Results 111 to 120 of about 1,107,303 (283)
Structural Polymorphism of polyG Inclusions Revealed by In Situ Cryo‐Electron Tomography
Correlative cryo‐electron tomography in primary cortical neurons and NIID mouse brain tissue reveals that polyG inclusions are interconnected ribbon‐like assemblies rather than canonical amyloid fibrils. Multiple compartment‐specific ribbon states show distinct 26S proteasome accessibility, while cytoplasmic ribbons contact and deform ER‐like ...
Yunwen Qian +12 more
wiley +1 more source
A Phosphorylation‐Induced Micellization Switch in the Low‐Complexity Domain of TDP‐43
Phosphorylation of TAR DNA‐binding protein's 43 kDa (TDP‐43) low‐complexity domain by casein kinase 1 delta (CK1δ) acts as a molecular switch, redirecting its self‐assembly from macroscopic phase separation toward finite‐sized, spherical block‐copolymer micelles of ∼30 nm.
Rodrigo F. Dillenburg +16 more
wiley +1 more source
Estudo bioquímico e comportamental em camundongos submetidos à infusão intracerebroventricular dos peptídeos beta-amilóide AB1-40 E AB25-35 e o papel neuroprotetor da atorvastatina [PDF]
Dissertação (mestrado) - Universidade Federal de Santa Catarina. Centro de Ciências Biológicas. Programa de Pós-Graduação em Neurociências.The accumulation and aggregation of beta-amyloid peptide (Aâ) in brain of patients with Alzheimer's disease results
Piermartiri, Tetsade Camboim Bizerra
core
In NIID, expanded NOTCH2NLC repeats give rise to nuclear polyG inclusions. Tracer‐guided in situ cryo‐electron tomography enables cross‐scale structural analysis from mouse brain to native neuronal nuclei, revealing dense‐core/peripheral‐halo inclusions built from compact polyG ribbons.
Hui Dong +13 more
wiley +1 more source
Inflammatory components in human Alzheimer's disease and after active amyloid-β42 immunization
Inflammatory processes are important in the pathogenesis of Alzheimer's disease and in response to amyloid-β immunotherapy. We investigated the expression of multiple inflammatory markers in the brains of 28 non-immunized patients with Alzheimer's ...
Cheaveau, M. +18 more
core +1 more source
Antigenic peptides Aβ42 and E7 self‐assemble into nanofibrils; APTES and TEOS induce SiO2 NP formation on these fibrils to form SiO2@fibril nanovaccines, which activate BMDCs in vitro. In vivo, SiO2@Aβ42 fibril nanovaccines alleviate AD symptoms and clear Aβ42 plaques in APP/PS1 mice, and SiO2@E7 fibril nanovaccines inhibit tumor growth and promote ...
Xuecheng Yang +6 more
wiley +1 more source
Accumulation of amyloid-beta (Aβ) in the brain has been explored as a primary cause of Alzheimer's Disease (AD). Better known as the amyloid hypothesis, it has been the main target of researchers vying to bring their therapeutic interventions to market ...
Chelsea Ann Stellick Bedrejo +6 more
doaj +1 more source
Therapeutic Gene Editing of APOE4 in Sporadic Alzheimer's Disease via Prime Editor 7
Prime Editor 7‐mediated conversion of APOE4 to APOE3 alleviates Alzheimer's disease‐associated pathology in AD mouse models and patient‐derived neurons and improves cognitive performance in vivo, supporting therapeutic genome editing as a promising strategy for APOE4‐associated neurodegeneration.
Yunkyung Kim +16 more
wiley +1 more source
Regulation of Mint1-dependent APP trafficking by N1-Src [PDF]
Alzheimer’s disease (AD) is a neurodegenerative disease characterised by the accumulation of Amyloid-beta (Aβ) plaques and neurofibrillary tangles. Aβ plaques form as a result of improper trafficking and processing of the Amyloid precursor protein (APP).
Black, Hannah Lucy
core +1 more source
A Unifying Thermodynamic Model for Phase Separation and Aging of Biopolymers
Phase separation and aging of intrinsically disordered proteins are placed in a unifying framework. A thermodynamically consistent time‐dependent version of associating‐polymer theory shows how the processes are intricately coupled. Assuming aging to occur through interacting sites resulting from reversible conformational transitions, the model ...
Jasper J. Michels +2 more
wiley +1 more source

