Results 101 to 110 of about 14,023 (271)
Noninvasive imaging of amyloid‐beta and tau in rodent and nonhuman primate models
VIEW, Volume 7, Issue 1, February 2026.Imaging of amyloid‐beta plaque and tau accumulation in rodent and nonhuman primate model of Alzheimer's disease. Created in BioRender. Ni R. 2026. https://BioRender.com/a97h5ec Abstract Neurodegenerative diseases are characterized by the aberrant accumulation of protein aggregates.
Ruiqing Ni, Axel Rominger
wiley +1 more source
Secreted APP Regulates the Function of Full-Length APP in Neurite Outgrowth Through Interaction With Integrin Beta1 [PDF]
, 2011 Background: β-Amyloid precursor protein (APP) has been reported to play a role in the outgrowth of neurites from cultured neurons. Both cell-surface APP and its soluble, ectodomain cleavage product (APPs-α) have been implicated in regulating the length ...
Chang, Rui +4 more
core +1 more source
Molecular Neurodegeneration, 2006 Amyloid-β peptide (Aβ) accumulation in the brain is an early, toxic event in the pathogenesis of Alzheimer's disease (AD). Aβ is produced by proteolytic processing of a transmembrane protein, β-amyloid precursor protein (APP), by β- and γ-secretases ...
Cam Judy A, Bu Guojun
doaj +1 more source
Targeted Nanodelivery of WGX50 and Curcumin via Gold Nanoparticles for Alzheimer's Therapy
Journal of Cellular and Molecular Medicine, Volume 30, Issue 3, February 2026.ABSTRACT Alzheimer's disease (AD) is a progressive neurodegenerative disorder, posing a global health challenge. It affects millions of people, causing cognitive decline and a heavy burden on healthcare systems. Neuroinflammation is a key pathological feature of AD, often associated with the dysregulation of microRNAs such as hsa‐miR‐146a‐5p. WGX50 (N‐[
Madeeha Shahzad Lodhi +5 more
wiley +1 more source
BMC Cell Biology, 2011 Background The amyloid precursor protein (APP) is cleaved by β- and γ-secretases to generate toxic amyloid β (Aβ) peptides. Alternatively, α-secretases cleave APP within the Aβ domain, precluding Aβ formation and releasing the soluble ectodomain, sAPPα ...
Slack Barbara E +2 more
doaj +1 more source
Journal of Neurochemistry, Volume 170, Issue 2, February 2026.The interplay between the cholesterol metabolism and assembly of Aβ42 (Amyloid beta‐42) peptide in pathological aggregates is considered one of the major molecular mechanisms in the development of Alzheimer's disease (AD). Our combined studies revealed that Aβ42 was capable of removing cholesterol from the membrane at physiologically relevant low ...
Rishiram Baral +2 more
wiley +1 more source
Transmembrane segment proteases [PDF]
, 2018 Summary: Transmembrane segment proteases comprise a novel class of proteases that cleave substrates within hydrophobic membrane-spanning segments. They cleave in parts of proteins that upon first glance should be protected by the hydrophobic environment ...
Martoglio, B.
core
A resorcinarene for inhibition of Aβ fibrillation. [PDF]
, 2017 Amyloid-β peptides (Aβ) fibrillation is the hallmark of Alzheimer's disease (AD). However, it has been challenging to discover potent agents in order to inhibit Aβ fibrillation.
Han, Xu +8 more
core +1 more source
Cellular basis of Alzheimer′s disease
Annals of Indian Academy of Neurology, 2010 Alzheimer′s disease (AD) is the most common form of neurodegenerative disease. A characteristic feature of the disease is the presence of amyloid-β (Aβ) which either in its soluble oligomeric form or in the plaque-associated form is ...
Bali Jitin +5 more
doaj
USP10 in Neurological Disorders: Mechanistic Insights and Emerging Therapeutic Strategies
Annals of the New York Academy of Sciences, Volume 1556, Issue 1, February 2026.USP10 is a deubiquitinating enzyme that affects neurological diseases through multiple mechanisms, including the accumulation of toxic proteins, autophagy, and immune responses. In this review, we discuss the structure and characteristics of USP10 and summarize the role of USP10 in neurological disorders.
Celemuge +5 more
wiley +1 more source