Results 31 to 40 of about 20,912 (233)

Functional γ-secretase complex assembly in Golgi/trans-Golgi network: interactions among presenilin, nicastrin, Aph1, Pen-2, and γ-secretase substrates

Neurobiology of Disease, 2003
γ-Secretase is a proteolytic complex whose substrates include Notch, β-amyloid precursor protein (APP), and several other type I transmembrane proteins. Presenilin (PS) and nicastrin are known components of this high-molecular-weight complex, and recent ...
Stephanie Baulac, Matthew J LaVoie, W.Taylor Kimberly, Jennifer Strahle, Michael S Wolfe, Dennis J Selkoe, Weiming Xia   +6 more
doaj   +1 more source

P2Y2 Nucleotide Receptors Enhance α-Secretase-dependent Amyloid Precursor Protein Processing [PDF]

Journal of Biological Chemistry, 2005
The amyloid precursor protein (APP) is proteolytically processed by beta- and gamma-secretases to release amyloid beta, the main component in senile plaques found in the brains of patients with Alzheimer disease. Alternatively, APP can be cleaved within the amyloid beta domain by alpha-secretase releasing the non-amyloidogenic product sAPP alpha, which
Jean M, Camden, Ann M, Schrader, Ryan E, Camden, Fernando A, González, Laurie, Erb, Cheikh I, Seye, Gary A, Weisman   +6 more
openaire   +2 more sources

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

Frontiers 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

Emerging structures and dynamic mechanisms of γ-secretase for Alzheimer’s disease

Neural Regeneration Research
γ-Secretase, called “the proteasome of the membrane,” is a membrane-embedded protease complex that cleaves 150+ peptide substrates with central roles in biology and medicine, including amyloid precursor protein and the Notch family of cell-surface ...
Yinglong Miao, Michael S. Wolfe
doaj   +1 more source

The resveratrol trimer miyabenol C inhibits β-secretase activity and β-amyloid generation.

PLoS ONE, 2015
Accumulation and deposition of amyloid-β peptide (Aβ) in the brain is a primary cause of the pathogenesis of Alzheimer's disease (AD). Aβ is generated from amyloid-β precursor protein (APP) through sequential cleavages first by β-secretase and then by γ ...
Jin Hu, Ting Lin, Yuehong Gao, Junyue Xu, Chao Jiang, Guanghui Wang, Guojun Bu, Huaxi Xu, Haifeng Chen, Yun-wu Zhang   +9 more
doaj   +1 more source

Presenilin 2 is the predominant γ-secretase in microglia and modulates cytokine release. [PDF]

PLoS ONE, 2010
Presenilin 1 (PS1) and Presenilin 2 (PS2) are the enzymatic component of the γ-secretase complex that cleaves amyloid precursor protein (APP) to release amyloid beta (Aβ) peptide.
Suman Jayadev, Amanda Case, Alison J Eastman, Huy Nguyen, Julia Pollak, Jesse C Wiley, Thomas Möller, Richard S Morrison, Gwenn A Garden   +8 more
doaj   +1 more source

β‐secretase‐cleaved amyloid precursor protein in Alzheimer brain: a morphologic study [PDF]

Journal of Cellular and Molecular Medicine, 2004
Abstractβ‐amyloid (Aβ) is the main constituent of senile plaques seen in Alzheimer's disease. Aβ is derived from the amyloid precursor protein (APP) via proteolytic cleavage by proteases β‐ and β‐secretase. In this study, we examined content and localization of β‐secretase‐cleaved APP (β‐sAPP) in brain tissue sections from the frontal, temporal and ...
Sennvik, Kristina, Bogdanovic, N, Volkmann, Inga, Fastbom, J, Benedikz, Eirikur   +4 more
openaire   +3 more sources

Regulation of amyloid precursor protein processing by serotonin signaling. [PDF]

PLoS ONE, 2014
Proteolytic processing of the amyloid precursor protein (APP) by the β- and γ-secretases releases the amyloid-β peptide (Aβ), which deposits in senile plaques and contributes to the etiology of Alzheimer's disease (AD). The α-secretase cleaves APP in the
Anna A Pimenova, Amantha Thathiah, Bart De Strooper, Ina Tesseur   +3 more
doaj   +1 more source

-Secretase-Regulated Signaling Mechanisms: Notch and Amyloid Precursor Protein [PDF]

, 2012
In Drosophila, Notch mutations lost a lateral signaling ability and produced a neurogenic phenotype, where cells destined to become epidermis switch fate and give rise to neural tissue (Artavanis-Tsakonas et al. 1995; Lewis 1998). Therefore, when Notch signaling was disrupted, too many neurons were generated.
Nakayama, Kohzo, Nagase, Hisashi, Koh, Chang-Sung, Ohkawara, Takeshi   +3 more
openaire   +2 more sources

Cellular prion protein regulates β-secretase cleavage of the Alzheimer's amyloid precursor protein [PDF]

Proceedings of the National Academy of Sciences, 2007
Proteolytic processing of the amyloid precursor protein (APP) by β-secretase, β-site APP cleaving enzyme (BACE1), is the initial step in the production of the amyloid β (Aβ) peptide, which is involved in the pathogenesis of Alzheimer's disease.
Parkin, Ed, Watt, Nicole T., Hussain, Ishrut, Eckman, Elizabeth A., Eckman, Christopher B., Manson, Jean C., Baybutt, Herbert N., Turner, Anthony J., Hooper, Nigel M.   +8 more
openaire   +3 more sources