A5039802209- Alzheimer's disease research and treatments
- Computational Drug Discovery Methods
- Cholinesterase and Neurodegenerative Diseases
- Neuroinflammation and Neurodegeneration Mechanisms
- Tryptophan and brain disorders
- Prion Diseases and Protein Misfolding
- Neuroscience and Neuropharmacology Research
- Medicinal Plants and Neuroprotection
- Dementia and Cognitive Impairment Research
- Cerebrospinal fluid and hydrocephalus
- Nuclear Receptors and Signaling
Yonsei University
2020-2024
Incheon National University
2024
Alzheimer's disease (AD), the most common cause of dementia, is a complex condition characterized by multiple pathophysiological mechanisms including amyloid-β (Aβ) plaque accumulation and neuroinflammation in brain. The current immunotherapy approaches, such as anti-Aβ monoclonal antibody (mAb) therapy, Aβ vaccines, adoptive regulatory T (Treg) cell transfer, target single mechanism, which may lead to unsatisfactory therapeutic efficacy. Furthermore, vaccines often induce helper 1 (Th1)...
Abstract Transgenic mouse models recapitulating Alzheimer’s disease (AD) pathology are pivotal in molecular studies and drug evaluation. In transgenic selectively expressing amyloid-β (Aβ), thioflavin S (ThS), a fluorescent dye with β-sheet binding properties, is widely employed to observe amyloid plaque accumulation. this study, we investigated the possibility that commonly used Aβ-expressing AD model mouse, 5XFAD, generates ThS-positive aggregates of structures addition Aβ fibrils. To test...
Alzheimer's disease (AD) is the most common type of dementia characterized by abnormal accumulation amyloid-β (Aβ) in brain. Aβ misfolding associated with neuroinflammation and synaptic dysfunction, leading to learning memory deficits. Therefore, production aggregation have been one popular drug targets for AD. Failures candidates regulating aforementioned cascade stimulated development immunotherapy agents clearance accumulated Here, we report that quinacrine, a blood-brain barrier...
Aggregation of misfolded amyloid-β (Aβ) and hyperphosphorylated tau proteins to plaques tangles, respectively, is the major drug target Alzheimer's disease (AD), as former an onset biomarker latter associated with neurodegeneration. Thus, we report a small molecule candidate, DN5355, dual-targeting function toward aggregates both Aβ tau. DN5355 was selected through series four screenings assessing 52 chemicals for their functions inhibit reverse aggregation by utilizing thioflavin T. When...
Comprehending early amyloidogenesis is essential for the development of effective therapeutic strategies. In tauopathies like Alzheimer’s disease (AD), abnormal accumulation tau protein initiated by pathological seeds. Mounting evidence implies that microtubule binding domain, consisting three to four repeats, plays a pivotal role in this process, yet exact region driving formation pathogenic species needs be further scrutinized. Here, we chemically synthesized individual repeats identify...
Comprehending early amyloidogenesis is essential for the development of effective therapeutic strategies. In tauopathies like Alzheimer’s disease (AD), abnormal accumulation tau protein initiated by pathological seeds. Mounting evidence implies that microtubule binding domain, consisting three to four repeats, plays a pivotal role in this process, yet exact region driving formation pathogenic species needs be further scrutinized. Here, we chemically synthesized individual repeats identify...
Abstract Alzheimer’s disease (AD) is a neurodegenerative characterized by the abnormal assembly of amyloid-β (Aβ) and tau aggregates in brain. When Aβ proteins misfold, progressive brain cell death, synaptic loss, atrophy, cognitive decline are observed. Here, we report that memory-enhancing botanical natural product mixture, HX106N, efficiently inhibits formation oligomers fibrils aggregation tau. HX106N mixture extract Dimocarpus longan , Liriope platyphylla Salvia miltiorrhiza Gastrodia...
Abstract Background Alzheimer’s disease (AD) is predominantly caused by the aggregation of amyloid‐β (Aβ) peptides into neurotoxic plaques. Current therapeutic approaches using monoclonal antibodies, like aducanumab and lecanemab, have shown promise in reversing Aβ aggregation. However, these treatments are expensive challenging to administer. Small molecules offer a more accessible alternative but face specificity hurdles. Our study explores library hybrid compounds, integrating structures...