Results 61 to 70 of about 120,581 (311)

Carboranyl‐Curcuminoids for the Neutron Capture‐Based Treatment of Amyloid Aggregates in Alzheimer's Disease

open access: yesAdvanced Science, EarlyView.
The 10B‐enriched monocarbonyl analog of curcumin (BMAC) 10B‐9 enables site‐specific Boron Neutron Capture Therapy (BNCT) on amyloid‐β (Aβ) fibrils. Neutron irradiation induces histidine oxidation and fibril destabilization, as revealed by 1H‐NMR and FESEM analyses.
Sebastiano Micocci   +13 more
wiley   +1 more source

TRANSTHYRETIN POLYNEUROPATHY (CLINICAL CASE)

open access: yesМедицина в Кузбассе, 2023
Amyloidosis is a violation of protein metabolism, accompanied by the formation in tissues of a specific protein-polysaccharide complex (amyloid) of a fibrillar structure, characterized by a high orderliness of fibrils 5-10 nm thick due to the abundance ...
Наталья Викторовна Коробкова   +8 more
doaj  

Experimental approaches to study cerebral amyloidosis in a transgenic mouse model of Alzheimer's disease [PDF]

open access: yes, 2004
Misfolding, aggregation and the accumulation of proteins in the brain are common characteristics of diverse age-related neurodegenerative diseases. Each of these neurodegenerative diseases is associated with abnormalities in the folding of a different
Meyer-Lühmann, Melanie
core   +1 more source

Divergent Roles of mGlu2 and mGlu3 Receptors in Amyloid‐β Production and Cognitive Dysfunctions in Alzheimer's Disease

open access: yesAdvanced Science, EarlyView.
This study explores the opposing effects of the mGluR2 and mGluR3 receptors on amyloid precursor protein processing. mGluR2 promotes amyloidogenic cleavage, while mGluR3 favors non‐amyloidogenic pathways. Using a brain‐penetrant nanobody as a mGluR2 positive allosteric modulator, the study uncovers how its chronic activation aggravates amyloid‐β burden
Pierre‐André Lafon   +21 more
wiley   +1 more source

Identification of candidate substrates for ectodomain shedding by the metalloprotease-disintegrin ADAM8 [PDF]

open access: yes, 2006
ADAM proteases are type I transmembrane proteins with extracellular metalloprotease domains. As for most ADAM family members, ADAM8 (CD156a, MS2) is involved in ectodomain shedding of membrane proteins and is linked to inflammation and neurodegeneration.
Bartsch, Jörg W.   +15 more
core   +1 more source

Smart Nanotechnologies for Multimodal Neuromodulation and Brain Interfacing

open access: yesAdvanced Science, EarlyView.
Recent advances in smart nanotechnologies are expanding the toolbox for brain interfacing, from wireless neuromodulation and high‐resolution sensing to targeted delivery within the central nervous system. By combining responsive nanomaterials with bioinspired design, these platforms enable multimodal interactions with neurons and glia, while also ...
Tommaso Curiale   +6 more
wiley   +1 more source

Cholesterol-dependent amyloid β production: space for multifarious interactions between amyloid precursor protein, secretases, and cholesterol

open access: yesCell & Bioscience, 2023
Amyloid β is considered a key player in the development and progression of Alzheimer’s disease (AD). Many studies investigating the effect of statins on lowering cholesterol suggest that there may be a link between cholesterol levels and AD pathology ...
Vladimir Rudajev, Jiri Novotny
doaj   +1 more source

Initiation and spreading of Tau pathology. is β-Amyloid the only key? [PDF]

open access: yes, 2009
Neurodegenerative diseases associated with dementia affect 5-10 % of individuals over the age of 65 in the Western world and represent one of the main health-related socioeconomic burdens.
Clavaguera, Florence
core   +1 more source

Targeting PLD3 Reverses the Immunosuppressive Niche by Reprogramming Tumor‐Associated Macrophages and Potentiates Antitumor Immunity

open access: yesAdvanced Science, EarlyView.
PLD3 activates the lysosomal‐AKT‐NF‐κB axis to drive cellular senescence in macrophages, establishing an immunosuppressive TME by limiting the infiltration of cytotoxic T, NK, and NKT cells, which confers resistance to anti‐PD‐1 therapy. Abrine inhibits PLD3 expression, restoring antitumor immunity and synergizing with anti‐PD‐1 treatment.
Xingtu Qin   +11 more
wiley   +1 more source

TDP‐43 Aggregation: The Healthy‐Toxic Balance of the Prion‐Like Domain

open access: yesAdvanced Science, EarlyView.
TDP‐43 function relies on a delicate balance between reversible phase‐separated states and irreversible aggregation. Under physiological conditions, TDP‐43 forms dynamic droplets and oligomers that support normal cellular functions. In pathological contexts, this balance shifts toward aberrant aggregation, leading to toxic species.
Luca Zangrando   +2 more
wiley   +1 more source

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