Results 31 to 40 of about 36,206 (272)

Ablation of Prion Protein in Wild Type Human Amyloid Precursor Protein (APP) Transgenic Mice Does Not Alter The Proteolysis of APP, Levels of Amyloid-β or Pathologic Phenotype.

PLoS ONE, 2016
The cellular prion protein (PrPC) has been proposed to play an important role in the pathogenesis of Alzheimer's disease. In cellular models PrPC inhibited the action of the β-secretase BACE1 on wild type amyloid precursor protein resulting in a ...
Isobel J Whitehouse, Deborah Brown, Herbert Baybutt, Abigail B Diack, Katherine A B Kellett, Pedro Piccardo, Jean C Manson, Nigel M Hooper   +7 more
doaj   +1 more source

The role of the Amyloid Precursor Protein mutations and PERK-dependent signaling pathways in the pathogenesis of Alzheimer’s disease [PDF]

, 2016
Alzheimer’s disease (AD) is a highly complex, progressive, age-related neurodegenerative human disease entity. The genetic basis of AD is strictly connected with occurrence of mutations in Amyloid Precursor (APP) gene on chromosome 21.
Diehl, J. Alan, Lewko, Dawid, Majsterek, Ireneusz, Nowak, Alicja, Pytel, Dariusz, Rozpędek, Wioletta   +5 more
core   +2 more sources

A reporter for amyloid precursor protein  -secretase activity in Drosophila [PDF]

Human Molecular Genetics, 2003
A key event in the pathogenesis of Alzheimer's disease (AD) is the deposition of senile plaques consisting largely of a peptide known as beta-amyloid (Abeta) that is derived from the amyloid precursor protein (APP). A proteolytic activity called gamma-secretase cleaves APP in the transmembrane domain and is required for Abeta generation. Aberrant gamma-
Guo, Ming, Hong, Elizabeth J., Fernandes, Jolene, Zipursky, S. Larry, Hay, Bruce A.   +4 more
openaire   +3 more sources

Probing Mechanisms and Therapeutic Potential of γ-Secretase in Alzheimer’s Disease

Molecules, 2021
The membrane-embedded γ-secretase complex carries out hydrolysis within the lipid bilayer in proteolyzing nearly 150 different membrane protein substrates.
Michael S. Wolfe
doaj   +1 more source

Calcium in the initiation, progression and as an effector of Alzheimer's disease pathology. [PDF]

, 2009
The cause(s) of sporadic Alzheimer's disease (sAD) are complex and currently poorly understood. They likely result from a combination of genetic, environmental, proteomic and lipidomic factors that crucially occur only in the aged brain.
Green, Kim N
core   +1 more source

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

Cell 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, Sabyashachi Mishra, K. Muruga Poopathi Raja, Michael Willem, Antonio Baici, Kai Simons, Oliver Brüstle, Philipp Koch, Christian Haass, Amedeo Caflisch, Lawrence Rajendran   +10 more
doaj   +1 more source

Alzheimer's Disease; Mechanism, Mutations, and Applications of Nano-Medicine

Frontiers in Bioscience-Landmark, 2023
Background: In the past 10 years, significant progress has been made in understanding the pathogenic chain of events that causes Alzheimer’s disease (AD).
Muhammad Maisam, Muhammad Tahir Khan, Madeeha Shahzad Lodhi, Kejie Mou, Zili Liu, Dongqing Wei   +5 more
doaj   +1 more source

BACE1 activity impairs neuronal glucose oxidation:rescue by beta-hydroxybutyrate and lipoic acid [PDF]

, 2015
Glucose hypometabolism and impaired mitochondrial function in neurons have been suggested to play early and perhaps causative roles in Alzheimer's disease (AD) pathogenesis. Activity of the aspartic acid protease, beta-site amyloid precursor protein (APP)
Arsenian, Bateman, Beal, Bielarczyk, Blass, Bogaert, Bosetti, Bouzier-Sore, Bubber, Butterworth, Casley, Casley, Caspersen, Coleman, Costantini, Danial, David L. Hamilton, DeKosky, DeKosky, Devi, Du, Fang, Forero, Fukumoto, Geula, Gibson, Giménez-Cassina, Guglielmotto, Gómez-Isla, Hager, Hamilton, Harada, Henderson, Henderson, Hirai, Holsinger, Huang, Hussain, Itoh, Jack, Jack, Jack, Jha, John A. Findlay, Johnson, Kankotia, Kawaja, Kim, Knopman, Ko, Korolainen, Lei, Li, Lustbader, Magistretti, Manczak, Martiskainen, Masdeu, Mastrogiacoma, Maurer, McKenna, Meakin, Michael L. J. Ashford, Mirshamsi, Mosconi, Mosconi, Mowrer, Mucke, Mullen, Nelson, Nilsen, Nunomura, O'Connor, Packer, Parker, Patel, Pereira, Perry, Phypers, Puglielli, Reger, Reiman, Sancheti, Shankar, Shearman, Sinha, Small, Sokoloff, Sorbi, Sowell, Swerdlow, Tyler, Vaishnavi, Vassar, Vassar, Velliquette, Vlassenko, von Kienlin, Wilkins, Wischmeyer, Wise, Xun, Yang, Yao, Yao, Zaidan, Zhang, Zhang, Zhao   +108 more
core   +6 more sources

Anti-Aβ drug screening platform using human iPS cell-derived neurons for the treatment of Alzheimer's disease. [PDF]

PLoS ONE, 2011
BackgroundAlzheimer's disease (AD) is a neurodegenerative disorder that causes progressive memory and cognitive decline during middle to late adult life.
Naoki Yahata, Masashi Asai, Shiho Kitaoka, Kazutoshi Takahashi, Isao Asaka, Hiroyuki Hioki, Takeshi Kaneko, Kei Maruyama, Takaomi C Saido, Tatsutoshi Nakahata, Takashi Asada, Shinya Yamanaka, Nobuhisa Iwata, Haruhisa Inoue   +13 more
doaj   +1 more source

Dieckol Ameliorates Aβ Production via PI3K/Akt/GSK-3β Regulated APP Processing in SweAPP N2a Cell

Marine Drugs, 2021
The proteolytic processing of amyloid precursor protein (APP) by β-secretase (BACE1) and γ-secretase releases amyloid-β peptide (Aβ), which deposits in amyloid plaques and contributes to the initial causative events of Alzheimer’s disease (AD).
Jeong-Hyun Yoon, Nayoung Lee, Kumju Youn, Mi Ra Jo, Hyeung-Rak Kim, Dong-Seok Lee, Chi-Tang Ho, Mira Jun   +7 more
doaj   +1 more source