peptides produced by β- and γ-secretase-mediated cleavage of the amyloid precursor protein (APP).
Saoussen Ben Halima   +10 more
doaj   +1 more source

Human Papillomavirus L2 Capsid Protein Stabilizes γ-Secretase during Viral Infection

open access: yesViruses, 2022
Intracellular trafficking of human papillomavirus (HPV) during virus entry requires γ-secretase, a cellular protease consisting of a complex of four cellular transmembrane (TM) proteins. γ-secretase typically cleaves substrate proteins but it plays a non-
Mac Crite, Daniel DiMaio
doaj   +1 more source

Super-resolution microscopy reveals majorly mono- and dimeric presenilin1/γ-secretase at the cell surface

open access: yeseLife, 2020
γ-Secretase is a multi-subunit enzyme whose aberrant activity is associated with Alzheimer’s disease and cancer. While its structure is atomically resolved, γ-secretase localization in the membrane in situ relies mostly on biochemical data.
Abril Angélica Escamilla-Ayala   +12 more
doaj   +1 more source

The evolved divergence of γ-secretase-susceptibility of homologous proteins Ngfrb and Nradd in zebrafish

open access: yesBMC Research Notes, 2021
Objective NGFR/p75NTR and NRADD/NRH proteins are closely related structurally and are encoded by genes that arose from a duplication event early in vertebrate evolution.
Tanya Jayne   +3 more
doaj   +1 more source

A γ-secretase inhibitor, but not a γ-secretase modulator, induced defects in BDNF axonal trafficking and signaling: evidence for a role for APP. [PDF]

open access: yes, 2015
Clues to Alzheimer disease (AD) pathogenesis come from a variety of different sources including studies of clinical and neuropathological features, biomarkers, genomics and animal and cellular models. An important role for amyloid precursor protein (APP)
Cheng, Soan   +11 more
core   +2 more sources

Visualization of Alzheimer’s Disease Related α-/β-/γ-Secretase Ternary Complex by Bimolecular Fluorescence Complementation Based Fluorescence Resonance Energy Transfer

open access: yesFrontiers in Molecular Neuroscience, 2018
The competitive ectodomain shedding of amyloid-β precursor protein (APP) by α-secretase and β-secretase, and the subsequent regulated intramembrane proteolysis by γ-secretase are the key processes in amyloid-β peptides (Aβ) generation.
Xin Wang, Gang Pei, Gang Pei
doaj   +1 more source

Targeting Amyloidogenic Processing of APP in Alzheimer’s Disease

open access: yesFrontiers in Molecular Neuroscience, 2020
Alzheimer’s disease (AD) is the most common type of senile dementia, characterized by neurofibrillary tangle and amyloid plaque in brain pathology. Major efforts in AD drug were devoted to the interference with the production and accumulation of amyloid ...
Jing Zhao   +7 more
doaj   +1 more source

Signal peptide peptidases and gamma-secretase: Cousins of the same protease family? [PDF]

open access: yes, 2007
Signal peptide peptidase (SPIP) is an unusual aspartyl protease, which mediates clearance of signal peptides by proteolysis within the endoplasmic reticulum (ER).
Christian Haass   +15 more
core   +2 more sources

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