{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T18:06:19Z","timestamp":1791223579076,"version":"4.1.0"},"reference-count":349,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2025,1,10]],"date-time":"2025-01-10T00:00:00Z","timestamp":1736467200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100002632","name":"Hallym University","doi-asserted-by":"publisher","award":["HRF-2023-03-001"],"award-info":[{"award-number":["HRF-2023-03-001"]}],"id":[{"id":"10.13039\/501100002632","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>Amyloid-\u03b2 peptide (A\u03b2) is a critical cause of Alzheimer\u2019s disease (AD). It is generated from amyloid precursor protein (APP) through cleavages by \u03b2-secretase and \u03b3-secretase. \u03b3-Secretase, which includes presenilin, is regulated by several stimuli. Tau protein has also been identified as a significant factor in AD. In particular, Tau phosphorylation is crucial for neuronal impairment, as phosphorylated Tau detaches from microtubules, leading to the formation of neurofibrillary tangles and the destabilization of the microtubule structure. This instability in microtubules damages axons and dendrites, resulting in neuronal impairment. Notably, A\u03b2 is linked to Tau phosphorylation. Another crucial factor in AD is neuroinflammation, primarily occurring in the microglia. Microglia possess several receptors that bind with A\u03b2, triggering the expression and release of an inflammatory factor, although their main physiological function is to phagocytose debris and pathogens in the brain. NF-\u03baB activation plays a major role in neuroinflammation. Additionally, the production of reactive oxygen species (ROS) in the microglia contributes to this neuroinflammation. In microglia, superoxide is produced through NADPH oxidase, specifically NOX2. Rho GTPases play an essential role in regulating various cellular processes, including cytoskeletal rearrangement, morphology changes, migration, and transcription. The typical function of Rho GTPases involves regulating actin filament formation. Neurons, with their complex processes and synapse connections, rely on cytoskeletal dynamics for structural support. Other brain cells, such as astrocytes, microglia, and oligodendrocytes, also depend on specific cytoskeletal structures to maintain their unique cellular architectures. Thus, the aberrant regulation of Rho GTPases activity can disrupt actin filaments, leading to altered cell morphology, including changes in neuronal processes and synapses, and potentially contributing to brain diseases such as AD.<\/jats:p>","DOI":"10.3390\/cells14020089","type":"journal-article","created":{"date-parts":[[2025,1,10]],"date-time":"2025-01-10T06:25:54Z","timestamp":1736490354000},"page":"89","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":29,"title":["Molecular Mechanisms of Alzheimer\u2019s Disease Induced by Amyloid-\u03b2 and Tau Phosphorylation Along with RhoA Activity: Perspective of RhoA\/Rho-Associated Protein Kinase Inhibitors for Neuronal Therapy"],"prefix":"10.3390","volume":"14","author":[{"given":"Eun Hee","family":"Ahn","sequence":"first","affiliation":[{"name":"Department of Physiology, Hallym University College of Medicine, Chuncheon 24252, Kangwon-do, Republic of Korea"},{"name":"Department of Neurology, Hallym University College of Medicine, Chuncheon 24252, Kangwon-do, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2323-4742","authenticated-orcid":false,"given":"Jae-Bong","family":"Park","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Hallym University College of Medicine, Chuncheon 24252, Kangwon-do, Republic of Korea"},{"name":"Institute of Cell Differentiation and Aging, Hallym University College of Medicine, Chuncheon 24252, Kangwon-do, Republic of Korea"},{"name":"ELMED Co., Hallym University College of Medicine, Chuncheon 24252, Kangwon-do, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,1,10]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"5481","DOI":"10.1038\/s41380-021-01249-0","article-title":"The Amyloid-\u03b2 Pathway in Alzheimer\u2019s Disease","volume":"26","author":"Hampel","year":"2021","journal-title":"Mol. 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