Results 41 to 50 of about 337,024 (290)

Interactions between amyloid, amyloid precursor protein, and mitochondria

open access: yesBiochemical Society Transactions, 2023
Mitochondrial dysfunction and Aβ accumulation are hallmarks of Alzheimer's disease (AD). Decades of research describe a relationship between mitochondrial function and Aβ production. Amyloid precursor protein (APP), of which Aβ is generated from, is found within mitochondria.
openaire   +2 more sources

FMRP mediates mGluR5-dependent translation of amyloid precursor protein. [PDF]

open access: yesPLoS Biology, 2007
Amyloid precursor protein (APP) facilitates synapse formation in the developing brain, while beta-amyloid (Abeta) accumulation, which is associated with Alzheimer disease, results in synaptic loss and impaired neurotransmission.
Cara J Westmark, James S Malter
doaj   +1 more source

The amyloid precursor protein is a conserved Wnt receptor

open access: yeseLife, 2021
The Amyloid Precursor Protein (APP) and its homologues are transmembrane proteins required for various aspects of neuronal development and activity, whose molecular function is unknown. Specifically, it is unclear whether APP acts as a receptor, and if so what its ligand(s) may be.
Tingting Zhang   +14 more
openaire   +6 more sources

Dual Action of Memantine in Alzheimer Disease: A Hypothesis

open access: yesTaiwanese Journal of Obstetrics & Gynecology, 2009
Objective: In this study, we proposed a hypothesis to explain the mechanisms of memantine action in treating Alzheimer disease (AD). Memantine may reduce the expression of amyloid precursor protein and tau protein, as well as acting as an antagonist of N-
Tzong-Yuan Wu, Chih-Ping Chen
doaj   +1 more source

Proteinopathy, oxidative stress and mitochondrial dysfunction: cross talk in alzheimer’s disease and parkinson’s disease [PDF]

open access: yes, 2017
Alzheimer's disease and Parkinson's disease are two common neurodegenerative diseases of the elderly people that have devastating effects in terms of morbidity and mortality.
Chakrabarti, S.   +3 more
core   +3 more sources

The alpha-synuclein 5'untranslated region targeted translation blockers: anti-alpha synuclein efficacy of cardiac glycosides and Posiphen [PDF]

open access: yes, 2011
Increased brain α-synuclein (SNCA) protein expression resulting from gene duplication and triplication can cause a familial form of Parkinson's disease (PD).
Bandyopadhyay, Sanghamitra   +9 more
core   +1 more source

Activation of Ras-ERK Signaling and GSK-3 by Amyloid Precursor Protein and Amyloid Beta Facilitates Neurodegeneration in Alzheimer’s Disease

open access: yeseNeuro, 2017
It is widely accepted that amyloid β (Aβ) generated from amyloid precursor protein (APP) oligomerizes and fibrillizes to form neuritic plaques in Alzheimer’s disease (AD), yet little is known about the contribution of APP to intracellular signaling ...
Lisa Kirouac   +3 more
semanticscholar   +1 more source

Amyloid Precursor-like Protein 1 Influences Endocytosis and Proteolytic Processing of the Amyloid Precursor Protein [PDF]

open access: yesJournal of Biological Chemistry, 2006
Ectodomain shedding of the amyloid precursor protein (APP) is a key regulatory step in the generation of the Alzheimer disease amyloid beta peptide (Abeta). The molecular mechanisms underlying the control of APP shedding remain little understood but are in part dependent on the low density lipoprotein receptor-related protein (LRP), which is involved ...
Neumann, Stephanie   +6 more
openaire   +3 more sources

Enzymatic Screening of β-Amyloid Precursor Protein-Based Substrates

open access: yesCompounds, 2023
We performed an enzymatic screening of synthetic peptides based on β-amyloid precursor protein substrates. The template peptide sequence was a decapeptide derived from our previous screening study, which determined several effective unnatural amino acids.
Reo Yamada   +5 more
doaj   +1 more source

Crystal structure of monomeric human β-2- microglobulin reveals clues to its amyloidogenic properties [PDF]

open access: yes, 2002
Dissociation of human β-2-microglobulin (β(2)m) from the heavy chain of the class I HLA complex is a critical first step in the formation of amyloid fibrils from this protein.
A. P. Kalverda   +31 more
core   +2 more sources

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