Results 21 to 30 of about 40,728 (191)

Gamma-secretase composed of PS1/Pen2/Aph1a can cleave notch and amyloid precursor protein in the absence of nicastrin [PDF]

open access: yes, 2010
γ-secretase is a multiprotein intramembrane-cleaving protease with a growing list of protein substrates including the Notch receptors and the amyloid precursor protein.
Ilagan, Ma. Xenia G   +3 more
core   +2 more sources

Different types of γ-secretes complexes and their effect on substrate processing [PDF]

open access: yes, 2012
The γ-secretase complex is a transmembrane aspartyl protease that generates the Alzheimer disease (AD) related amyloid β-peptide (Aβ) from the amyloid precursor protein (APP). The γ- secretase complex cleaves APP at two different sites (γ- and ε-sites)
Pamrén, Annelie
core   +1 more source

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

Super-resolution microscopy reveals γ-secretase at both sides of the neuronal synapse [PDF]

open access: yes, 2016
The transmembrane protein assembly γ-secretase is a key protease in regulated intramembrane processing (RIP) of around 100 type-1 transmembrane proteins.
Bengt Winblad   +4 more
core   +1 more source

Caveolin‐1 inhibition mediates the opposing effects of alcohol on γ‐secretase activity in arterial endothelial and smooth muscle cells

open access: yesPhysiological Reports, 2023
Notch is important to vessel homeostasis. We investigated the mechanistic role of caveolin‐1 (Cav‐1) in mediating the effects of alcohol (Ethanol/EtOH) on the γ‐secretase proteolytic activity necessary for Notch signaling in vascular cells.
Naresh K. Rajendran   +3 more
doaj   +1 more source

The very many faces of presenilins and the γ-secretase complex [PDF]

open access: yes, 2013
Presenilin is a central, catalytic component of the γ-secretase complex which conducts intramembrane cleavage of various protein substrates. Although identified and mainly studied through its role in the development of amyloid plaques in Alzheimer ...
Michalina Smolarkiewicz   +2 more
core   +1 more source

Molecular mechanism of the intramembrane cleavage of the β-carboxyl terminal fragment of amyloid precursor protein by γ-secretase [PDF]

open access: yesFrontiers in Physiology, 2014
Amyloid β-protein (Aβ) plays a central role in the pathogenesis of Alzheimer's disease, the most common age-associated neurodegenerative disorder. Aβ is generated through intramembrane proteolysis of the β-carboxyl terminal fragment (βCTF) of β-amyloid precursor protein (APP) by γ-secretase.
openaire   +3 more sources

Proteomic Profiling of γ-Secretase Substrates and Mapping of Substrate Requirements [PDF]

open access: yes, 2011
The presenilin/γ-secretase complex, an unusual intramembrane aspartyl protease, plays an essential role in cellular signaling and membrane protein turnover.
Elias, Joshua E   +3 more
core   +1 more source

Determination of the Proteolytic Cleavage Sites of the Amyloid Precursor-Like Protein 2 by the Proteases ADAM10, BACE1 and γ-Secretase

open access: yesPLoS ONE, 2011
Regulated intramembrane proteolysis of the amyloid precursor protein (APP) by the protease activities α-, β- and γ-secretase controls the generation of the neurotoxic amyloid β peptide. APLP2, the amyloid precursor-like protein 2, is a homolog of APP, which shows functional overlap with APP, but lacks an amyloid β domain.
Hogl, Sebastian   +3 more
openaire   +5 more sources

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